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Database: PDB
Entry: 6BD3
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Original site: 6BD3 
HEADER    TRANSFERASE                             21-OCT-17   6BD3              
TITLE     SACCHAROMYCES CEREVISIAE ACETOHYDROXYACID SYNTHASE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACETOHYDROXY-ACID SYNTHASE CATALYTIC SUBUNIT,ALS;           
COMPND   5 EC: 2.2.1.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: ILV2, SMR1, YMR108W, YM9718.07;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    AHAS, FAD, 2-HYDROXYETHYL-THDP, DIOXYGEN, TRANSFERASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.W.GUDDAT,T.LONHIENNE                                                
REVDAT   4   08-JAN-20 6BD3    1       REMARK                                   
REVDAT   3   22-MAY-19 6BD3    1       JRNL                                     
REVDAT   2   06-DEC-17 6BD3    1       REMARK                                   
REVDAT   1   08-NOV-17 6BD3    0                                                
SPRSDE     08-NOV-17 6BD3      5INV                                             
JRNL        AUTH   T.LONHIENNE,M.D.GARCIA,C.NOBLE,J.HARMER,J.A.FRASER,          
JRNL        AUTH 2 C.M.WILLIAMS,L.W.GUDDAT                                      
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURES OF THE ACETOHYDROXYACID   
JRNL        TITL 2 SYNTHASE-PYRUVATE COMPLEX PROVIDE NEW INSIGHTS INTO ITS      
JRNL        TITL 3 CATALYTIC MECHANISM                                          
JRNL        REF    CHEMISTRYSELECT                            2017              
JRNL        REFN                   ESSN 2365-6549                               
JRNL        DOI    10.1002/SLCT.201702128                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 86040                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999                            
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 47.3159 -  5.4936    0.99     6324   150  0.1748 0.1857        
REMARK   3     2  5.4936 -  4.3614    1.00     6118   147  0.1412 0.1739        
REMARK   3     3  4.3614 -  3.8103    1.00     6075   144  0.1362 0.1605        
REMARK   3     4  3.8103 -  3.4621    1.00     6041   143  0.1515 0.1668        
REMARK   3     5  3.4621 -  3.2140    1.00     6023   144  0.1572 0.2124        
REMARK   3     6  3.2140 -  3.0245    1.00     6008   143  0.1772 0.2061        
REMARK   3     7  3.0245 -  2.8731    1.00     5996   143  0.1871 0.2200        
REMARK   3     8  2.8731 -  2.7480    1.00     6000   142  0.1954 0.2389        
REMARK   3     9  2.7480 -  2.6423    1.00     5981   143  0.2021 0.2355        
REMARK   3    10  2.6423 -  2.5511    1.00     5974   142  0.2036 0.2513        
REMARK   3    11  2.5511 -  2.4713    1.00     5944   141  0.2143 0.2820        
REMARK   3    12  2.4713 -  2.4007    1.00     5949   142  0.2331 0.2472        
REMARK   3    13  2.4007 -  2.3375    1.00     5931   141  0.2339 0.2143        
REMARK   3    14  2.3375 -  2.2805    0.95     5677   134  0.2516 0.3148        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.950           
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      :  0.004           8665                                  
REMARK   3   ANGLE     :  0.842          11769                                  
REMARK   3   CHIRALITY :  0.054           1331                                  
REMARK   3   PLANARITY :  0.003           1508                                  
REMARK   3   DIHEDRAL  : 15.121           3169                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 298 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 212.8107 126.5900 205.1256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2369 T22:   0.3801                                     
REMARK   3      T33:   0.1982 T12:  -0.0579                                     
REMARK   3      T13:   0.0022 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9541 L22:   1.2514                                     
REMARK   3      L33:   0.9488 L12:   0.6305                                     
REMARK   3      L13:  -0.5805 L23:  -0.5901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1162 S12:  -0.1655 S13:   0.0331                       
REMARK   3      S21:   0.1651 S22:  -0.1820 S23:  -0.0815                       
REMARK   3      S31:  -0.0928 S32:   0.3680 S33:   0.0752                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 648 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 195.0215 102.6290 205.3618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3361 T22:   0.2781                                     
REMARK   3      T33:   0.3069 T12:  -0.0709                                     
REMARK   3      T13:   0.0048 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5254 L22:   1.0239                                     
REMARK   3      L33:   3.0101 L12:  -0.3338                                     
REMARK   3      L13:   0.1453 L23:  -1.4464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0415 S12:  -0.0353 S13:  -0.2446                       
REMARK   3      S21:  -0.1654 S22:   0.0462 S23:   0.1740                       
REMARK   3      S31:   0.3771 S32:  -0.1679 S33:  -0.0831                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 163 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 175.1052 133.4131 200.5843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2180 T22:   0.5005                                     
REMARK   3      T33:   0.3315 T12:  -0.0755                                     
REMARK   3      T13:   0.0059 T23:  -0.0781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0108 L22:   1.6393                                     
REMARK   3      L33:   3.2606 L12:  -0.4927                                     
REMARK   3      L13:  -1.8014 L23:  -0.4166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0634 S12:   0.1323 S13:  -0.0077                       
REMARK   3      S21:   0.0746 S22:  -0.1562 S23:   0.4338                       
REMARK   3      S31:   0.0541 S32:  -0.6344 S33:   0.1164                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 183.7855 145.2442 206.2879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2961 T22:   0.3014                                     
REMARK   3      T33:   0.3325 T12:  -0.0016                                     
REMARK   3      T13:   0.0352 T23:  -0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8734 L22:   2.2324                                     
REMARK   3      L33:   2.7074 L12:  -0.0489                                     
REMARK   3      L13:  -0.6634 L23:   0.3926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1381 S12:  -0.2083 S13:   0.4284                       
REMARK   3      S21:   0.1853 S22:  -0.0548 S23:   0.1210                       
REMARK   3      S31:  -0.5236 S32:  -0.1799 S33:  -0.0466                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 316 THROUGH 450 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 195.3514 164.9696 189.0559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3244 T22:   0.6823                                     
REMARK   3      T33:   1.0039 T12:  -0.2198                                     
REMARK   3      T13:   0.3051 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6962 L22:   3.3532                                     
REMARK   3      L33:   3.1032 L12:   0.6342                                     
REMARK   3      L13:  -1.1559 L23:   0.7020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5256 S12:   0.0787 S13:   0.9709                       
REMARK   3      S21:  -0.5357 S22:   0.2471 S23:  -0.5853                       
REMARK   3      S31:  -2.2787 S32:   0.7239 S33:  -0.6203                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 451 THROUGH 498 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 196.7134 148.5438 170.7526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4106 T22:   0.7054                                     
REMARK   3      T33:   0.4224 T12:  -0.0410                                     
REMARK   3      T13:   0.1010 T23:   0.1647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2900 L22:   4.7351                                     
REMARK   3      L33:   1.4111 L12:   0.4039                                     
REMARK   3      L13:   0.2209 L23:   0.3510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2230 S12:   0.4222 S13:   0.2566                       
REMARK   3      S21:  -0.6290 S22:  -0.1937 S23:  -0.6922                       
REMARK   3      S31:  -0.4700 S32:   0.5836 S33:  -0.1660                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 499 THROUGH 621 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 194.7133 135.3633 179.8302              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1995 T22:   0.4406                                     
REMARK   3      T33:   0.2267 T12:   0.0231                                     
REMARK   3      T13:  -0.0096 T23:   0.0395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3490 L22:   3.5221                                     
REMARK   3      L33:   2.9033 L12:   0.2311                                     
REMARK   3      L13:  -0.1112 L23:  -0.1027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:   0.3082 S13:   0.1194                       
REMARK   3      S21:  -0.1425 S22:  -0.0618 S23:  -0.3340                       
REMARK   3      S31:   0.0003 S32:   0.2790 S33:  -0.0281                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 622 THROUGH 649 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 192.2677 134.5798 167.8020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2719 T22:   0.5392                                     
REMARK   3      T33:   0.2234 T12:  -0.0055                                     
REMARK   3      T13:  -0.0260 T23:   0.0626                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3594 L22:   8.4808                                     
REMARK   3      L33:   4.4275 L12:  -1.2711                                     
REMARK   3      L13:  -3.7660 L23:  -1.3092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1803 S12:   0.4440 S13:   0.1017                       
REMARK   3      S21:  -0.3191 S22:  -0.1865 S23:  -0.5036                       
REMARK   3      S31:   0.0136 S32:   0.0449 S33:  -0.0786                       
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 6BD3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230606.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-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   : 86039                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
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, 0.7 MM BSM AND 4.5 MM DTT.           
REMARK 280  CRYSTALS WERE OBTAINED MY MIXING EQUAL VOLUMES (300 NL) OF WELL     
REMARK 280  SOLUTION (1.6M NA/K HYDROGEN PHOSPHATE PH 6.5) AND COMPLEX          
REMARK 280  SOLUTION. CRYSTALS WERE SOAKED WITH PYRUVATE (PYRUVATE POWDER       
REMARK 280  ADDED TO THE DROP) FOR THREE WEEKS, PH 5.8, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
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       47.94900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.00050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.38300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.00050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.94900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.38300            
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: 11590 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ASN A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     GLN A   281                                                      
REMARK 465     GLU A   579                                                      
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     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    83                                                      
REMARK 465     ASN B   271                                                      
REMARK 465     ALA B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ASN B   274                                                      
REMARK 465     TYR B   591                                                      
REMARK 465     GLU B   592                                                      
REMARK 465     HIS B   593                                                      
REMARK 465     ARG B   594                                                      
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     LYS B 648    CG   CD   CE   NZ                                   
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    LYS B   453     N    LYS B   455              2.12            
REMARK 500   OG1  THR A   162     O1   OXY A   705              2.17            
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    GLN A 202     -121.68     54.60                                   
REMARK 500    GLU A 203      126.79     56.25                                   
REMARK 500    ASP A 350     -149.05     63.70                                   
REMARK 500    MET A 463       92.85    -55.61                                   
REMARK 500    ASN A 577       64.84   -108.06                                   
REMARK 500    ALA B 299       78.12     56.22                                   
REMARK 500    LYS B 300      -68.61   -100.73                                   
REMARK 500    ASP B 350     -160.59     59.88                                   
REMARK 500    HIS B 355       13.64   -142.20                                   
REMARK 500    PHE B 377       77.00     50.93                                   
REMARK 500    LYS B 387      -98.29    -64.21                                   
REMARK 500    ALA B 396       24.96    -78.46                                   
REMARK 500    ALA B 397       36.75   -158.75                                   
REMARK 500    GLU B 398      -12.73   -162.08                                   
REMARK 500    VAL B 416      -50.73   -129.37                                   
REMARK 500    LYS B 437       20.81    -75.94                                   
REMARK 500    PRO B 440       91.20    -56.81                                   
REMARK 500    ARG B 444       22.27   -163.78                                   
REMARK 500    SER B 445      -25.25    -34.63                                   
REMARK 500    PHE B 448       51.85    -69.01                                   
REMARK 500    ALA B 449      -67.36   -151.77                                   
REMARK 500    LYS B 453      -90.05    -70.29                                   
REMARK 500    TRP B 454       15.19     14.18                                   
REMARK 500    LYS B 455       58.85    177.86                                   
REMARK 500    LYS B 456     -138.68     56.20                                   
REMARK 500    TYR B 458      111.46     55.02                                   
REMARK 500    PRO B 459      -85.55   -108.19                                   
REMARK 500    TYR B 460       45.81   -159.99                                   
REMARK 500    MET B 463       99.62    -66.43                                   
REMARK 500    PRO B 467      124.93    -33.64                                   
REMARK 500    THR B 598       88.15     66.70                                   
REMARK 500    LYS B 648      -70.94    -55.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 701   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 343   OE1                                                    
REMARK 620 2 GLN A 506   O   159.2                                              
REMARK 620 3 TRP A 508   O    79.4  90.6                                        
REMARK 620 4 HOH A 809   O   110.7  80.8 169.4                                  
REMARK 620 5 HOH A 893   O    82.8  82.1 104.4  80.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 550   OD1                                                    
REMARK 620 2 ASN A 577   OD1  86.4                                              
REMARK 620 3 TPP A 703   O1A  97.4 167.9                                        
REMARK 620 4 TPP A 703   O1B 169.4  97.4  80.9                                  
REMARK 620 5 HOH A 834   O    92.3  91.4  99.9  77.7                            
REMARK 620 6 HOH A 891   O    91.3  84.9  83.5  99.0 174.7                      
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 343   OE1                                                    
REMARK 620 2 ASP B 350   OD2  79.0                                              
REMARK 620 3 GLN B 506   O   163.1 113.1                                        
REMARK 620 4 TRP B 508   O    80.5 154.6  90.3                                  
REMARK 620 5 HOH B 825   O    85.3  86.7  83.7 106.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 550   OD1                                                    
REMARK 620 2 ASN B 577   OD1  81.7                                              
REMARK 620 3 HTL B 703   O23 150.0  99.0                                        
REMARK 620 4 HOH B 808   O    76.6  82.0  73.7                                  
REMARK 620 5 HOH B 864   O   103.1  93.8 106.8 175.8                            
REMARK 620 6 HTL B 703   O12  88.6 165.9  84.3  85.8  98.4                      
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 MG A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY 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 CO2 A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 701                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HTL B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 712                 
DBREF  6BD3 A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  6BD3 B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 6BD3 MET A   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER A   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER A   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY A   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LEU A   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 VAL A   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PRO A   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ARG A   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY A   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER A   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY A   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET A   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS A   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLU A   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 THR A   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA A   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA A   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA A   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS A   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PHE A   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLU A   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ARG A   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLN A   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS A   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET A   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER A   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PRO A   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LEU A   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY A   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 THR A   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP A   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS A   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA A   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET A   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY A   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER A   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET B   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER B   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER B   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY B   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LEU B   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 VAL B   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PRO B   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ARG B   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY B   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER B   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY B   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET B   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS B   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLU B   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 THR B   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA B   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA B   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA B   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS B   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PHE B   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLU B   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ARG B   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLN B   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 HIS B   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET B   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 SER B   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 PRO B   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LEU B   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY B   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 THR B   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ASP B   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 LYS B   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 ALA B   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 MET B   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 GLY B   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD3 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     MG  A 702       1                                                       
HET    TPP  A 703      26                                                       
HET    OXY  A 704       2                                                       
HET    OXY  A 705       2                                                       
HET    CO2  A 706       3                                                       
HET    FAD  A 707      53                                                       
HET      K  B 701       1                                                       
HET     MG  B 702       1                                                       
HET    HTL  B 703      29                                                       
HET    OXY  B 704       2                                                       
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    PO4  B 710       5                                                       
HET    FAD  B 711      53                                                       
HET    ACT  B 712       4                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETNAM     OXY OXYGEN MOLECULE                                                  
HETNAM     CO2 CARBON DIOXIDE                                                   
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     HTL 2-ACETYL-THIAMINE DIPHOSPHATE                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ACT ACETATE ION                                                      
HETSYN     HTL 2-ACETYL-3-[(4-AMINO-2-METHYL-5-PYRIMIDINYL)METHYL]-4-           
HETSYN   2 HTL  METHYL-5-(4,6,6-TRIHYDROXY-3,5-DIOXA-4,6-DIPHOSPHAHEX-          
HETSYN   3 HTL  1-YL)THIAZOLIUM INNER SALT P,P'-DIOXIDE                         
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  TPP    C12 H19 N4 O7 P2 S 1+                                        
FORMUL   6  OXY    8(O2)                                                        
FORMUL   8  CO2    C O2                                                         
FORMUL   9  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  12  HTL    C14 H21 N4 O8 P2 S 1+                                        
FORMUL  19  PO4    O4 P 3-                                                      
FORMUL  21  ACT    C2 H3 O2 1-                                                  
FORMUL  22  HOH   *320(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  ASN A  127  1                                  10    
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 GLU A  283  ALA A  299  1                                  17    
HELIX   15 AB6 ALA A  308  HIS A  313  5                                   6    
HELIX   16 AB7 ASP A  315  ALA A  327  1                                  13    
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 LYS B  265  THR B  267  5                                   3    
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  LEU B  362  1                                   6    
HELIX   52 AF7 ALA B  389  ARG B  394  1                                   6    
HELIX   53 AF8 ALA B  395  GLU B  398  5                                   4    
HELIX   54 AF9 SER B  409  ILE B  413  5                                   5    
HELIX   55 AG1 ASP B  426  SER B  436  1                                  11    
HELIX   56 AG2 GLU B  446  TRP B  454  1                                   9    
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 GLU B  559  GLY B  567  1                                   9    
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  VAL A 373   N  TYR A 305           
SHEET    5 AA3 6 GLY A 402  GLU A 407  1  O  PHE A 406   N  ALA A 372           
SHEET    6 AA3 6 ILE A 421  GLU A 424  1  O  ILE A 421   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  LEU A 641   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  LEU B 304   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  GLY B 402   N  ILE B 370           
SHEET    6 AA7 6 ILE B 421  GLU B 424  1  O  ILE B 421   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 545   N  ILE B 492           
SHEET    4 AA8 6 LYS B 571  ASN B 576  1  O  LYS B 571   N  ASP B 546           
SHEET    5 AA8 6 VAL B 639  GLU B 644  1  O  LEU B 641   N  ILE B 572           
SHEET    6 AA8 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  GLU B 642           
SHEET    1 AA9 2 VAL B 583  THR B 584  0                                        
SHEET    2 AA9 2 SER B 596  HIS B 597 -1  O  HIS B 597   N  VAL B 583           
LINK         OE1 GLN A 343                 K     K A 701     1555   1555  2.87  
LINK         O   GLN A 506                 K     K A 701     1555   1555  2.74  
LINK         O   TRP A 508                 K     K A 701     1555   1555  2.75  
LINK         OD1 ASP A 550                MG    MG A 702     1555   1555  2.15  
LINK         OD1 ASN A 577                MG    MG A 702     1555   1555  2.35  
LINK         OE1 GLN B 343                 K     K B 701     1555   1555  2.89  
LINK         OD2 ASP B 350                 K     K B 701     1555   1555  3.41  
LINK         O   GLN B 506                 K     K B 701     1555   1555  2.85  
LINK         O   TRP B 508                 K     K B 701     1555   1555  2.74  
LINK         OD1 ASP B 550                MG    MG B 702     1555   1555  2.11  
LINK         OD1 ASN B 577                MG    MG B 702     1555   1555  2.10  
LINK         K     K A 701                 O   HOH A 809     1555   1555  2.94  
LINK         K     K A 701                 O   HOH A 893     1555   1555  2.77  
LINK        MG    MG A 702                 O1A TPP A 703     1555   1555  2.09  
LINK        MG    MG A 702                 O1B TPP A 703     1555   1555  2.14  
LINK        MG    MG A 702                 O   HOH A 834     1555   1555  2.07  
LINK        MG    MG A 702                 O   HOH A 891     1555   1555  2.10  
LINK         K     K B 701                 O   HOH B 825     1555   1555  2.83  
LINK        MG    MG B 702                 O23 HTL B 703     1555   1555  1.84  
LINK        MG    MG B 702                 O   HOH B 808     1555   1555  2.26  
LINK        MG    MG B 702                 O   HOH B 864     1555   1555  2.15  
LINK        MG    MG B 702                 O12 HTL B 703     1555   1555  1.96  
CISPEP   1 PHE B  388    ALA B  389          0        -5.62                     
CISPEP   2 LYS B  455    LYS B  456          0        -2.78                     
SITE     1 AC1  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC1  6 HOH A 809  HOH A 893                                          
SITE     1 AC2  5 ASP A 550  ASN A 577  TPP A 703  HOH A 834                    
SITE     2 AC2  5 HOH A 891                                                     
SITE     1 AC3 20 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC3 20 GLY A 523  MET A 525  ASP A 550  ALA A 551                    
SITE     3 AC3 20 SER A 552  ASN A 577   MG A 702  HOH A 834                    
SITE     4 AC3 20 HOH A 891  HOH A 948  PRO B 114  GLU B 139                    
SITE     5 AC3 20 PRO B 165  ASN B 169  GLN B 202  ACT B 712                    
SITE     1 AC4  6 ALA A 551  GLN A 600  HOH A 811  HOH A 833                    
SITE     2 AC4  6 TYR B 113  LYS B 137                                          
SITE     1 AC5  8 GLY A 115  GLY A 116  ALA A 117  THR A 162                    
SITE     2 AC5  8 SER A 163  GLN A 202  CO2 A 706  HOH A 939                    
SITE     1 AC6  5 GLY A 116  OXY A 705  HOH A 939  HTL B 703                    
SITE     2 AC6  5 OXY B 704                                                     
SITE     1 AC7 29 ARG A 241  GLY A 307  ALA A 308  GLY A 309                    
SITE     2 AC7 29 ASN A 312  THR A 334  LEU A 335  GLN A 336                    
SITE     3 AC7 29 LEU A 352  GLY A 353  MET A 354  HIS A 355                    
SITE     4 AC7 29 GLY A 374  ALA A 375  ARG A 376  ASP A 378                    
SITE     5 AC7 29 ARG A 380  VAL A 381  GLU A 407  VAL A 408                    
SITE     6 AC7 29 ASN A 412  GLY A 425  ASP A 426  ALA A 427                    
SITE     7 AC7 29 HOH A 817  HOH A 829  HOH A 914  HOH A 938                    
SITE     8 AC7 29 PHE B 201                                                     
SITE     1 AC8  5 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC8  5 HOH B 825                                                     
SITE     1 AC9  5 ASP B 550  ASN B 577  HTL B 703  HOH B 808                    
SITE     2 AC9  5 HOH B 864                                                     
SITE     1 AD1 21 TYR A 113  PRO A 114  GLU A 139  PRO A 165                    
SITE     2 AD1 21 ASN A 169  GLN A 202  CO2 A 706  VAL B 497                    
SITE     3 AD1 21 GLN B 499  HIS B 500  GLY B 523  MET B 525                    
SITE     4 AD1 21 GLY B 549  ASP B 550  ALA B 551  SER B 552                    
SITE     5 AD1 21 ASN B 577   MG B 702  OXY B 704  OXY B 708                    
SITE     6 AD1 21 HOH B 808                                                     
SITE     1 AD2  3 CO2 A 706  MET B 582  HTL B 703                               
SITE     1 AD3  4 GLU B 578  GLN B 580  HIS B 599  GLN B 600                    
SITE     1 AD4  3 GLN A 600  TYR B 113  HOH B 885                               
SITE     1 AD5  4 GLU B 578  GLN B 600  LEU B 601  ASN B 602                    
SITE     1 AD6  4 GLN B 499  MET B 582  HTL B 703  HOH B 864                    
SITE     1 AD7  7 GLY B 115  GLY B 116  ALA B 117  THR B 162                    
SITE     2 AD7  7 SER B 163  GLN B 202  ACT B 712                               
SITE     1 AD8  5 HIS A 126  GLU B 541  HIS B 597  THR B 598                    
SITE     2 AD8  5 HIS B 599                                                     
SITE     1 AD9 31 PHE A 201  ARG B 241  GLY B 307  ALA B 308                    
SITE     2 AD9 31 GLY B 309  ASN B 312  THR B 334  LEU B 335                    
SITE     3 AD9 31 LEU B 352  MET B 354  HIS B 355  GLY B 374                    
SITE     4 AD9 31 ALA B 375  ARG B 376  ASP B 378  ARG B 380                    
SITE     5 AD9 31 VAL B 381  GLU B 407  VAL B 408  ASN B 412                    
SITE     6 AD9 31 GLY B 425  ASP B 426  ALA B 427  GLN B 501                    
SITE     7 AD9 31 MET B 502  GLY B 520  GLY B 521  HOH B 820                    
SITE     8 AD9 31 HOH B 844  HOH B 852  HOH B 876                               
SITE     1 AE1  5 TPP A 703  GLY B 116  GLN B 202  OXY B 709                    
SITE     2 AE1  5 HOH B 847                                                     
CRYST1   95.898  108.766  180.001  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      0.010428  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009194  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005556        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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