GenomeNet

Database: PDB
Entry: 6BD9
LinkDB: 6BD9
Original site: 6BD9 
HEADER    TRANSFERASE                             22-OCT-17   6BD9              
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                                         
KEYWDS    AHAS, PYRUVATE, FAD, DIOXYGEN, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.W.GUDDAT,T.LONHIENNE                                                
REVDAT   4   08-JAN-20 6BD9    1       REMARK                                   
REVDAT   3   22-MAY-19 6BD9    1       JRNL                                     
REVDAT   2   06-DEC-17 6BD9    1       REMARK                                   
REVDAT   1   08-NOV-17 6BD9    0                                                
SPRSDE     08-NOV-17 6BD9      5INU                                             
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.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 127477                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.570                           
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 29.9326 -  4.7701    1.00     9826   155  0.1436 0.1504        
REMARK   3     2  4.7701 -  3.7886    1.00     9532   153  0.1232 0.1377        
REMARK   3     3  3.7886 -  3.3104    1.00     9456   151  0.1435 0.1776        
REMARK   3     4  3.3104 -  3.0080    1.00     9396   149  0.1630 0.2181        
REMARK   3     5  3.0080 -  2.7926    0.99     9364   150  0.1749 0.1990        
REMARK   3     6  2.7926 -  2.6281    0.98     9211   146  0.1694 0.1773        
REMARK   3     7  2.6281 -  2.4965    0.97     9060   144  0.1629 0.1689        
REMARK   3     8  2.4965 -  2.3879    0.95     8885   143  0.1762 0.2123        
REMARK   3     9  2.3879 -  2.2960    0.93     8638   137  0.1759 0.2007        
REMARK   3    10  2.2960 -  2.2168    0.91     8493   135  0.1795 0.2002        
REMARK   3    11  2.2168 -  2.1475    0.91     8479   135  0.1874 0.2012        
REMARK   3    12  2.1475 -  2.0861    0.91     8439   135  0.2090 0.2725        
REMARK   3    13  2.0861 -  2.0312    0.90     8425   135  0.2280 0.2509        
REMARK   3    14  2.0312 -  1.9817    0.90     8274   131  0.2392 0.2462        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.980           
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      :  0.019           8814                                  
REMARK   3   ANGLE     :  1.745          11976                                  
REMARK   3   CHIRALITY :  0.103           1347                                  
REMARK   3   PLANARITY :  0.009           1543                                  
REMARK   3   DIHEDRAL  : 17.578           3251                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 271 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 213.5920 131.4064  23.0631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1447 T22:   0.2093                                     
REMARK   3      T33:   0.1542 T12:  -0.0265                                     
REMARK   3      T13:  -0.0133 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3855 L22:   0.9892                                     
REMARK   3      L33:   1.4377 L12:   0.7032                                     
REMARK   3      L13:  -0.5448 L23:   0.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0855 S12:  -0.1477 S13:   0.0536                       
REMARK   3      S21:   0.1104 S22:  -0.1070 S23:  -0.0955                       
REMARK   3      S31:  -0.0324 S32:   0.3108 S33:   0.0149                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 648 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 195.7934 105.5469  27.0341              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2283 T22:   0.1624                                     
REMARK   3      T33:   0.2279 T12:  -0.0450                                     
REMARK   3      T13:  -0.0029 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3917 L22:   1.0323                                     
REMARK   3      L33:   2.4516 L12:  -0.2886                                     
REMARK   3      L13:   0.1622 L23:  -1.3484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0227 S12:  -0.0504 S13:  -0.1731                       
REMARK   3      S21:  -0.1102 S22:   0.0533 S23:   0.1547                       
REMARK   3      S31:   0.2721 S32:  -0.1398 S33:  -0.0490                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 255 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 180.6049 137.7431  25.1943              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1352 T22:   0.2082                                     
REMARK   3      T33:   0.1901 T12:  -0.0229                                     
REMARK   3      T13:   0.0174 T23:  -0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6006 L22:   1.1254                                     
REMARK   3      L33:   1.9575 L12:   0.2034                                     
REMARK   3      L13:  -0.3905 L23:   0.2921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0328 S12:  -0.0432 S13:   0.0343                       
REMARK   3      S21:   0.0644 S22:  -0.0772 S23:   0.2256                       
REMARK   3      S31:   0.0065 S32:  -0.3444 S33:   0.0330                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 181.7675 163.7601  22.7023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9374 T22:   0.3639                                     
REMARK   3      T33:   0.6935 T12:   0.0358                                     
REMARK   3      T13:   0.1222 T23:  -0.0429                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4293 L22:   0.6437                                     
REMARK   3      L33:   2.2702 L12:  -0.6630                                     
REMARK   3      L13:  -0.5487 L23:   0.7541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4172 S12:  -0.0716 S13:   0.5911                       
REMARK   3      S21:   0.0550 S22:  -0.1224 S23:  -0.2062                       
REMARK   3      S31:  -1.5291 S32:  -0.1976 S33:  -0.1588                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 316 THROUGH 472 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 197.2477 165.9229   5.5408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3720 T22:   0.5203                                     
REMARK   3      T33:   0.8045 T12:  -0.3099                                     
REMARK   3      T13:   0.3421 T23:   0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6273 L22:   2.6794                                     
REMARK   3      L33:   2.8183 L12:  -0.0673                                     
REMARK   3      L13:  -0.0930 L23:   0.7599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5115 S12:   0.0051 S13:   0.7845                       
REMARK   3      S21:  -0.8902 S22:   0.3298 S23:  -0.4557                       
REMARK   3      S31:  -2.4915 S32:   1.0928 S33:  -0.3419                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 473 THROUGH 646 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 194.2711 139.4549  -2.9714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1456 T22:   0.2725                                     
REMARK   3      T33:   0.1832 T12:  -0.0040                                     
REMARK   3      T13:   0.0117 T23:   0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0533 L22:   1.7051                                     
REMARK   3      L33:   2.4187 L12:  -0.1852                                     
REMARK   3      L13:   0.3795 L23:  -0.4389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:   0.3131 S13:   0.1706                       
REMARK   3      S21:  -0.1458 S22:  -0.1027 S23:  -0.2091                       
REMARK   3      S31:  -0.0767 S32:   0.2804 S33:   0.0008                       
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 6BD9 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_1000230607.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-15                          
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   : 127729                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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   (%): 65.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56                     
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 THEN SOAKED WITH PYRUVATE (ADDED AS         
REMARK 280  POWDER IN THE DROP) FOR 2 HOURS, 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       48.01200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.12200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.48350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.12200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.01200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.48350            
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: 12510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ARG A   279                                                      
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     LYS B   647                                                      
REMARK 465     LYS B   648                                                      
REMARK 465     VAL B   649                                                      
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 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   OD1  ASN B   297     N    PHE B   439              1.95            
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    PRO A 269      129.28    -37.27                                   
REMARK 500    ASP A 350     -151.94     69.37                                   
REMARK 500    ARG A 400       13.54   -140.36                                   
REMARK 500    ASN B 127       49.26   -100.57                                   
REMARK 500    SER B 270     -126.44    -76.44                                   
REMARK 500    ASN B 271      121.08   -170.54                                   
REMARK 500    ALA B 272      -98.77    -67.65                                   
REMARK 500    LEU B 273     -108.35    -82.31                                   
REMARK 500    ALA B 292      -54.12     65.33                                   
REMARK 500    ALA B 299     -151.57     65.06                                   
REMARK 500    LYS B 300     -127.75    121.76                                   
REMARK 500    LYS B 301       75.41   -110.94                                   
REMARK 500    GLN B 328       79.73     39.07                                   
REMARK 500    ASP B 350     -147.69     61.25                                   
REMARK 500    VAL B 364     -119.48    -76.23                                   
REMARK 500    GLN B 365      110.56    -19.21                                   
REMARK 500    ASN B 366       26.89     88.06                                   
REMARK 500    ALA B 367     -105.69    -59.77                                   
REMARK 500    ASP B 368      -77.04    141.04                                   
REMARK 500    ARG B 380       -8.62    -53.22                                   
REMARK 500    ASN B 384       15.32    100.74                                   
REMARK 500    ILE B 385      -96.10    -31.04                                   
REMARK 500    SER B 386      -37.70    -37.48                                   
REMARK 500    PRO B 390      -37.73    -39.12                                   
REMARK 500    GLU B 398        6.39    -65.06                                   
REMARK 500    MET B 435      -76.70    -45.70                                   
REMARK 500    LYS B 437        9.43    -59.94                                   
REMARK 500    PRO B 440      152.40    -42.80                                   
REMARK 500    ARG B 444       51.10   -141.90                                   
REMARK 500    ASN B 452       17.42    -61.43                                   
REMARK 500    PRO B 467      116.79    -35.04                                   
REMARK 500    PHE B 590       37.02    -80.53                                   
REMARK 500    TYR B 591        2.87     43.68                                   
REMARK 500    THR B 598       86.64     69.13                                   
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   159.4                                              
REMARK 620 3 TRP A 508   O    84.9  90.3                                        
REMARK 620 4 HOH A 836   O   104.8  82.6 168.6                                  
REMARK 620 5 HOH A1078   O    93.3 106.4  86.3  87.3                            
REMARK 620 6 HOH A 970   O    81.1  80.9 105.6  82.0 166.2                      
REMARK 620 N                    1     2     3     4     5                       
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  87.3                                              
REMARK 620 3 TPP A 704   O1A  85.5 172.8                                        
REMARK 620 4 TPP A 704   O1B 158.7  95.3  91.3                                  
REMARK 620 5 HOH A 864   O    78.9  87.2  91.3  80.1                            
REMARK 620 6 HOH A1013   O    95.8  87.5  93.4 105.5 172.6                      
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 GLN B 506   O   162.9                                              
REMARK 620 3 TRP B 508   O    86.3  89.4                                        
REMARK 620 4 HOH B 937   O    87.4 108.9  86.7                                  
REMARK 620 5 HOH B 884   O    78.8  86.3 104.9 161.3                            
REMARK 620 6 HOH B 801   O   101.0  84.4 172.1  90.7  79.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 703  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 550   OD1                                                    
REMARK 620 2 ASN B 577   OD1  85.4                                              
REMARK 620 3 HOH B 877   O    83.0  84.3                                        
REMARK 620 4 TPP B 704   O2B 163.8  93.1  80.8                                  
REMARK 620 5 HOH B 981   O    95.0  90.3 174.4 101.2                            
REMARK 620 6 TPP B 704   O1A  89.9 175.1  93.8  91.0  91.5                      
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 FAD A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PYR A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PYR A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 701                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PYR B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PYR B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 713                 
DBREF  6BD9 A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  6BD9 B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 6BD9 MET A   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER A   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER A   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY A   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LEU A   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 VAL A   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PRO A   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ARG A   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY A   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER A   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY A   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET A   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS A   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLU A   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 THR A   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA A   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA A   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA A   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS A   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PHE A   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLU A   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ARG A   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLN A   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS A   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET A   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER A   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PRO A   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LEU A   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY A   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 THR A   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP A   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS A   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA A   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET A   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY A   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER A   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET B   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER B   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER B   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY B   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LEU B   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 VAL B   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PRO B   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ARG B   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY B   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER B   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY B   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET B   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS B   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLU B   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 THR B   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA B   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA B   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA B   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS B   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PHE B   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLU B   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ARG B   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLN B   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 HIS B   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET B   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 SER B   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 PRO B   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LEU B   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY B   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 THR B   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ASP B   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 LYS B   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 ALA B   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 MET B   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 GLY B   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 6BD9 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    FAD  A 703      53                                                       
HET    TPP  A 704      26                                                       
HET    PYR  A 705       6                                                       
HET    PYR  A 706       6                                                       
HET    OXY  A 707       2                                                       
HET    OXY  A 708       2                                                       
HET      K  B 701       1                                                       
HET    FAD  B 702      53                                                       
HET     MG  B 703       1                                                       
HET    TPP  B 704      26                                                       
HET    PYR  B 705       6                                                       
HET    PYR  B 706       6                                                       
HET    OXY  B 707       2                                                       
HET    OXY  B 708       2                                                       
HET    OXY  B 709       2                                                       
HET    OXY  B 710       2                                                       
HET    OXY  B 711       2                                                       
HET    OXY  B 712       2                                                       
HET    PO4  B 713       5                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETNAM     PYR PYRUVIC ACID                                                     
HETNAM     OXY OXYGEN MOLECULE                                                  
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   6  TPP    2(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL   7  PYR    4(C3 H4 O3)                                                  
FORMUL   9  OXY    8(O2)                                                        
FORMUL  23  PO4    O4 P 3-                                                      
FORMUL  24  HOH   *635(H2 O)                                                    
HELIX    1 AA1 THR A   93  GLN A  105  1                                  13    
HELIX    2 AA2 GLY A  115  ALA A  117  5                                   3    
HELIX    3 AA3 ILE A  118  SER A  128  1                                  11    
HELIX    4 AA4 HIS A  138  GLY A  154  1                                  17    
HELIX    5 AA5 GLY A  164  ASN A  169  1                                   6    
HELIX    6 AA6 VAL A  170  GLY A  181  1                                  12    
HELIX    7 AA7 PRO A  192  ILE A  196  5                                   5    
HELIX    8 AA8 ASP A  205  SER A  210  1                                   6    
HELIX    9 AA9 ARG A  211  THR A  214  5                                   4    
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 GLN A  281  ALA A  299  1                                  19    
HELIX   15 AB6 ALA A  308  HIS A  313  5                                   6    
HELIX   16 AB7 ASP A  315  GLN A  328  1                                  14    
HELIX   17 AB8 LEU A  335  LEU A  338  5                                   4    
HELIX   18 AB9 CYS A  357  ALA A  367  1                                  11    
HELIX   19 AC1 ASP A  378  GLY A  383  1                                   6    
HELIX   20 AC2 ASN A  384  PHE A  388  5                                   5    
HELIX   21 AC3 ALA A  389  GLU A  398  1                                  10    
HELIX   22 AC4 SER A  409  ILE A  413  5                                   5    
HELIX   23 AC5 ASP A  426  SER A  436  1                                  11    
HELIX   24 AC6 ARG A  444  TYR A  458  1                                  15    
HELIX   25 AC7 LYS A  472  THR A  487  1                                  16    
HELIX   26 AC8 GLY A  498  TRP A  508  1                                  11    
HELIX   27 AC9 TYR A  527  LYS A  539  1                                  13    
HELIX   28 AD1 ASP A  550  LEU A  557  1                                   8    
HELIX   29 AD2 GLU A  559  GLY A  567  1                                   9    
HELIX   30 AD3 ASP A  604  GLY A  613  1                                  10    
HELIX   31 AD4 LYS A  621  GLU A  623  5                                   3    
HELIX   32 AD5 GLU A  624  THR A  635  1                                  12    
HELIX   33 AD6 THR B   93  GLN B  105  1                                  13    
HELIX   34 AD7 GLY B  115  ALA B  117  5                                   3    
HELIX   35 AD8 ILE B  118  ASN B  127  1                                  10    
HELIX   36 AD9 HIS B  138  GLY B  154  1                                  17    
HELIX   37 AE1 GLY B  164  ASN B  169  1                                   6    
HELIX   38 AE2 VAL B  170  GLY B  181  1                                  12    
HELIX   39 AE3 PRO B  192  ILE B  196  5                                   5    
HELIX   40 AE4 ASP B  205  SER B  210  1                                   6    
HELIX   41 AE5 ARG B  211  THR B  214  5                                   4    
HELIX   42 AE6 SER B  222  GLU B  224  5                                   3    
HELIX   43 AE7 GLU B  225  SER B  239  1                                  15    
HELIX   44 AE8 LYS B  251  ALA B  256  1                                   6    
HELIX   45 AE9 LYS B  265  THR B  267  5                                   3    
HELIX   46 AF1 SER B  278  LEU B  298  1                                  21    
HELIX   47 AF2 ALA B  308  HIS B  313  5                                   6    
HELIX   48 AF3 ASP B  315  ALA B  327  1                                  13    
HELIX   49 AF4 LEU B  335  LEU B  338  5                                   4    
HELIX   50 AF5 CYS B  357  VAL B  364  1                                   8    
HELIX   51 AF6 ASP B  378  GLY B  383  1                                   6    
HELIX   52 AF7 GLU B  391  ALA B  396  1                                   6    
HELIX   53 AF8 SER B  409  ILE B  413  5                                   5    
HELIX   54 AF9 ASP B  426  MET B  435  1                                  10    
HELIX   55 AG1 ARG B  444  TYR B  458  1                                  15    
HELIX   56 AG2 LYS B  472  THR B  487  1                                  16    
HELIX   57 AG3 GLY B  498  TRP B  508  1                                  11    
HELIX   58 AG4 TYR B  527  LYS B  539  1                                  13    
HELIX   59 AG5 ASP B  550  LEU B  557  1                                   8    
HELIX   60 AG6 GLU B  559  GLY B  567  1                                   9    
HELIX   61 AG7 ASP B  604  MET B  612  1                                   9    
HELIX   62 AG8 LYS B  621  GLU B  623  5                                   3    
HELIX   63 AG9 GLU B  624  THR B  635  1                                  12    
SHEET    1 AA1 2 MET A  85  ASP A  86  0                                        
SHEET    2 AA1 2 ILE A 262  PRO A 263 -1  O  ILE A 262   N  ASP A  86           
SHEET    1 AA2 6 ASN A 132  VAL A 134  0                                        
SHEET    2 AA2 6 THR A 109  GLY A 112  1  N  VAL A 110   O  VAL A 134           
SHEET    3 AA2 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4 AA2 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5 AA2 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6 AA2 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1 AA3 6 SER A 348  MET A 351  0                                        
SHEET    2 AA3 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3 AA3 6 PRO A 302  VAL A 306  1  N  LEU A 304   O  THR A 332           
SHEET    4 AA3 6 LEU A 369  VAL A 373  1  O  ILE A 371   N  VAL A 303           
SHEET    5 AA3 6 GLY A 402  GLU A 407  1  O  ILE A 404   N  ALA A 372           
SHEET    6 AA3 6 ILE A 421  GLU A 424  1  O  VAL A 423   N  HIS A 405           
SHEET    1 AA4 6 PHE A 516  ILE A 517  0                                        
SHEET    2 AA4 6 VAL A 491  THR A 495  1  N  VAL A 493   O  ILE A 517           
SHEET    3 AA4 6 LEU A 543  GLY A 549  1  O  ILE A 547   N  THR A 494           
SHEET    4 AA4 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 546           
SHEET    5 AA4 6 VAL A 639  GLU A 644  1  O  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  PHE B 406   N  ALA B 372           
SHEET    6 AA7 6 ILE B 421  GLU B 424  1  O  VAL B 423   N  HIS B 405           
SHEET    1 AA8 6 PHE B 516  ILE B 517  0                                        
SHEET    2 AA8 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3 AA8 6 LEU B 543  GLY B 549  1  O  ILE B 545   N  THR B 494           
SHEET    4 AA8 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 548           
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  VAL B 619   O  GLU B 642           
SHEET    1 AA9 2 VAL B 583  GLN B 587  0                                        
SHEET    2 AA9 2 ARG B 594  HIS B 597 -1  O  TYR B 595   N  GLN B 585           
LINK         OE1 GLN A 343                 K     K A 701     1555   1555  2.83  
LINK         O   GLN A 506                 K     K A 701     1555   1555  2.74  
LINK         O   TRP A 508                 K     K A 701     1555   1555  2.62  
LINK         OD1 ASP A 550                MG    MG A 702     1555   1555  2.22  
LINK         OD1 ASN A 577                MG    MG A 702     1555   1555  2.18  
LINK         OE1 GLN B 343                 K     K B 701     1555   1555  2.76  
LINK         O   GLN B 506                 K     K B 701     1555   1555  2.79  
LINK         O   TRP B 508                 K     K B 701     1555   1555  2.60  
LINK         OD1 ASP B 550                MG    MG B 703     1555   1555  2.09  
LINK         OD1 ASN B 577                MG    MG B 703     1555   1555  2.12  
LINK         K     K A 701                 O   HOH A 836     1555   1555  2.88  
LINK         K     K A 701                 O   HOH A1078     1555   1555  2.72  
LINK         K     K A 701                 O   HOH A 970     1555   1555  2.83  
LINK        MG    MG A 702                 O1A TPP A 704     1555   1555  2.07  
LINK        MG    MG A 702                 O1B TPP A 704     1555   1555  2.06  
LINK        MG    MG A 702                 O   HOH A 864     1555   1555  2.10  
LINK        MG    MG A 702                 O   HOH A1013     1555   1555  2.00  
LINK         K     K B 701                 O   HOH B 937     1555   1555  2.86  
LINK         K     K B 701                 O   HOH B 884     1555   1555  2.82  
LINK         K     K B 701                 O   HOH B 801     1555   1555  2.77  
LINK        MG    MG B 703                 O   HOH B 877     1555   1555  2.21  
LINK        MG    MG B 703                 O2B TPP B 704     1555   1555  1.96  
LINK        MG    MG B 703                 O   HOH B 981     1555   1555  2.17  
LINK        MG    MG B 703                 O1A TPP B 704     1555   1555  2.09  
CISPEP   1 SER A  270    ASN A  271          0         7.19                     
CISPEP   2 GLY B  383    ASN B  384          0         4.68                     
SITE     1 AC1  6 GLN A 343  GLN A 506  TRP A 508  HOH A 836                    
SITE     2 AC1  6 HOH A 970  HOH A1078                                          
SITE     1 AC2  5 ASP A 550  ASN A 577  TPP A 704  HOH A 864                    
SITE     2 AC2  5 HOH A1013                                                     
SITE     1 AC3 28 ARG A 241  GLY A 307  ALA A 308  GLY A 309                    
SITE     2 AC3 28 ASN A 312  THR A 334  LEU A 335  LEU A 352                    
SITE     3 AC3 28 GLY A 353  MET A 354  HIS A 355  GLY A 356                    
SITE     4 AC3 28 GLY A 374  ALA A 375  ARG A 376  ASP A 378                    
SITE     5 AC3 28 ARG A 380  VAL A 381  GLU A 407  VAL A 408                    
SITE     6 AC3 28 ASN A 412  GLY A 425  ASP A 426  ALA A 427                    
SITE     7 AC3 28 HOH A 883  HOH A 919  HOH A 950  HOH A1021                    
SITE     1 AC4 26 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC4 26 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC4 26 ALA A 551  SER A 552  ASN A 577   MG A 702                    
SITE     4 AC4 26 HOH A 864  HOH A 895  HOH A 907  HOH A1013                    
SITE     5 AC4 26 HOH A1045  TYR B 113  PRO B 114  GLY B 115                    
SITE     6 AC4 26 GLU B 139  PRO B 165  ASN B 169  GLN B 202                    
SITE     7 AC4 26 PYR B 705  OXY B 711                                          
SITE     1 AC5  8 GLY A 115  GLY A 116  PHE A 201  GLN A 202                    
SITE     2 AC5  8 PYR A 706  OXY A 708  TPP B 704  OXY B 712                    
SITE     1 AC6  8 GLY A 116  ALA A 117  SER A 163  PHE A 201                    
SITE     2 AC6  8 GLN A 202  LYS A 251  PYR A 705  OXY A 708                    
SITE     1 AC7  6 ALA A 551  GLN A 600  HOH A 801  HOH A 819                    
SITE     2 AC7  6 TYR B 113  LYS B 137                                          
SITE     1 AC8  8 GLY A 115  GLY A 116  ALA A 117  THR A 162                    
SITE     2 AC8  8 SER A 163  GLN A 202  PYR A 705  PYR A 706                    
SITE     1 AC9  6 GLN B 343  GLN B 506  TRP B 508  HOH B 801                    
SITE     2 AC9  6 HOH B 884  HOH B 937                                          
SITE     1 AD1 31 PHE A 201  ARG B 241  GLY B 307  ALA B 308                    
SITE     2 AD1 31 GLY B 309  ASN B 312  THR B 334  LEU B 335                    
SITE     3 AD1 31 LEU B 352  MET B 354  HIS B 355  GLY B 374                    
SITE     4 AD1 31 ALA B 375  ARG B 376  ARG B 380  VAL B 381                    
SITE     5 AD1 31 GLU B 407  VAL B 408  SER B 409  ASN B 412                    
SITE     6 AD1 31 GLY B 425  ASP B 426  ALA B 427  GLN B 501                    
SITE     7 AD1 31 MET B 502  GLY B 520  GLY B 521  HOH B 896                    
SITE     8 AD1 31 HOH B 916  HOH B 926  HOH B 962                               
SITE     1 AD2  5 ASP B 550  ASN B 577  TPP B 704  HOH B 877                    
SITE     2 AD2  5 HOH B 981                                                     
SITE     1 AD3 24 TYR A 113  PRO A 114  GLY A 115  GLU A 139                    
SITE     2 AD3 24 PRO A 165  ASN A 169  PYR A 705  VAL B 497                    
SITE     3 AD3 24 GLY B 498  GLN B 499  HIS B 500  GLY B 523                    
SITE     4 AD3 24 MET B 525  GLY B 549  ASP B 550  ALA B 551                    
SITE     5 AD3 24 SER B 552  ASN B 577   MG B 703  OXY B 712                    
SITE     6 AD3 24 HOH B 866  HOH B 877  HOH B 964  HOH B 981                    
SITE     1 AD4  9 TPP A 704  HOH A 895  GLY B 116  PHE B 201                    
SITE     2 AD4  9 GLN B 202  PYR B 706  OXY B 710  OXY B 711                    
SITE     3 AD4  9 HOH B 835                                                     
SITE     1 AD5  6 GLY B 116  ALA B 117  SER B 163  PYR B 705                    
SITE     2 AD5  6 OXY B 710  HOH B 878                                          
SITE     1 AD6  4 GLU B 578  GLN B 580  HIS B 599  GLN B 600                    
SITE     1 AD7  5 GLU B 578  GLN B 600  LEU B 601  ASN B 602                    
SITE     2 AD7  5 HOH B 821                                                     
SITE     1 AD8  2 HOH A1045  TYR B 113                                          
SITE     1 AD9  7 GLY B 116  ALA B 117  THR B 162  SER B 163                    
SITE     2 AD9  7 GLN B 202  PYR B 705  PYR B 706                               
SITE     1 AE1  4 TPP A 704  GLY B 115  PYR B 705  HOH B 843                    
SITE     1 AE2  3 PYR A 705  MET B 582  TPP B 704                               
SITE     1 AE3  6 HIS A 126  GLU B 541  HIS B 597  THR B 598                    
SITE     2 AE3  6 HIS B 599  HOH B 967                                          
CRYST1   96.024  110.967  180.244  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      0.010414  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009012  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005548        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system