GenomeNet

Database: PDB
Entry: 5FEM
LinkDB: 5FEM
Original site: 5FEM 
HEADER    TRANSFERASE                             17-DEC-15   5FEM              
TITLE     SACCHAROMYCES CEREVISIAE ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH    
TITLE    2 BENSULFURON METHYL                                                   
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 (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 ATCC: 204508;                                                        
SOURCE   8 GENE: ILV2, SMR1, YMR108W, YM9718.07;                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HERBICIDE, SULFONYLUREA, BRANCHED-CHAIN AMINO ACID, ACETOHYDROXYACID  
KEYWDS   2 SYNTHASE, THDP, FAD, PYRUVATE, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.W.GUDDAT,T.LONHIENNE                                                
REVDAT   5   08-JAN-20 5FEM    1       REMARK                                   
REVDAT   4   23-MAY-18 5FEM    1       HETSYN                                   
REVDAT   3   27-SEP-17 5FEM    1       JRNL   REMARK                            
REVDAT   2   06-APR-16 5FEM    1       JRNL                                     
REVDAT   1   16-MAR-16 5FEM    0                                                
JRNL        AUTH   T.LONHIENNE,A.NOUWENS,C.M.WILLIAMS,J.A.FRASER,Y.T.LEE,       
JRNL        AUTH 2 N.P.WEST,L.W.GUDDAT                                          
JRNL        TITL   COMMERCIAL HERBICIDES CAN TRIGGER THE OXIDATIVE INACTIVATION 
JRNL        TITL 2 OF ACETOHYDROXYACID SYNTHASE.                                
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  55  4247 2016              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   26924714                                                     
JRNL        DOI    10.1002/ANIE.201511985                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 114267                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.173                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.750                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.9243 -  5.2229    1.00     8519   152  0.1783 0.1802        
REMARK   3     2  5.2229 -  4.1462    1.00     8197   146  0.1375 0.1415        
REMARK   3     3  4.1462 -  3.6223    1.00     8120   145  0.1299 0.1581        
REMARK   3     4  3.6223 -  3.2912    1.00     8047   142  0.1306 0.1325        
REMARK   3     5  3.2912 -  3.0553    1.00     8075   144  0.1396 0.1777        
REMARK   3     6  3.0553 -  2.8752    1.00     7976   143  0.1470 0.1925        
REMARK   3     7  2.8752 -  2.7312    1.00     8023   142  0.1538 0.1965        
REMARK   3     8  2.7312 -  2.6124    1.00     7963   142  0.1499 0.1823        
REMARK   3     9  2.6124 -  2.5118    1.00     7957   142  0.1493 0.1951        
REMARK   3    10  2.5118 -  2.4251    1.00     7986   143  0.1622 0.1741        
REMARK   3    11  2.4251 -  2.3493    1.00     7946   141  0.1619 0.2064        
REMARK   3    12  2.3493 -  2.2821    1.00     7951   142  0.1680 0.1940        
REMARK   3    13  2.2821 -  2.2221    1.00     7939   141  0.1713 0.2087        
REMARK   3    14  2.2221 -  2.1678    0.96     7568   135  0.1958 0.2353        
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.280           
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      :  0.005           9586                                  
REMARK   3   ANGLE     :  0.984          13037                                  
REMARK   3   CHIRALITY :  0.060           1449                                  
REMARK   3   PLANARITY :  0.004           1676                                  
REMARK   3   DIHEDRAL  : 17.340           3565                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 255 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 206.7344  64.9409 236.2998              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1157 T22:   0.1507                                     
REMARK   3      T33:   0.2035 T12:   0.0161                                     
REMARK   3      T13:   0.0082 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0532 L22:   1.2068                                     
REMARK   3      L33:   0.9488 L12:  -0.1577                                     
REMARK   3      L13:  -0.2660 L23:   0.4211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0029 S12:   0.0178 S13:  -0.0410                       
REMARK   3      S21:  -0.0233 S22:   0.0296 S23:  -0.2375                       
REMARK   3      S31:   0.0939 S32:   0.0977 S33:  -0.0078                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 213.8152  84.7046 251.0986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2801 T22:   0.3640                                     
REMARK   3      T33:   0.3820 T12:  -0.0226                                     
REMARK   3      T13:  -0.0387 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6865 L22:   1.8216                                     
REMARK   3      L33:   1.2391 L12:  -0.8259                                     
REMARK   3      L13:  -0.9016 L23:   1.4896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0146 S12:  -0.1968 S13:   0.0682                       
REMARK   3      S21:   0.2085 S22:   0.1574 S23:  -0.3846                       
REMARK   3      S31:   0.0583 S32:   0.3437 S33:  -0.2004                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 498 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 186.2025  88.5897 255.1483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1296 T22:   0.1850                                     
REMARK   3      T33:   0.1614 T12:   0.0180                                     
REMARK   3      T13:   0.0100 T23:  -0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8591 L22:   0.9686                                     
REMARK   3      L33:   0.4286 L12:   0.3743                                     
REMARK   3      L13:   0.0256 L23:   0.0351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0221 S12:  -0.1271 S13:   0.1257                       
REMARK   3      S21:   0.0598 S22:  -0.0459 S23:   0.0435                       
REMARK   3      S31:  -0.0750 S32:  -0.0699 S33:   0.0136                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 499 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 174.5486  71.2315 242.5826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1091 T22:   0.2249                                     
REMARK   3      T33:   0.1811 T12:  -0.0114                                     
REMARK   3      T13:   0.0042 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5426 L22:   0.8746                                     
REMARK   3      L33:   0.6060 L12:  -0.1625                                     
REMARK   3      L13:  -0.0049 L23:  -0.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.0064 S13:  -0.0058                       
REMARK   3      S21:  -0.0105 S22:   0.0013 S23:   0.1492                       
REMARK   3      S31:  -0.0020 S32:  -0.1667 S33:  -0.0030                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 205 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 182.5313  77.9148 218.1594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1673 T22:   0.2402                                     
REMARK   3      T33:   0.1738 T12:   0.0125                                     
REMARK   3      T13:  -0.0203 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0341 L22:   1.7682                                     
REMARK   3      L33:   1.2007 L12:  -0.3880                                     
REMARK   3      L13:  -0.2681 L23:   0.2556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0365 S12:   0.2159 S13:   0.0912                       
REMARK   3      S21:  -0.2208 S22:  -0.0521 S23:   0.0950                       
REMARK   3      S31:  -0.0776 S32:  -0.0996 S33:   0.0340                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 188.9125  85.1066 212.3513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2809 T22:   0.2834                                     
REMARK   3      T33:   0.2177 T12:  -0.0023                                     
REMARK   3      T13:   0.0208 T23:   0.0496                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3542 L22:   2.1738                                     
REMARK   3      L33:   1.3265 L12:  -0.8701                                     
REMARK   3      L13:  -0.5416 L23:   0.7245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0701 S12:   0.2529 S13:   0.1636                       
REMARK   3      S21:  -0.4515 S22:  -0.0639 S23:  -0.0556                       
REMARK   3      S31:  -0.2547 S32:  -0.0209 S33:  -0.0609                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 203.2004  54.8493 196.8832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4501 T22:   0.4619                                     
REMARK   3      T33:   0.2644 T12:   0.1214                                     
REMARK   3      T13:   0.0724 T23:  -0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2785 L22:   1.7111                                     
REMARK   3      L33:   1.7786 L12:  -0.1162                                     
REMARK   3      L13:  -0.2196 L23:   0.3807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1240 S12:   0.2081 S13:   0.0118                       
REMARK   3      S21:  -0.4407 S22:  -0.1484 S23:  -0.2372                       
REMARK   3      S31:   0.0598 S32:   0.2164 S33:  -0.0119                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 398 THROUGH 498 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 198.3234  49.4190 201.3533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4186 T22:   0.3660                                     
REMARK   3      T33:   0.2549 T12:   0.0753                                     
REMARK   3      T13:   0.0125 T23:  -0.0911                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7888 L22:   0.7738                                     
REMARK   3      L33:   1.5522 L12:  -0.1754                                     
REMARK   3      L13:  -0.4232 L23:  -0.2136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1064 S12:   0.2154 S13:  -0.1168                       
REMARK   3      S21:  -0.4505 S22:  -0.1740 S23:  -0.0863                       
REMARK   3      S31:   0.2547 S32:   0.1511 S33:   0.0203                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 499 THROUGH 604 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 189.0792  51.6451 220.9522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2396 T22:   0.2601                                     
REMARK   3      T33:   0.2398 T12:  -0.0249                                     
REMARK   3      T13:   0.0068 T23:  -0.0521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9524 L22:   1.0705                                     
REMARK   3      L33:   1.0095 L12:  -0.2839                                     
REMARK   3      L13:   0.1168 L23:   0.0680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0487 S12:   0.0948 S13:  -0.1260                       
REMARK   3      S21:  -0.0868 S22:  -0.0463 S23:  -0.0132                       
REMARK   3      S31:   0.1526 S32:   0.0141 S33:  -0.0011                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 605 THROUGH 654 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 180.4154  42.7220 223.2399              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2697 T22:   0.2349                                     
REMARK   3      T33:   0.2906 T12:  -0.0433                                     
REMARK   3      T13:  -0.0372 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5841 L22:   1.4213                                     
REMARK   3      L33:   1.4125 L12:  -0.4511                                     
REMARK   3      L13:  -0.3753 L23:   0.2521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0198 S12:   0.0807 S13:  -0.2901                       
REMARK   3      S21:  -0.0621 S22:  -0.0771 S23:   0.2210                       
REMARK   3      S31:   0.2780 S32:  -0.1584 S33:   0.0251                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 655 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 205.9045  36.2750 223.1255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4283 T22:   0.3928                                     
REMARK   3      T33:   0.4705 T12:   0.0538                                     
REMARK   3      T13:  -0.0119 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2810 L22:   1.8957                                     
REMARK   3      L33:   3.2412 L12:   0.1057                                     
REMARK   3      L13:  -0.3693 L23:  -0.6021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1286 S12:   0.0605 S13:  -0.4205                       
REMARK   3      S21:  -0.0930 S22:  -0.0725 S23:  -0.0576                       
REMARK   3      S31:   0.3423 S32:   0.1094 S33:   0.0696                       
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 5FEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216361.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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   : 114282                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.168                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1N0H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
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, VAPOR DIFFUSION, TEMPERATURE 291K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 11950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ASN A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     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     ASN B   271                                                      
REMARK 465     ALA B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ASN B   274                                                      
REMARK 465     GLN B   275                                                      
REMARK 465     LEU B   276                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     THR A 277    OG1  CG2                                            
REMARK 470     LYS A 456    CG   CD   CE   NZ                                   
REMARK 470     THR B 277    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 557   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    LEU B 557   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A 216      147.31   -170.07                                   
REMARK 500    ASP A 350     -159.40     69.98                                   
REMARK 500    GLU A 663       50.68   -113.08                                   
REMARK 500    ASP B 350     -157.49     69.91                                   
REMARK 500    TYR B 460       78.20    -65.86                                   
REMARK 500    GLU B 663       49.37   -108.89                                   
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                              MG A 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 343   OE1                                                    
REMARK 620 2 ASP A 350   OD2  82.9                                              
REMARK 620 3 GLN A 506   O   164.1 103.6                                        
REMARK 620 4 TRP A 508   O    84.9 167.6  87.7                                  
REMARK 620 5 HOH A 845   O    80.7  69.8  87.9 105.9                            
REMARK 620 6 HOH A1091   O    94.2  98.5  99.0  84.7 167.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 550   OD1                                                    
REMARK 620 2 ASN A 577   OD1  85.4                                              
REMARK 620 3 GLU A 579   O   100.0  88.0                                        
REMARK 620 4 TPP A 705   O1A  86.9 172.3  92.6                                  
REMARK 620 5 HOH A 867   O    82.9  84.5 171.7  95.4                            
REMARK 620 6 TPP A 705   O1B 166.3  96.1  93.7  91.5  83.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 343   OE1                                                    
REMARK 620 2 ASP B 350   OD2  81.9                                              
REMARK 620 3 GLN B 506   O   167.4 107.2                                        
REMARK 620 4 TRP B 508   O    81.4 163.3  89.4                                  
REMARK 620 5 HOH B 822   O    80.3  72.2  94.1 105.8                            
REMARK 620 6 HOH B1008   O   101.6  97.1  86.2  85.4 168.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 702  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 550   OD1                                                    
REMARK 620 2 ASN B 577   OD1  84.2                                              
REMARK 620 3 GLU B 579   O   103.2  89.8                                        
REMARK 620 4 TPP B 705   O2B 161.2  97.2  95.6                                  
REMARK 620 5 HOH B 873   O    80.7  87.4 174.9  80.6                            
REMARK 620 6 TPP B 705   O2A  89.0 173.0  93.5  88.7  89.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 60G A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 60G B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP B 705                 
DBREF  5FEM A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  5FEM B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 5FEM MET A   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER A   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER A   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY A   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LEU A   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM VAL A   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PRO A   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ARG A   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY A   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER A   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY A   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET A   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS A   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLU A   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM THR A   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA A   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA A   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA A   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS A   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PHE A   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLU A   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ARG A   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLN A   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS A   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET A   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER A   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PRO A   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LEU A   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY A   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM THR A   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP A   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS A   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA A   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET A   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY A   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER A   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET B   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER B   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER B   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY B   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LEU B   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM VAL B   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PRO B   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ARG B   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY B   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER B   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY B   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET B   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS B   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLU B   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM THR B   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA B   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA B   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA B   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS B   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PHE B   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLU B   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ARG B   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLN B   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM HIS B   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET B   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM SER B   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM PRO B   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LEU B   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY B   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM THR B   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ASP B   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM LYS B   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM ALA B   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM MET B   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM GLY B   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5FEM 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     MG  A 701       1                                                       
HET    FAD  A 702      53                                                       
HET    60G  A 703      28                                                       
HET     MG  A 704       1                                                       
HET    TPP  A 705      26                                                       
HET    FAD  B 701      53                                                       
HET     MG  B 702       1                                                       
HET    60G  B 703      28                                                       
HET     MG  B 704       1                                                       
HET    TPP  B 705      26                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     60G METHYL 2-[(4,6-DIMETHOXYPYRIMIDIN-2-YL)                          
HETNAM   2 60G  CARBAMOYLSULFAMOYLMETHYL]BENZOATE                               
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETSYN     60G BENSULFURON METHYL                                               
FORMUL   3   MG    4(MG 2+)                                                     
FORMUL   4  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   5  60G    2(C16 H18 N4 O7 S)                                           
FORMUL   7  TPP    2(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL  13  HOH   *557(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  ILE A  125  1                                   8    
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 ASP A  205  SER A  210  1                                   6    
HELIX    8 AA8 ARG A  211  THR A  214  5                                   4    
HELIX    9 AA9 SER A  222  GLU A  224  5                                   3    
HELIX   10 AB1 GLU A  225  SER A  239  1                                  15    
HELIX   11 AB2 LYS A  251  ALA A  256  1                                   6    
HELIX   12 AB3 THR A  264  LEU A  268  1                                   5    
HELIX   13 AB4 SER A  278  ALA A  299  1                                  22    
HELIX   14 AB5 ALA A  308  HIS A  313  5                                   6    
HELIX   15 AB6 ASP A  315  GLN A  328  1                                  14    
HELIX   16 AB7 LEU A  335  LEU A  338  5                                   4    
HELIX   17 AB8 CYS A  357  ALA A  367  1                                  11    
HELIX   18 AB9 ASP A  378  GLY A  383  1                                   6    
HELIX   19 AC1 ASN A  384  PHE A  388  5                                   5    
HELIX   20 AC2 ALA A  389  GLU A  398  1                                  10    
HELIX   21 AC3 SER A  409  ILE A  413  5                                   5    
HELIX   22 AC4 ASP A  426  MET A  435  1                                  10    
HELIX   23 AC5 SER A  436  ILE A  438  5                                   3    
HELIX   24 AC6 ARG A  444  TYR A  458  1                                  15    
HELIX   25 AC7 LYS A  472  ASP A  486  1                                  15    
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 GLN A  580  TYR A  591  1                                  12    
HELIX   31 AD4 ASP A  604  MET A  612  1                                   9    
HELIX   32 AD5 LYS A  621  GLU A  623  5                                   3    
HELIX   33 AD6 GLU A  624  THR A  635  1                                  12    
HELIX   34 AD7 ASP A  668  THR A  683  1                                  16    
HELIX   35 AD8 THR B   93  GLN B  105  1                                  13    
HELIX   36 AD9 GLY B  115  ALA B  117  5                                   3    
HELIX   37 AE1 ILE B  118  ILE B  125  1                                   8    
HELIX   38 AE2 HIS B  138  GLY B  154  1                                  17    
HELIX   39 AE3 GLY B  164  ASN B  169  1                                   6    
HELIX   40 AE4 VAL B  170  GLY B  181  1                                  12    
HELIX   41 AE5 ASP B  205  SER B  210  1                                   6    
HELIX   42 AE6 ARG B  211  THR B  214  5                                   4    
HELIX   43 AE7 SER B  222  GLU B  224  5                                   3    
HELIX   44 AE8 GLU B  225  SER B  239  1                                  15    
HELIX   45 AE9 LYS B  251  ALA B  256  1                                   6    
HELIX   46 AF1 LYS B  265  THR B  267  5                                   3    
HELIX   47 AF2 SER B  278  ALA B  299  1                                  22    
HELIX   48 AF3 ALA B  308  HIS B  313  5                                   6    
HELIX   49 AF4 ASP B  315  GLN B  328  1                                  14    
HELIX   50 AF5 LEU B  335  LEU B  338  5                                   4    
HELIX   51 AF6 CYS B  357  ALA B  367  1                                  11    
HELIX   52 AF7 ASP B  378  GLY B  383  1                                   6    
HELIX   53 AF8 ASN B  384  PHE B  388  5                                   5    
HELIX   54 AF9 ALA B  389  GLU B  398  1                                  10    
HELIX   55 AG1 SER B  409  ILE B  413  5                                   5    
HELIX   56 AG2 ASP B  426  MET B  435  1                                  10    
HELIX   57 AG3 SER B  436  ILE B  438  5                                   3    
HELIX   58 AG4 ARG B  444  TYR B  458  1                                  15    
HELIX   59 AG5 LYS B  472  ASP B  486  1                                  15    
HELIX   60 AG6 GLY B  498  TRP B  508  1                                  11    
HELIX   61 AG7 TYR B  527  LYS B  539  1                                  13    
HELIX   62 AG8 ASP B  550  LEU B  557  1                                   8    
HELIX   63 AG9 GLU B  559  GLY B  567  1                                   9    
HELIX   64 AH1 GLN B  580  TYR B  591  1                                  12    
HELIX   65 AH2 ASP B  604  MET B  612  1                                   9    
HELIX   66 AH3 LYS B  621  GLU B  623  5                                   3    
HELIX   67 AH4 GLU B  624  THR B  635  1                                  12    
HELIX   68 AH5 ASP B  668  GLY B  684  1                                  17    
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  TYR A 113  1  N  VAL A 110   O  VAL A 134           
SHEET    3 AA2 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4 AA2 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5 AA2 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6 AA2 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1 AA3 6 SER A 348  MET A 351  0                                        
SHEET    2 AA3 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3 AA3 6 PRO A 302  VAL A 306  1  N  LEU A 304   O  THR A 332           
SHEET    4 AA3 6 LEU A 369  VAL A 373  1  O  VAL A 373   N  TYR A 305           
SHEET    5 AA3 6 GLY A 402  GLU A 407  1  O  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 545   N  ILE A 492           
SHEET    4 AA4 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 548           
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  TYR B 113  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  ILE B 371   N  VAL B 303           
SHEET    5 AA7 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6 AA7 6 ILE B 421  GLU B 424  1  O  VAL B 423   N  HIS B 405           
SHEET    1 AA8 6 PHE B 516  ILE B 517  0                                        
SHEET    2 AA8 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3 AA8 6 LEU B 543  GLY B 549  1  O  ILE B 547   N  THR B 494           
SHEET    4 AA8 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 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  LEU B 617   O  GLU B 642           
LINK         OE1 GLN A 343                MG    MG A 704     1555   1555  2.71  
LINK         OD2 ASP A 350                MG    MG A 704     1555   1555  2.78  
LINK         O   GLN A 506                MG    MG A 704     1555   1555  2.70  
LINK         O   TRP A 508                MG    MG A 704     1555   1555  2.60  
LINK         OD1 ASP A 550                MG    MG A 701     1555   1555  2.10  
LINK         OD1 ASN A 577                MG    MG A 701     1555   1555  2.15  
LINK         O   GLU A 579                MG    MG A 701     1555   1555  2.16  
LINK         OE1 GLN B 343                MG    MG B 704     1555   1555  2.73  
LINK         OD2 ASP B 350                MG    MG B 704     1555   1555  2.75  
LINK         O   GLN B 506                MG    MG B 704     1555   1555  2.66  
LINK         O   TRP B 508                MG    MG B 704     1555   1555  2.60  
LINK         OD1 ASP B 550                MG    MG B 702     1555   1555  2.10  
LINK         OD1 ASN B 577                MG    MG B 702     1555   1555  2.15  
LINK         O   GLU B 579                MG    MG B 702     1555   1555  2.08  
LINK        MG    MG A 701                 O1A TPP A 705     1555   1555  2.02  
LINK        MG    MG A 701                 O   HOH A 867     1555   1555  2.19  
LINK        MG    MG A 701                 O1B TPP A 705     1555   1555  1.98  
LINK        MG    MG A 704                 O   HOH A 845     1555   1555  2.73  
LINK        MG    MG A 704                 O   HOH A1091     1555   1555  2.90  
LINK        MG    MG B 702                 O2B TPP B 705     1555   1555  2.04  
LINK        MG    MG B 702                 O   HOH B 873     1555   1555  2.17  
LINK        MG    MG B 702                 O2A TPP B 705     1555   1555  1.99  
LINK        MG    MG B 704                 O   HOH B 822     1555   1555  2.53  
LINK        MG    MG B 704                 O   HOH B1008     1555   1555  2.88  
CISPEP   1 LEU A  652    PRO A  653          0        -1.92                     
CISPEP   2 LEU B  652    PRO B  653          0        -0.63                     
SITE     1 AC1  5 ASP A 550  ASN A 577  GLU A 579  TPP A 705                    
SITE     2 AC1  5 HOH A 867                                                     
SITE     1 AC2 36 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 AC2 36 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 AC2 36 GLN A 336  LEU A 352  GLY A 353  MET A 354                    
SITE     4 AC2 36 HIS A 355  GLY A 374  ALA A 375  ARG A 376                    
SITE     5 AC2 36 ASP A 378  ARG A 380  VAL A 381  GLU A 407                    
SITE     6 AC2 36 VAL A 408  ASN A 412  GLY A 425  ASP A 426                    
SITE     7 AC2 36 ALA A 427  GLN A 501  MET A 502  GLY A 520                    
SITE     8 AC2 36 GLY A 521  60G A 703  HOH A 826  HOH A 855                    
SITE     9 AC2 36 HOH A 937  HOH A 939  HOH A1036  PHE B 201                    
SITE     1 AC3 14 MET A 354  ASP A 379  ARG A 380  MET A 582                    
SITE     2 AC3 14 TRP A 586  FAD A 702  HOH A 864  GLY B 116                    
SITE     3 AC3 14 ALA B 117  VAL B 191  PRO B 192  PHE B 201                    
SITE     4 AC3 14 GLN B 202  LYS B 251                                          
SITE     1 AC4  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC4  6 HOH A 845  HOH A1091                                          
SITE     1 AC5 25 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC5 25 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC5 25 ALA A 551  SER A 552  ASN A 577  GLU A 579                    
SITE     4 AC5 25 GLN A 580  GLY A 581  MET A 582  VAL A 583                    
SITE     5 AC5 25  MG A 701  HOH A 867  TYR B 113  PRO B 114                    
SITE     6 AC5 25 GLY B 115  GLU B 139  PRO B 165  ASN B 169                    
SITE     7 AC5 25 GLN B 202                                                     
SITE     1 AC6 38 PHE A 201  ASP B 180  ARG B 241  GLY B 307                    
SITE     2 AC6 38 ALA B 308  GLY B 309  ASN B 312  THR B 334                    
SITE     3 AC6 38 LEU B 335  GLN B 336  MET B 351  LEU B 352                    
SITE     4 AC6 38 GLY B 353  MET B 354  HIS B 355  GLY B 374                    
SITE     5 AC6 38 ALA B 375  ARG B 376  ASP B 378  ARG B 380                    
SITE     6 AC6 38 VAL B 381  GLU B 407  VAL B 408  ASN B 412                    
SITE     7 AC6 38 GLY B 425  ASP B 426  ALA B 427  GLN B 501                    
SITE     8 AC6 38 MET B 502  GLY B 520  GLY B 521  60G B 703                    
SITE     9 AC6 38 HOH B 805  HOH B 835  HOH B 845  HOH B 864                    
SITE    10 AC6 38 HOH B 882  HOH B 953                                          
SITE     1 AC7  5 ASP B 550  ASN B 577  GLU B 579  TPP B 705                    
SITE     2 AC7  5 HOH B 873                                                     
SITE     1 AC8 11 GLY A 116  VAL A 191  PRO A 192  PHE A 201                    
SITE     2 AC8 11 GLN A 202  LYS A 251  MET B 354  ARG B 380                    
SITE     3 AC8 11 MET B 582  TRP B 586  FAD B 701                               
SITE     1 AC9  6 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC9  6 HOH B 822  HOH B1008                                          
SITE     1 AD1 25 TYR A 113  PRO A 114  GLY A 115  GLU A 139                    
SITE     2 AD1 25 PRO A 165  ASN A 169  GLN A 202  VAL B 497                    
SITE     3 AD1 25 GLY B 498  GLN B 499  HIS B 500  GLY B 523                    
SITE     4 AD1 25 MET B 525  GLY B 549  ASP B 550  ALA B 551                    
SITE     5 AD1 25 SER B 552  ASN B 577  GLU B 579  GLN B 580                    
SITE     6 AD1 25 GLY B 581  MET B 582  VAL B 583   MG B 702                    
SITE     7 AD1 25 HOH B 873                                                     
CRYST1  154.673  154.673  178.385  90.00  90.00  90.00 P 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006465  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005606        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system