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Database: PDB
Entry: 5WKC
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HEADER    STRUCTURAL PROTEIN,TRANSFERASE          25-JUL-17   5WKC              
TITLE     SACCHAROMYCES CEREVISIAE ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH THE
TITLE    2 HERBICIDE PENOXSULAM                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL;    
COMPND   3 CHAIN: A, B, E;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 58-687;                                       
COMPND   5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE CATALYTIC SUBUNIT,ALS;           
COMPND   6 EC: 2.2.1.6;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL;    
COMPND  10 CHAIN: D;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 58-687;                                       
COMPND  12 SYNONYM: ACETOHYDROXY-ACID SYNTHASE CATALYTIC SUBUNIT,ALS;           
COMPND  13 EC: 2.2.1.6;                                                         
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;                 
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: ILV2, SMR1, YMR108W, YM9718.07;                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;                 
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 559292;                                              
SOURCE  13 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  14 GENE: ILV2, SMR1, YMR108W, YM9718.07;                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AHAS, ACETOHYDROXYACID SYNTHASE; SCAHAS; THIAMINE DIPHOSPHATE; FLAVIN 
KEYWDS   2 ADENINE DINUCLEOTIDE; PENOXSULAM; AMINOETHENETHIOL DIPHOSPHATE;      
KEYWDS   3 PERACETATE., STRUCTURAL PROTEIN, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.L.GUDDAT,G.T.LONHIENNE                                              
REVDAT   5   08-JAN-20 5WKC    1       REMARK                                   
REVDAT   4   23-OCT-19 5WKC    1       REMARK                                   
REVDAT   3   07-MAR-18 5WKC    1       JRNL                                     
REVDAT   2   28-FEB-18 5WKC    1       JRNL                                     
REVDAT   1   14-FEB-18 5WKC    0                                                
JRNL        AUTH   T.LONHIENNE,M.D.GARCIA,G.PIERENS,M.MOBLI,A.NOUWENS,          
JRNL        AUTH 2 L.W.GUDDAT                                                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE MECHANISM OF INHIBITION OF AHAS 
JRNL        TITL 2 BY HERBICIDES.                                               
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115 E1945 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   29440497                                                     
JRNL        DOI    10.1073/PNAS.1714392115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 182982                         
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                     : 0.180                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.090                           
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 48.8046 -  5.6220    1.00    13474   149  0.1368 0.1414        
REMARK   3     2  5.6220 -  4.4633    1.00    13110   145  0.1217 0.1491        
REMARK   3     3  4.4633 -  3.8994    1.00    13006   144  0.1203 0.1540        
REMARK   3     4  3.8994 -  3.5430    1.00    12983   144  0.1325 0.1601        
REMARK   3     5  3.5430 -  3.2891    1.00    12949   142  0.1447 0.1899        
REMARK   3     6  3.2891 -  3.0952    1.00    12902   143  0.1575 0.1759        
REMARK   3     7  3.0952 -  2.9402    1.00    12860   142  0.1633 0.2002        
REMARK   3     8  2.9402 -  2.8123    1.00    12889   142  0.1726 0.2224        
REMARK   3     9  2.8123 -  2.7040    1.00    12840   143  0.1811 0.2234        
REMARK   3    10  2.7040 -  2.6107    1.00    12880   142  0.1746 0.1903        
REMARK   3    11  2.6107 -  2.5291    1.00    12789   141  0.1796 0.2246        
REMARK   3    12  2.5291 -  2.4568    1.00    12855   142  0.1897 0.2282        
REMARK   3    13  2.4568 -  2.3921    1.00    12807   142  0.2061 0.2253        
REMARK   3    14  2.3921 -  2.3338    0.99    12638   139  0.2124 0.2495        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.680           
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      :  0.008          19091                                  
REMARK   3   ANGLE     :  0.917          25972                                  
REMARK   3   CHIRALITY :  0.037           2882                                  
REMARK   3   PLANARITY :  0.003           3337                                  
REMARK   3   DIHEDRAL  : 14.264           7131                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 85 THROUGH 255 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9248 474.0040  40.2435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2081 T22:   0.2523                                     
REMARK   3      T33:   0.1882 T12:  -0.0402                                     
REMARK   3      T13:   0.0511 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0564 L22:   1.6113                                     
REMARK   3      L33:   1.1709 L12:   0.0305                                     
REMARK   3      L13:   0.2156 L23:   0.0426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:   0.3776 S13:   0.0512                       
REMARK   3      S21:  -0.2608 S22:   0.0107 S23:  -0.2105                       
REMARK   3      S31:  -0.0564 S32:   0.2303 S33:  -0.0081                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5023 465.3640  18.0725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6087 T22:   0.8454                                     
REMARK   3      T33:   0.3171 T12:   0.0180                                     
REMARK   3      T13:   0.0020 T23:  -0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6570 L22:   0.1777                                     
REMARK   3      L33:   5.1604 L12:   1.0520                                     
REMARK   3      L13:   6.6698 L23:   0.8684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4024 S12:   1.4407 S13:  -0.5325                       
REMARK   3      S21:  -0.2959 S22:   0.0414 S23:  -0.2159                       
REMARK   3      S31:   0.4795 S32:   0.8944 S33:  -0.4216                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7871 483.3012  34.0487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3113 T22:   0.3289                                     
REMARK   3      T33:   0.2515 T12:   0.0036                                     
REMARK   3      T13:  -0.0561 T23:   0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9109 L22:   0.7796                                     
REMARK   3      L33:   0.8421 L12:  -0.0051                                     
REMARK   3      L13:  -0.0721 L23:   0.1358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:   0.3461 S13:   0.1677                       
REMARK   3      S21:  -0.2267 S22:  -0.0066 S23:   0.1041                       
REMARK   3      S31:  -0.1403 S32:  -0.1636 S33:   0.0203                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 366 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9853 458.0303 115.3545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1649 T22:   0.1744                                     
REMARK   3      T33:   0.2743 T12:  -0.0308                                     
REMARK   3      T13:  -0.0167 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5595 L22:   0.9790                                     
REMARK   3      L33:   0.7844 L12:  -0.2311                                     
REMARK   3      L13:   0.1632 L23:  -0.5609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:  -0.0021 S13:  -0.1187                       
REMARK   3      S21:  -0.0260 S22:   0.0128 S23:   0.1317                       
REMARK   3      S31:   0.0873 S32:  -0.0317 S33:  -0.0315                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 367 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3442 480.6568 111.2466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.1824                                     
REMARK   3      T33:   0.2838 T12:  -0.0545                                     
REMARK   3      T13:  -0.0273 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6831 L22:   0.4007                                     
REMARK   3      L33:   0.6259 L12:   0.0675                                     
REMARK   3      L13:   0.0870 L23:   0.0431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:  -0.0072 S13:   0.1563                       
REMARK   3      S21:  -0.0107 S22:   0.0048 S23:  -0.0015                       
REMARK   3      S31:  -0.1613 S32:   0.0758 S33:   0.0108                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 84 THROUGH 255 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8836 476.5680 141.4778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2973 T22:   0.2998                                     
REMARK   3      T33:   0.2168 T12:  -0.0614                                     
REMARK   3      T13:   0.0109 T23:  -0.0760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8016 L22:   2.4658                                     
REMARK   3      L33:   1.2891 L12:  -0.3513                                     
REMARK   3      L13:   0.1606 L23:  -0.2862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:  -0.3687 S13:   0.1654                       
REMARK   3      S21:   0.4795 S22:   0.0081 S23:   0.0858                       
REMARK   3      S31:  -0.1663 S32:  -0.0119 S33:   0.0030                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 256 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4427 466.6842 163.8899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9054 T22:   0.9889                                     
REMARK   3      T33:   0.5780 T12:  -0.0126                                     
REMARK   3      T13:   0.1286 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3384 L22:   9.5174                                     
REMARK   3      L33:   9.4071 L12:  -3.2946                                     
REMARK   3      L13:   3.1865 L23:  -9.4975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3021 S12:  -0.9877 S13:  -0.0836                       
REMARK   3      S21:   1.0459 S22:   0.8829 S23:   0.7552                       
REMARK   3      S31:  -0.2902 S32:  -1.2035 S33:  -0.6547                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 299 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2921 449.9186 156.2126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5901 T22:   0.6226                                     
REMARK   3      T33:   0.3770 T12:  -0.0027                                     
REMARK   3      T13:  -0.1272 T23:   0.1363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0803 L22:   1.3317                                     
REMARK   3      L33:   1.0894 L12:  -0.0626                                     
REMARK   3      L13:  -0.3527 L23:  -0.0254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0406 S12:  -0.6268 S13:  -0.2865                       
REMARK   3      S21:   0.6304 S22:   0.0355 S23:  -0.0496                       
REMARK   3      S31:   0.2180 S32:   0.1964 S33:   0.0037                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 543 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.7239 451.7185 133.9492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2674 T22:   0.3760                                     
REMARK   3      T33:   0.3592 T12:  -0.0134                                     
REMARK   3      T13:  -0.1094 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1085 L22:   1.9732                                     
REMARK   3      L33:   0.7583 L12:   0.1842                                     
REMARK   3      L13:   0.0893 L23:  -0.0353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:  -0.1868 S13:  -0.1980                       
REMARK   3      S21:   0.2292 S22:   0.0074 S23:  -0.3324                       
REMARK   3      S31:   0.1022 S32:   0.2555 S33:  -0.0205                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 84 THROUGH 238 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7305 464.7557  59.2184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1337 T22:   0.1210                                     
REMARK   3      T33:   0.1704 T12:  -0.0204                                     
REMARK   3      T13:  -0.0040 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7635 L22:   1.1440                                     
REMARK   3      L33:   1.2363 L12:  -0.0046                                     
REMARK   3      L13:   0.1184 L23:   0.0335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.0242 S13:  -0.1229                       
REMARK   3      S21:  -0.0218 S22:   0.0099 S23:   0.0899                       
REMARK   3      S31:   0.0398 S32:  -0.0990 S33:   0.0156                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 239 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8355 455.4808  60.1831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2178 T22:   0.2214                                     
REMARK   3      T33:   0.3033 T12:  -0.0597                                     
REMARK   3      T13:  -0.0228 T23:   0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9281 L22:   0.3108                                     
REMARK   3      L33:   0.5233 L12:  -0.3451                                     
REMARK   3      L13:   0.8662 L23:   0.1822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1242 S12:  -0.3978 S13:  -0.5025                       
REMARK   3      S21:   0.1595 S22:  -0.0759 S23:   0.1049                       
REMARK   3      S31:   0.1348 S32:  -0.2625 S33:  -0.0571                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 279 THROUGH 457 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4494 459.8146  79.0773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1761 T22:   0.1691                                     
REMARK   3      T33:   0.2292 T12:   0.0084                                     
REMARK   3      T13:  -0.0556 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7298 L22:   1.9191                                     
REMARK   3      L33:   2.1607 L12:   0.2565                                     
REMARK   3      L13:  -0.0704 L23:  -0.1195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0244 S12:  -0.0585 S13:  -0.0734                       
REMARK   3      S21:   0.2154 S22:  -0.0569 S23:  -0.2092                       
REMARK   3      S31:   0.1350 S32:   0.2398 S33:   0.0208                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 458 THROUGH 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0411 486.8476  67.4534              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2158 T22:   0.1528                                     
REMARK   3      T33:   0.2632 T12:  -0.0575                                     
REMARK   3      T13:  -0.0154 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3912 L22:   0.5418                                     
REMARK   3      L33:   0.7507 L12:   0.1125                                     
REMARK   3      L13:  -0.0298 L23:   0.1116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0184 S12:  -0.0596 S13:   0.2036                       
REMARK   3      S21:   0.0190 S22:  -0.0034 S23:  -0.1230                       
REMARK   3      S31:  -0.1800 S32:   0.1609 S33:  -0.0176                       
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 5WKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229182.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8 - 7.2                          
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   : 183012                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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   (%): 66.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SUCCINIC ACID PH 7.0, 0.1 M HEPES    
REMARK 280  PH 7.0 AND 1% W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 2,000.,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000      109.10650            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      180.97000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000      109.10650            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      180.97000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000      109.10650            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      180.97000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000      109.10650            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      180.97000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      109.10650            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      180.97000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      109.10650            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      180.97000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000      109.10650            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      180.97000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      109.10650            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000      109.10650            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      180.97000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 10870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     PRO A    83                                                      
REMARK 465     ASP A    84                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     PRO A   269                                                      
REMARK 465     SER A   270                                                      
REMARK 465     ASN A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ARG A   279                                                      
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     SER B   270                                                      
REMARK 465     ASN B   271                                                      
REMARK 465     ALA B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ASN B   274                                                      
REMARK 465     GLN B   275                                                      
REMARK 465     LEU B   276                                                      
REMARK 465     MET E    11                                                      
REMARK 465     HIS E    12                                                      
REMARK 465     HIS E    13                                                      
REMARK 465     HIS E    14                                                      
REMARK 465     HIS E    15                                                      
REMARK 465     HIS E    16                                                      
REMARK 465     HIS E    17                                                      
REMARK 465     SER E    18                                                      
REMARK 465     SER E    19                                                      
REMARK 465     GLY E    20                                                      
REMARK 465     LEU E    21                                                      
REMARK 465     VAL E    22                                                      
REMARK 465     PRO E    23                                                      
REMARK 465     ARG E    24                                                      
REMARK 465     GLY E    25                                                      
REMARK 465     SER E    26                                                      
REMARK 465     GLY E    27                                                      
REMARK 465     MET E    28                                                      
REMARK 465     LYS E    29                                                      
REMARK 465     GLU E    30                                                      
REMARK 465     THR E    31                                                      
REMARK 465     ALA E    32                                                      
REMARK 465     ALA E    33                                                      
REMARK 465     ALA E    34                                                      
REMARK 465     LYS E    35                                                      
REMARK 465     PHE E    36                                                      
REMARK 465     GLU E    37                                                      
REMARK 465     ARG E    38                                                      
REMARK 465     GLN E    39                                                      
REMARK 465     HIS E    40                                                      
REMARK 465     MET E    41                                                      
REMARK 465     ASP E    42                                                      
REMARK 465     SER E    43                                                      
REMARK 465     PRO E    44                                                      
REMARK 465     ASP E    45                                                      
REMARK 465     LEU E    46                                                      
REMARK 465     GLY E    47                                                      
REMARK 465     THR E    48                                                      
REMARK 465     ASP E    49                                                      
REMARK 465     ASP E    50                                                      
REMARK 465     ASP E    51                                                      
REMARK 465     ASP E    52                                                      
REMARK 465     LYS E    53                                                      
REMARK 465     ALA E    54                                                      
REMARK 465     MET E    55                                                      
REMARK 465     GLY E    56                                                      
REMARK 465     SER E    57                                                      
REMARK 465     ALA E    58                                                      
REMARK 465     PRO E    59                                                      
REMARK 465     SER E    60                                                      
REMARK 465     PHE E    61                                                      
REMARK 465     ASN E    62                                                      
REMARK 465     VAL E    63                                                      
REMARK 465     ASP E    64                                                      
REMARK 465     PRO E    65                                                      
REMARK 465     LEU E    66                                                      
REMARK 465     GLU E    67                                                      
REMARK 465     GLN E    68                                                      
REMARK 465     PRO E    69                                                      
REMARK 465     ALA E    70                                                      
REMARK 465     GLU E    71                                                      
REMARK 465     PRO E    72                                                      
REMARK 465     SER E    73                                                      
REMARK 465     LYS E    74                                                      
REMARK 465     LEU E    75                                                      
REMARK 465     ALA E    76                                                      
REMARK 465     LYS E    77                                                      
REMARK 465     LYS E    78                                                      
REMARK 465     LEU E    79                                                      
REMARK 465     ARG E    80                                                      
REMARK 465     ALA E    81                                                      
REMARK 465     GLU E    82                                                      
REMARK 465     PRO E    83                                                      
REMARK 465     SER E   270                                                      
REMARK 465     ASN E   271                                                      
REMARK 465     ALA E   272                                                      
REMARK 465     LEU E   273                                                      
REMARK 465     ASN E   274                                                      
REMARK 465     GLN E   275                                                      
REMARK 465     LEU E   276                                                      
REMARK 465     THR E   277                                                      
REMARK 465     SER E   278                                                      
REMARK 465     ARG E   279                                                      
REMARK 465     ALA E   280                                                      
REMARK 465     GLN E   281                                                      
REMARK 465     MET D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     HIS D    13                                                      
REMARK 465     HIS D    14                                                      
REMARK 465     HIS D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     HIS D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     GLY D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     VAL D    22                                                      
REMARK 465     PRO D    23                                                      
REMARK 465     ARG D    24                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     MET D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     GLU D    30                                                      
REMARK 465     THR D    31                                                      
REMARK 465     ALA D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     ALA D    34                                                      
REMARK 465     LYS D    35                                                      
REMARK 465     PHE D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     ARG D    38                                                      
REMARK 465     GLN D    39                                                      
REMARK 465     HIS D    40                                                      
REMARK 465     MET D    41                                                      
REMARK 465     ASP D    42                                                      
REMARK 465     SER D    43                                                      
REMARK 465     PRO D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     GLY D    47                                                      
REMARK 465     THR D    48                                                      
REMARK 465     ASP D    49                                                      
REMARK 465     ASP D    50                                                      
REMARK 465     ASP D    51                                                      
REMARK 465     ASP D    52                                                      
REMARK 465     LYS D    53                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     MET D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     ALA D    58                                                      
REMARK 465     PRO D    59                                                      
REMARK 465     SER D    60                                                      
REMARK 465     PHE D    61                                                      
REMARK 465     ASN D    62                                                      
REMARK 465     VAL D    63                                                      
REMARK 465     ASP D    64                                                      
REMARK 465     PRO D    65                                                      
REMARK 465     LEU D    66                                                      
REMARK 465     GLU D    67                                                      
REMARK 465     GLN D    68                                                      
REMARK 465     PRO D    69                                                      
REMARK 465     ALA D    70                                                      
REMARK 465     GLU D    71                                                      
REMARK 465     PRO D    72                                                      
REMARK 465     SER D    73                                                      
REMARK 465     LYS D    74                                                      
REMARK 465     LEU D    75                                                      
REMARK 465     ALA D    76                                                      
REMARK 465     LYS D    77                                                      
REMARK 465     LYS D    78                                                      
REMARK 465     LEU D    79                                                      
REMARK 465     ARG D    80                                                      
REMARK 465     ALA D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     PRO D    83                                                      
REMARK 465     SER D   270                                                      
REMARK 465     ASN D   271                                                      
REMARK 465     ALA D   272                                                      
REMARK 465     LEU D   273                                                      
REMARK 465     ASN D   274                                                      
REMARK 465     GLN D   275                                                      
REMARK 465     LEU D   276                                                      
REMARK 465     THR D   277                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 265    CG   CD   CE   NZ                                   
REMARK 470     LYS D 456    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B    84     OG1  THR B   264              1.99            
REMARK 500   O    PHE A   388     NH1  ARG A   393              2.10            
REMARK 500   O    ASP E   282     N    VAL E   285              2.14            
REMARK 500   O    HOH E   892     O    HOH E   939              2.15            
REMARK 500   O    HOH E   954     O    HOH E   956              2.16            
REMARK 500   OE1  GLU D   283     O    HOH D   801              2.17            
REMARK 500   O    HOH B   919     O    HOH B  1146              2.17            
REMARK 500   O    HOH D  1019     O    HOH D  1164              2.18            
REMARK 500   OD1  ASP A   379     O    HOH A   801              2.18            
REMARK 500   O    HOH B  1016     O    HOH B  1129              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  1097     O    HOH E   806     3775     2.19            
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      142.71   -174.07                                   
REMARK 500    ASP A 350     -159.23     65.59                                   
REMARK 500    GLU A 663       46.10   -104.87                                   
REMARK 500    ASP B  84      115.34     90.01                                   
REMARK 500    TRP B 216      146.36   -170.39                                   
REMARK 500    ASP B 350     -162.74     65.04                                   
REMARK 500    GLU B 663       43.38   -107.12                                   
REMARK 500    TRP E 216      140.14   -175.01                                   
REMARK 500    GLU E 283      -36.64    -32.44                                   
REMARK 500    ASP E 350     -157.09     62.54                                   
REMARK 500    LYS E 442     -100.10    -33.64                                   
REMARK 500    GLU E 663       45.25   -108.14                                   
REMARK 500    TRP D 216      147.32   -170.95                                   
REMARK 500    ASP D 350     -161.94     70.28                                   
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 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 550   OD1                                                    
REMARK 620 2 ASN A 577   OD1  87.6                                              
REMARK 620 3 GLU A 579   O   102.9  90.5                                        
REMARK 620 4 AUJ A 705   OAI 162.4  99.6  93.1                                  
REMARK 620 5 AUJ A 705   OAK  91.1 177.1  92.3  80.8                            
REMARK 620 6 HOH A 845   O    78.9  85.1 175.2  85.8  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 550   OD1                                                    
REMARK 620 2 ASN B 577   OD1  83.9                                              
REMARK 620 3 GLU B 579   O    96.3  86.9                                        
REMARK 620 4 TP9 B 704   O1A  90.5 174.0  91.5                                  
REMARK 620 5 TP9 B 704   O2B 164.6  99.4  98.9  86.5                            
REMARK 620 6 HOH B 897   O    83.2  87.2 174.1  94.4  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 550   OD1                                                    
REMARK 620 2 ASN E 577   OD1  84.3                                              
REMARK 620 3 GLU E 579   O   102.2  88.3                                        
REMARK 620 4 TP9 E 704   O2A  88.7 172.8  94.6                                  
REMARK 620 5 TP9 E 704   O3B 164.1  98.0  93.6  88.5                            
REMARK 620 6 HOH E 831   O    79.4  84.1 172.0  93.2  85.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 550   OD1                                                    
REMARK 620 2 ASN D 577   OD1  83.7                                              
REMARK 620 3 GLU D 579   O    95.8  86.2                                        
REMARK 620 4 TP9 D 704   O2A  91.5 174.8  92.3                                  
REMARK 620 5 HOH D 922   O    86.1  88.7 174.3  93.0                            
REMARK 620 6 TP9 D 704   O3B 168.1 102.1  94.9  83.0  83.7                      
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 PXD A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F50 A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AUJ A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PXD B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TP9 B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F50 B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PXD E 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD E 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TP9 E 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F50 E 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PXD D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TP9 D 704                 
DBREF  5WKC A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  5WKC B   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  5WKC E   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  5WKC D   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 5WKC MET A   11  UNP  P07342              INITIATING METHIONINE          
SEQADV 5WKC HIS A   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER A   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER A   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY A   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU A   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC VAL A   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO A   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG A   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY A   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER A   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY A   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET A   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS A   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU A   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR A   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA A   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA A   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA A   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS A   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PHE A   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU A   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG A   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLN A   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS A   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET A   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER A   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO A   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU A   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY A   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR A   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP A   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS A   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA A   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET A   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY A   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER A   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET B   11  UNP  P07342              INITIATING METHIONINE          
SEQADV 5WKC HIS B   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER B   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER B   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY B   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU B   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC VAL B   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO B   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG B   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY B   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER B   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY B   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET B   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS B   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU B   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR B   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA B   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA B   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA B   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS B   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PHE B   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU B   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG B   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLN B   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS B   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET B   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER B   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO B   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU B   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY B   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR B   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP B   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS B   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA B   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET B   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY B   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER B   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET E   11  UNP  P07342              INITIATING METHIONINE          
SEQADV 5WKC HIS E   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER E   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER E   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY E   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU E   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC VAL E   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO E   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG E   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY E   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER E   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY E   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET E   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS E   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU E   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR E   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA E   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA E   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA E   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS E   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PHE E   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU E   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG E   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLN E   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS E   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET E   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER E   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO E   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU E   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY E   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR E   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP E   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS E   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA E   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET E   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY E   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER E   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET D   11  UNP  P07342              INITIATING METHIONINE          
SEQADV 5WKC HIS D   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER D   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER D   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY D   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU D   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC VAL D   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO D   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG D   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY D   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER D   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY D   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET D   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS D   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU D   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR D   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA D   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA D   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA D   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS D   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PHE D   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLU D   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ARG D   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLN D   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC HIS D   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET D   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER D   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC PRO D   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LEU D   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY D   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC THR D   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ASP D   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC LYS D   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC ALA D   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC MET D   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC GLY D   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5WKC SER D   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                                                          
SEQRES   1 E  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 E  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 E  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 E  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 E  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 E  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 E  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 E  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 E  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 E  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 E  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 E  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 E  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 E  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 E  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 E  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 E  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 E  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 E  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 E  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 E  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 E  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 E  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 E  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 E  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 E  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 E  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 E  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 E  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 E  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 E  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 E  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 E  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 E  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 E  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 E  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 E  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 E  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 E  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 E  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 E  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 E  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 E  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 E  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 E  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 E  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 E  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 E  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 E  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 E  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 E  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 E  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 E  677  HIS                                                          
SEQRES   1 D  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 D  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 D  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 D  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 D  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 D  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 D  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 D  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 D  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 D  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 D  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 D  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 D  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 D  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 D  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 D  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 D  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 D  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 D  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 D  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 D  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 D  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 D  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 D  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 D  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 D  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 D  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 D  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 D  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 D  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 D  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 D  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 D  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 D  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 D  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 D  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 D  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 D  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN SME TRP ALA          
SEQRES  39 D  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 D  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 D  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 D  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 D  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 D  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 D  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 D  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 D  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 D  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 D  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 D  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 D  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 D  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 D  677  HIS                                                          
MODRES 5WKC SME D  502  MET  MODIFIED RESIDUE                                   
HET    SME  D 502       9                                                       
HET     MG  A 701       1                                                       
HET    PXD  A 702      32                                                       
HET    FAD  A 703      53                                                       
HET    F50  A 704       5                                                       
HET    AUJ  A 705      31                                                       
HET     MG  B 701       1                                                       
HET    PXD  B 702      32                                                       
HET    FAD  B 703      53                                                       
HET    TP9  B 704      25                                                       
HET    F50  B 705       5                                                       
HET     MG  E 701       1                                                       
HET    PXD  E 702      32                                                       
HET    FAD  E 703      53                                                       
HET    TP9  E 704      25                                                       
HET    F50  E 705       5                                                       
HET     MG  D 701       1                                                       
HET    PXD  D 702      32                                                       
HET    FAD  D 703      53                                                       
HET    TP9  D 704      25                                                       
HETNAM     SME METHIONINE SULFOXIDE                                             
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PXD 2-(2,2-DIFLUOROETHOXY)-N-(5,8-DIMETHOXY[1,2,                     
HETNAM   2 PXD  4]TRIAZOLO[1,5-C]PYRIMIDIN-2-YL)-6-(TRIFLUOROMETHYL)            
HETNAM   3 PXD  BENZENESULFONAMIDE                                              
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     F50 ETHANEPEROXOIC ACID                                              
HETNAM     AUJ 2-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-2-               
HETNAM   2 AUJ  [(1~{S})-1-(DIOXIDANYL)-1-OXIDANYL-ETHYL]-4-METHYL-1,           
HETNAM   3 AUJ  3-THIAZOL-5-YL]ETHYL PHOSPHONO HYDROGEN PHOSPHATE               
HETNAM     TP9 (3Z)-4-{[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]AMINO}-          
HETNAM   2 TP9  3-MERCAPTOPENT-3-EN-1-YL TRIHYDROGEN DIPHOSPHATE                
HETSYN     PXD PENOXSULAM                                                       
FORMUL   4  SME    C5 H11 N O3 S                                                
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   6  PXD    4(C16 H14 F5 N5 O5 S)                                        
FORMUL   7  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   8  F50    3(C2 H4 O3)                                                  
FORMUL   9  AUJ    C14 H23 N4 O10 P2 S                                          
FORMUL  13  TP9    3(C11 H18 N4 O7 P2 S 2-)                                     
FORMUL  24  HOH   *1172(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 PRO A  263  THR A  267  5                                   5    
HELIX   13 AB4 GLN A  281  ALA A  299  1                                  19    
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 ALA A  389  GLU A  398  1                                  10    
HELIX   20 AC2 SER A  409  ILE A  413  5                                   5    
HELIX   21 AC3 ASP A  426  MET A  435  1                                  10    
HELIX   22 AC4 SER A  436  ILE A  438  5                                   3    
HELIX   23 AC5 ARG A  444  TYR A  458  1                                  15    
HELIX   24 AC6 LYS A  472  ASP A  486  1                                  15    
HELIX   25 AC7 GLY A  498  TRP A  508  1                                  11    
HELIX   26 AC8 TYR A  527  LYS A  539  1                                  13    
HELIX   27 AC9 ASP A  550  LEU A  557  1                                   8    
HELIX   28 AD1 GLU A  559  GLY A  567  1                                   9    
HELIX   29 AD2 GLN A  580  TYR A  591  1                                  12    
HELIX   30 AD3 ASP A  604  GLY A  613  1                                  10    
HELIX   31 AD4 LYS A  621  GLU A  623  5                                   3    
HELIX   32 AD5 GLU A  624  THR A  635  1                                  12    
HELIX   33 AD6 ASP A  668  GLY A  684  1                                  17    
HELIX   34 AD7 THR B   93  GLN B  105  1                                  13    
HELIX   35 AD8 ILE B  118  ILE B  125  1                                   8    
HELIX   36 AD9 HIS B  138  GLY B  154  1                                  17    
HELIX   37 AE1 GLY B  164  ASN B  169  1                                   6    
HELIX   38 AE2 VAL B  170  GLY B  181  1                                  12    
HELIX   39 AE3 ASP B  205  SER B  210  1                                   6    
HELIX   40 AE4 ARG B  211  THR B  214  5                                   4    
HELIX   41 AE5 SER B  222  GLU B  224  5                                   3    
HELIX   42 AE6 GLU B  225  SER B  239  1                                  15    
HELIX   43 AE7 LYS B  251  ALA B  256  1                                   6    
HELIX   44 AE8 LYS B  265  THR B  267  5                                   3    
HELIX   45 AE9 SER B  278  ALA B  299  1                                  22    
HELIX   46 AF1 ALA B  308  HIS B  313  5                                   6    
HELIX   47 AF2 ASP B  315  GLN B  328  1                                  14    
HELIX   48 AF3 LEU B  335  LEU B  338  5                                   4    
HELIX   49 AF4 CYS B  357  ALA B  367  1                                  11    
HELIX   50 AF5 ASP B  378  GLY B  383  1                                   6    
HELIX   51 AF6 ALA B  389  GLU B  398  1                                  10    
HELIX   52 AF7 SER B  409  ILE B  413  5                                   5    
HELIX   53 AF8 ASP B  426  MET B  435  1                                  10    
HELIX   54 AF9 SER B  436  ILE B  438  5                                   3    
HELIX   55 AG1 ARG B  444  TYR B  458  1                                  15    
HELIX   56 AG2 LYS B  472  ASP B  486  1                                  15    
HELIX   57 AG3 GLY B  498  TRP B  508  1                                  11    
HELIX   58 AG4 TYR B  527  LYS B  539  1                                  13    
HELIX   59 AG5 ASP B  550  LEU B  557  1                                   8    
HELIX   60 AG6 GLU B  559  GLY B  567  1                                   9    
HELIX   61 AG7 GLN B  580  TYR B  591  1                                  12    
HELIX   62 AG8 ASP B  604  MET B  612  1                                   9    
HELIX   63 AG9 LYS B  621  GLU B  623  5                                   3    
HELIX   64 AH1 GLU B  624  THR B  635  1                                  12    
HELIX   65 AH2 ASP B  668  THR B  683  1                                  16    
HELIX   66 AH3 THR E   93  GLN E  105  1                                  13    
HELIX   67 AH4 GLY E  115  ALA E  117  5                                   3    
HELIX   68 AH5 ILE E  118  ILE E  125  1                                   8    
HELIX   69 AH6 HIS E  138  GLY E  154  1                                  17    
HELIX   70 AH7 GLY E  164  ASN E  169  1                                   6    
HELIX   71 AH8 VAL E  170  GLY E  181  1                                  12    
HELIX   72 AH9 ASP E  205  SER E  210  1                                   6    
HELIX   73 AI1 ARG E  211  THR E  214  5                                   4    
HELIX   74 AI2 SER E  222  GLU E  224  5                                   3    
HELIX   75 AI3 GLU E  225  THR E  238  1                                  14    
HELIX   76 AI4 LYS E  251  ALA E  256  1                                   6    
HELIX   77 AI5 PRO E  263  LEU E  268  5                                   6    
HELIX   78 AI6 GLU E  283  ASN E  297  1                                  15    
HELIX   79 AI7 ALA E  308  HIS E  313  5                                   6    
HELIX   80 AI8 ASP E  315  GLN E  328  1                                  14    
HELIX   81 AI9 LEU E  335  LEU E  338  5                                   4    
HELIX   82 AJ1 CYS E  357  ALA E  367  1                                  11    
HELIX   83 AJ2 ASP E  378  GLY E  383  1                                   6    
HELIX   84 AJ3 ASN E  384  PHE E  388  5                                   5    
HELIX   85 AJ4 ALA E  389  GLU E  398  1                                  10    
HELIX   86 AJ5 SER E  409  ILE E  413  5                                   5    
HELIX   87 AJ6 ASP E  426  MET E  435  1                                  10    
HELIX   88 AJ7 SER E  436  ILE E  438  5                                   3    
HELIX   89 AJ8 ARG E  444  TYR E  458  1                                  15    
HELIX   90 AJ9 LYS E  472  ASP E  486  1                                  15    
HELIX   91 AK1 GLY E  498  TRP E  508  1                                  11    
HELIX   92 AK2 TYR E  527  LYS E  539  1                                  13    
HELIX   93 AK3 ASP E  550  LEU E  557  1                                   8    
HELIX   94 AK4 GLU E  559  GLY E  567  1                                   9    
HELIX   95 AK5 GLN E  580  TYR E  591  1                                  12    
HELIX   96 AK6 ASP E  604  GLY E  613  1                                  10    
HELIX   97 AK7 LYS E  621  GLU E  623  5                                   3    
HELIX   98 AK8 GLU E  624  THR E  635  1                                  12    
HELIX   99 AK9 ASP E  668  THR E  683  1                                  16    
HELIX  100 AL1 THR D   93  GLN D  105  1                                  13    
HELIX  101 AL2 ILE D  118  ILE D  125  1                                   8    
HELIX  102 AL3 HIS D  138  GLY D  154  1                                  17    
HELIX  103 AL4 GLY D  164  ASN D  169  1                                   6    
HELIX  104 AL5 VAL D  170  GLY D  181  1                                  12    
HELIX  105 AL6 PRO D  192  ILE D  196  5                                   5    
HELIX  106 AL7 ASP D  205  SER D  210  1                                   6    
HELIX  107 AL8 ARG D  211  THR D  214  5                                   4    
HELIX  108 AL9 SER D  222  GLU D  224  5                                   3    
HELIX  109 AM1 GLU D  225  SER D  239  1                                  15    
HELIX  110 AM2 LYS D  251  ALA D  256  1                                   6    
HELIX  111 AM3 LYS D  265  THR D  267  5                                   3    
HELIX  112 AM4 ARG D  279  ALA D  299  1                                  21    
HELIX  113 AM5 ALA D  308  HIS D  313  5                                   6    
HELIX  114 AM6 ASP D  315  GLN D  328  1                                  14    
HELIX  115 AM7 LEU D  335  LEU D  338  5                                   4    
HELIX  116 AM8 CYS D  357  ALA D  367  1                                  11    
HELIX  117 AM9 ASP D  378  GLY D  383  1                                   6    
HELIX  118 AN1 ASN D  384  PHE D  388  5                                   5    
HELIX  119 AN2 ALA D  389  GLU D  398  1                                  10    
HELIX  120 AN3 SER D  409  ILE D  413  5                                   5    
HELIX  121 AN4 ASP D  426  MET D  435  1                                  10    
HELIX  122 AN5 SER D  436  ILE D  438  5                                   3    
HELIX  123 AN6 ARG D  444  TYR D  458  1                                  15    
HELIX  124 AN7 LYS D  472  ASP D  486  1                                  15    
HELIX  125 AN8 GLY D  498  TRP D  508  1                                  11    
HELIX  126 AN9 TYR D  527  LYS D  539  1                                  13    
HELIX  127 AO1 ASP D  550  LEU D  557  1                                   8    
HELIX  128 AO2 GLU D  559  GLY D  567  1                                   9    
HELIX  129 AO3 GLN D  580  TYR D  591  1                                  12    
HELIX  130 AO4 ASP D  604  MET D  612  1                                   9    
HELIX  131 AO5 LYS D  621  GLU D  623  5                                   3    
HELIX  132 AO6 GLU D  624  THR D  635  1                                  12    
HELIX  133 AO7 ASP D  668  THR D  683  1                                  16    
SHEET    1 AA1 6 ASN A 132  VAL A 134  0                                        
SHEET    2 AA1 6 THR A 109  TYR A 113  1  N  VAL A 110   O  ASN A 132           
SHEET    3 AA1 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4 AA1 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5 AA1 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6 AA1 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1 AA2 6 SER A 348  MET A 351  0                                        
SHEET    2 AA2 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3 AA2 6 PRO A 302  VAL A 306  1  N  VAL A 306   O  THR A 332           
SHEET    4 AA2 6 LEU A 369  VAL A 373  1  O  VAL A 373   N  TYR A 305           
SHEET    5 AA2 6 GLY A 402  GLU A 407  1  O  PHE A 406   N  ALA A 372           
SHEET    6 AA2 6 ILE A 421  GLU A 424  1  O  VAL A 423   N  HIS A 405           
SHEET    1 AA3 6 PHE A 516  ILE A 517  0                                        
SHEET    2 AA3 6 VAL A 491  THR A 495  1  N  VAL A 493   O  ILE A 517           
SHEET    3 AA3 6 LEU A 543  GLY A 549  1  O  ILE A 547   N  THR A 494           
SHEET    4 AA3 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 548           
SHEET    5 AA3 6 VAL A 639  GLU A 644  1  O  LEU A 641   N  ILE A 572           
SHEET    6 AA3 6 LYS A 615  VAL A 619  1  N  LEU A 617   O  GLU A 642           
SHEET    1 AA4 2 MET B  85  ASP B  86  0                                        
SHEET    2 AA4 2 ILE B 262  PRO B 263 -1  O  ILE B 262   N  ASP B  86           
SHEET    1 AA5 6 ASN B 132  VAL B 134  0                                        
SHEET    2 AA5 6 THR B 109  TYR B 113  1  N  VAL B 110   O  VAL B 134           
SHEET    3 AA5 6 GLY B 157  VAL B 161  1  O  VAL B 158   N  PHE B 111           
SHEET    4 AA5 6 MET B 184  GLN B 190  1  O  PHE B 187   N  VAL B 159           
SHEET    5 AA5 6 PRO B 244  PRO B 250  1  O  LEU B 249   N  THR B 188           
SHEET    6 AA5 6 TRP B 216  MET B 219  1  N  VAL B 218   O  ASP B 248           
SHEET    1 AA6 6 SER B 348  MET B 351  0                                        
SHEET    2 AA6 6 VAL B 331  THR B 333  1  N  VAL B 331   O  LEU B 349           
SHEET    3 AA6 6 PRO B 302  VAL B 306  1  N  LEU B 304   O  THR B 332           
SHEET    4 AA6 6 LEU B 369  VAL B 373  1  O  VAL B 373   N  TYR B 305           
SHEET    5 AA6 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6 AA6 6 ILE B 421  GLU B 424  1  O  VAL B 423   N  HIS B 405           
SHEET    1 AA7 6 PHE B 516  ILE B 517  0                                        
SHEET    2 AA7 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3 AA7 6 LEU B 543  GLY B 549  1  O  ILE B 545   N  ILE B 492           
SHEET    4 AA7 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 548           
SHEET    5 AA7 6 VAL B 639  GLU B 644  1  O  LEU B 641   N  ILE B 572           
SHEET    6 AA7 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  LEU B 640           
SHEET    1 AA8 6 ASN E 132  VAL E 134  0                                        
SHEET    2 AA8 6 THR E 109  GLY E 112  1  N  VAL E 110   O  ASN E 132           
SHEET    3 AA8 6 GLY E 157  VAL E 161  1  O  VAL E 158   N  PHE E 111           
SHEET    4 AA8 6 MET E 184  GLN E 190  1  O  PHE E 187   N  VAL E 159           
SHEET    5 AA8 6 PRO E 244  PRO E 250  1  O  VAL E 245   N  VAL E 186           
SHEET    6 AA8 6 TRP E 216  MET E 219  1  N  VAL E 218   O  ASP E 248           
SHEET    1 AA9 6 SER E 348  MET E 351  0                                        
SHEET    2 AA9 6 VAL E 331  THR E 333  1  N  VAL E 331   O  LEU E 349           
SHEET    3 AA9 6 PRO E 302  VAL E 306  1  N  LEU E 304   O  THR E 332           
SHEET    4 AA9 6 LEU E 369  VAL E 373  1  O  VAL E 373   N  TYR E 305           
SHEET    5 AA9 6 GLY E 402  GLU E 407  1  O  PHE E 406   N  ALA E 372           
SHEET    6 AA9 6 ILE E 421  GLU E 424  1  O  VAL E 423   N  HIS E 405           
SHEET    1 AB1 6 PHE E 516  ILE E 517  0                                        
SHEET    2 AB1 6 VAL E 491  THR E 495  1  N  VAL E 493   O  ILE E 517           
SHEET    3 AB1 6 LEU E 543  GLY E 549  1  O  ILE E 545   N  ILE E 492           
SHEET    4 AB1 6 LYS E 571  ASN E 576  1  O  LEU E 573   N  ASP E 546           
SHEET    5 AB1 6 VAL E 639  GLU E 644  1  O  LEU E 641   N  ILE E 572           
SHEET    6 AB1 6 LYS E 615  VAL E 619  1  N  LEU E 617   O  GLU E 642           
SHEET    1 AB2 2 MET D  85  ASP D  86  0                                        
SHEET    2 AB2 2 ILE D 262  PRO D 263 -1  O  ILE D 262   N  ASP D  86           
SHEET    1 AB3 6 ASN D 132  VAL D 134  0                                        
SHEET    2 AB3 6 THR D 109  GLY D 112  1  N  VAL D 110   O  VAL D 134           
SHEET    3 AB3 6 GLY D 157  VAL D 161  1  O  VAL D 158   N  PHE D 111           
SHEET    4 AB3 6 MET D 184  GLN D 190  1  O  PHE D 187   N  VAL D 159           
SHEET    5 AB3 6 PRO D 244  PRO D 250  1  O  LEU D 249   N  THR D 188           
SHEET    6 AB3 6 TRP D 216  MET D 219  1  N  VAL D 218   O  ASP D 248           
SHEET    1 AB4 6 SER D 348  MET D 351  0                                        
SHEET    2 AB4 6 VAL D 331  THR D 333  1  N  VAL D 331   O  LEU D 349           
SHEET    3 AB4 6 PRO D 302  VAL D 306  1  N  VAL D 306   O  THR D 332           
SHEET    4 AB4 6 LEU D 369  VAL D 373  1  O  VAL D 373   N  TYR D 305           
SHEET    5 AB4 6 GLY D 402  GLU D 407  1  O  ILE D 404   N  ALA D 372           
SHEET    6 AB4 6 ILE D 421  GLU D 424  1  O  VAL D 423   N  HIS D 405           
SHEET    1 AB5 6 PHE D 516  ILE D 517  0                                        
SHEET    2 AB5 6 VAL D 491  THR D 495  1  N  VAL D 493   O  ILE D 517           
SHEET    3 AB5 6 LEU D 543  GLY D 549  1  O  ILE D 545   N  ILE D 492           
SHEET    4 AB5 6 LYS D 571  ASN D 576  1  O  LEU D 573   N  ASP D 548           
SHEET    5 AB5 6 VAL D 639  GLU D 644  1  O  LEU D 641   N  ILE D 572           
SHEET    6 AB5 6 LYS D 615  VAL D 619  1  N  LEU D 617   O  GLU D 642           
LINK         OD1 ASP A 550                MG    MG A 701     1555   1555  2.06  
LINK         OD1 ASN A 577                MG    MG A 701     1555   1555  2.07  
LINK         O   GLU A 579                MG    MG A 701     1555   1555  2.18  
LINK         OD1 ASP B 550                MG    MG B 701     1555   1555  2.14  
LINK         OD1 ASN B 577                MG    MG B 701     1555   1555  2.19  
LINK         O   GLU B 579                MG    MG B 701     1555   1555  2.20  
LINK         OD1 ASP E 550                MG    MG E 701     1555   1555  2.05  
LINK         OD1 ASN E 577                MG    MG E 701     1555   1555  2.16  
LINK         O   GLU E 579                MG    MG E 701     1555   1555  2.25  
LINK         C   GLN D 501                 N   SME D 502     1555   1555  1.33  
LINK         C   SME D 502                 N   TRP D 503     1555   1555  1.33  
LINK         OD1 ASP D 550                MG    MG D 701     1555   1555  2.10  
LINK         OD1 ASN D 577                MG    MG D 701     1555   1555  2.15  
LINK         O   GLU D 579                MG    MG D 701     1555   1555  2.22  
LINK        MG    MG A 701                 OAI AUJ A 705     1555   1555  2.26  
LINK        MG    MG A 701                 OAK AUJ A 705     1555   1555  2.10  
LINK        MG    MG A 701                 O   HOH A 845     1555   1555  2.16  
LINK        MG    MG B 701                 O1A TP9 B 704     1555   1555  2.09  
LINK        MG    MG B 701                 O2B TP9 B 704     1555   1555  2.16  
LINK        MG    MG B 701                 O   HOH B 897     1555   1555  2.14  
LINK        MG    MG E 701                 O2A TP9 E 704     1555   1555  2.07  
LINK        MG    MG E 701                 O3B TP9 E 704     1555   1555  2.18  
LINK        MG    MG E 701                 O   HOH E 831     1555   1555  2.09  
LINK        MG    MG D 701                 O2A TP9 D 704     1555   1555  2.09  
LINK        MG    MG D 701                 O   HOH D 922     1555   1555  2.11  
LINK        MG    MG D 701                 O3B TP9 D 704     1555   1555  2.03  
CISPEP   1 LEU A  652    PRO A  653          0         2.09                     
CISPEP   2 LEU B  652    PRO B  653          0         2.28                     
CISPEP   3 LEU E  652    PRO E  653          0        -0.31                     
CISPEP   4 LEU D  652    PRO D  653          0         1.46                     
SITE     1 AC1  5 ASP A 550  ASN A 577  GLU A 579  AUJ A 705                    
SITE     2 AC1  5 HOH A 845                                                     
SITE     1 AC2 15 MET A 354  ASP A 379  ARG A 380  MET A 582                    
SITE     2 AC2 15 VAL A 583  TRP A 586  FAD A 703  AUJ A 705                    
SITE     3 AC2 15 GLY D 116  ALA D 117  SER D 163  VAL D 191                    
SITE     4 AC2 15 PHE D 201  LYS D 251  HOH D 947                               
SITE     1 AC3 36 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 AC3 36 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 AC3 36 GLN A 336  LEU A 352  GLY A 353  MET A 354                    
SITE     4 AC3 36 HIS A 355  GLY A 374  ALA A 375  ARG A 376                    
SITE     5 AC3 36 ARG A 380  VAL A 381  GLU A 407  VAL A 408                    
SITE     6 AC3 36 ASN A 412  GLY A 425  ASP A 426  ALA A 427                    
SITE     7 AC3 36 GLN A 501  MET A 502  GLY A 520  GLY A 521                    
SITE     8 AC3 36 PXD A 702  HOH A 828  HOH A 831  HOH A 856                    
SITE     9 AC3 36 HOH A 863  HOH A 923  HOH A 937  PHE D 201                    
SITE     1 AC4  6 GLY A 115  GLY A 116  GLN A 202  MET D 582                    
SITE     2 AC4  6 PXD D 702  TP9 D 704                                          
SITE     1 AC5 26 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC5 26 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC5 26 ALA A 551  SER A 552  ASN A 577  GLU A 579                    
SITE     4 AC5 26 GLN A 580  GLY A 581  MET A 582  VAL A 583                    
SITE     5 AC5 26  MG A 701  PXD A 702  HOH A 845  TYR D 113                    
SITE     6 AC5 26 PRO D 114  GLY D 116  GLU D 139  PRO D 165                    
SITE     7 AC5 26 ASN D 169  GLN D 202                                          
SITE     1 AC6  5 ASP B 550  ASN B 577  GLU B 579  TP9 B 704                    
SITE     2 AC6  5 HOH B 897                                                     
SITE     1 AC7 16 MET B 354  ASP B 379  ARG B 380  MET B 582                    
SITE     2 AC7 16 VAL B 583  TRP B 586  FAD B 703  HOH B1001                    
SITE     3 AC7 16 HOH B1060  GLY E 116  ALA E 117  VAL E 191                    
SITE     4 AC7 16 PHE E 201  LYS E 251  F50 E 705  HOH E 804                    
SITE     1 AC8 34 ARG B 241  GLY B 307  ALA B 308  GLY B 309                    
SITE     2 AC8 34 ASN B 312  THR B 334  LEU B 335  GLN B 336                    
SITE     3 AC8 34 LEU B 352  GLY B 353  MET B 354  HIS B 355                    
SITE     4 AC8 34 GLY B 374  ALA B 375  ARG B 376  ARG B 380                    
SITE     5 AC8 34 VAL B 381  GLU B 407  VAL B 408  ASN B 412                    
SITE     6 AC8 34 GLY B 425  ASP B 426  ALA B 427  GLN B 501                    
SITE     7 AC8 34 MET B 502  GLY B 520  GLY B 521  PXD B 702                    
SITE     8 AC8 34 HOH B 852  HOH B 889  HOH B 946  HOH B 989                    
SITE     9 AC8 34 HOH B1050  PHE E 201                                          
SITE     1 AC9 24 VAL B 497  GLY B 498  GLN B 499  HIS B 500                    
SITE     2 AC9 24 GLY B 523  MET B 525  GLY B 549  ASP B 550                    
SITE     3 AC9 24 ALA B 551  SER B 552  ASN B 577  GLU B 579                    
SITE     4 AC9 24 GLN B 580  GLY B 581  MET B 582  VAL B 583                    
SITE     5 AC9 24  MG B 701  HOH B 897  TYR E 113  PRO E 114                    
SITE     6 AC9 24 GLU E 139  ASN E 169  GLN E 202  F50 E 705                    
SITE     1 AD1  6 GLY B 115  GLY B 116  GLN B 202  MET E 582                    
SITE     2 AD1  6 PXD E 702  TP9 E 704                                          
SITE     1 AD2  5 ASP E 550  ASN E 577  GLU E 579  TP9 E 704                    
SITE     2 AD2  5 HOH E 831                                                     
SITE     1 AD3 13 GLY B 116  ALA B 117  VAL B 191  PHE B 201                    
SITE     2 AD3 13 LYS B 251  F50 B 705  MET E 354  ASP E 379                    
SITE     3 AD3 13 ARG E 380  MET E 582  VAL E 583  TRP E 586                    
SITE     4 AD3 13 FAD E 703                                                     
SITE     1 AD4 35 PHE B 201  ASP E 180  ARG E 241  GLY E 307                    
SITE     2 AD4 35 ALA E 308  GLY E 309  ASN E 312  THR E 334                    
SITE     3 AD4 35 LEU E 335  GLN E 336  LEU E 352  GLY E 353                    
SITE     4 AD4 35 MET E 354  HIS E 355  GLY E 374  ALA E 375                    
SITE     5 AD4 35 ARG E 376  ARG E 380  VAL E 381  GLU E 407                    
SITE     6 AD4 35 VAL E 408  ASN E 412  GLY E 425  ASP E 426                    
SITE     7 AD4 35 ALA E 427  GLN E 501  MET E 502  GLY E 520                    
SITE     8 AD4 35 GLY E 521  PXD E 702  HOH E 809  HOH E 821                    
SITE     9 AD4 35 HOH E 835  HOH E 895  HOH E 918                               
SITE     1 AD5 24 PRO B 114  GLU B 139  PRO B 165  ASN B 169                    
SITE     2 AD5 24 GLN B 202  F50 B 705  VAL E 497  GLY E 498                    
SITE     3 AD5 24 GLN E 499  HIS E 500  GLY E 523  MET E 525                    
SITE     4 AD5 24 GLY E 549  ASP E 550  ALA E 551  SER E 552                    
SITE     5 AD5 24 ASN E 577  GLU E 579  GLN E 580  GLY E 581                    
SITE     6 AD5 24 MET E 582  VAL E 583   MG E 701  HOH E 831                    
SITE     1 AD6  5 MET B 582  PXD B 702  TP9 B 704  GLY E 116                    
SITE     2 AD6  5 GLN E 202                                                     
SITE     1 AD7  5 ASP D 550  ASN D 577  GLU D 579  TP9 D 704                    
SITE     2 AD7  5 HOH D 922                                                     
SITE     1 AD8 15 GLY A 116  ALA A 117  VAL A 191  PHE A 201                    
SITE     2 AD8 15 LYS A 251  F50 A 704  HOH A 822  MET D 354                    
SITE     3 AD8 15 ASP D 379  ARG D 380  MET D 582  VAL D 583                    
SITE     4 AD8 15 TRP D 586  FAD D 703  HOH D1066                               
SITE     1 AD9 36 PHE A 201  ASP D 180  ARG D 241  GLY D 307                    
SITE     2 AD9 36 ALA D 308  GLY D 309  ASN D 312  THR D 334                    
SITE     3 AD9 36 LEU D 335  GLN D 336  LEU D 352  GLY D 353                    
SITE     4 AD9 36 MET D 354  HIS D 355  GLY D 374  ALA D 375                    
SITE     5 AD9 36 ARG D 376  ARG D 380  VAL D 381  GLU D 407                    
SITE     6 AD9 36 VAL D 408  ASN D 412  GLY D 425  ASP D 426                    
SITE     7 AD9 36 ALA D 427  GLN D 501  SME D 502  GLY D 520                    
SITE     8 AD9 36 GLY D 521  MET D 582  PXD D 702  HOH D 815                    
SITE     9 AD9 36 HOH D 877  HOH D 890  HOH D 944  HOH D1005                    
SITE     1 AE1 25 TYR A 113  PRO A 114  GLU A 139  PRO A 165                    
SITE     2 AE1 25 ASN A 169  GLN A 202  F50 A 704  VAL D 497                    
SITE     3 AE1 25 GLY D 498  GLN D 499  HIS D 500  GLY D 523                    
SITE     4 AE1 25 MET D 525  GLY D 549  ASP D 550  ALA D 551                    
SITE     5 AE1 25 SER D 552  ASN D 577  GLU D 579  GLN D 580                    
SITE     6 AE1 25 GLY D 581  MET D 582  VAL D 583   MG D 701                    
SITE     7 AE1 25 HOH D 922                                                     
CRYST1  218.213  218.213  361.940  90.00  90.00  90.00 I 4 2 2      48          
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      0.004583  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004583  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002763        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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