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Database: PDB
Entry: 4UEK
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Original site: 4UEK 
HEADER    OXIDOREDUCTASE                          18-DEC-14   4UEK              
TITLE     GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM E. COLI WITH              
TITLE    2 TRIS WITHIN THE ACTIVE SITE.                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.1.251;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BENAVENTE,M.ESTEBAN-TORRES,G.W.KOHRING,A.CORTES-CABRERA,F.GAGO,     
AUTHOR   2 I.ACEBRON,B.DE LAS RIVAS,R.MUNOZ,J.M.MANCHENO                        
REVDAT   1   15-JUL-15 4UEK    0                                                
JRNL        AUTH   R.BENAVENTE,M.ESTEBAN-TORRES,G.W.KOHRING,A.CORTES-CABRERA,   
JRNL        AUTH 2 P.A.SANCHEZ-MURCIA,F.GAGO,I.ACEBRON,B.DE LAS RIVAS,R.MUNOZ,  
JRNL        AUTH 3 J.M.MANCHENO                                                 
JRNL        TITL   ENANTIOSELECTIVE OXIDATION OF GALACTITOL 1-PHOSPHATE BY      
JRNL        TITL 2 GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE FROM ESCHERICHIA      
JRNL        TITL 3 COLI                                                         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  1540 2015              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   26143925                                                     
JRNL        DOI    10.1107/S1399004715009281                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.900                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.455                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.31                          
REMARK   3   NUMBER OF REFLECTIONS             : 49078                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2047                          
REMARK   3   R VALUE            (WORKING SET) : 0.2018                          
REMARK   3   FREE R VALUE                     : 0.2577                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2487                            
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 45.4677 -  4.9774    0.99     2930   179  0.1904 0.2204        
REMARK   3     2  4.9774 -  3.9514    1.00     2914   151  0.1601 0.2145        
REMARK   3     3  3.9514 -  3.4521    0.99     2887   152  0.1819 0.2572        
REMARK   3     4  3.4521 -  3.1366    1.00     2876   170  0.2010 0.2206        
REMARK   3     5  3.1366 -  2.9118    0.99     2891   148  0.2173 0.3158        
REMARK   3     6  2.9118 -  2.7401    1.00     2858   153  0.2183 0.2777        
REMARK   3     7  2.7401 -  2.6029    1.00     2897   173  0.2146 0.2769        
REMARK   3     8  2.6029 -  2.4896    0.99     2881   162  0.2126 0.2724        
REMARK   3     9  2.4896 -  2.3938    0.99     2832   146  0.2151 0.2646        
REMARK   3    10  2.3938 -  2.3112    0.99     2917   136  0.2042 0.2389        
REMARK   3    11  2.3112 -  2.2389    1.00     2876   155  0.2007 0.2755        
REMARK   3    12  2.2389 -  2.1749    1.00     2862   136  0.2077 0.2644        
REMARK   3    13  2.1749 -  2.1177    0.92     2651   140  0.2220 0.3280        
REMARK   3    14  2.1177 -  2.0660    0.83     2399   120  0.2333 0.2618        
REMARK   3    15  2.0660 -  2.0190    0.73     2095   115  0.2429 0.3008        
REMARK   3    16  2.0190 -  1.9761    0.65     1852    97  0.2396 0.3166        
REMARK   3    17  1.9761 -  1.9365    0.56     1610    77  0.2367 0.2911        
REMARK   3    18  1.9365 -  1.9000    0.47     1363    77  0.2337 0.2824        
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)     : 0.23             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.11            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.04                          
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           5396                                  
REMARK   3   ANGLE     :  1.159           7322                                  
REMARK   3   CHIRALITY :  0.046            840                                  
REMARK   3   PLANARITY :  0.006            944                                  
REMARK   3   DIHEDRAL  : 13.869           1970                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID    1  THROUGH   46 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5982  -6.6928   2.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1307 T22:   0.1455                                     
REMARK   3      T33:   0.1577 T12:   0.0162                                     
REMARK   3      T13:   0.0279 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6828 L22:   3.1267                                     
REMARK   3      L33:   3.0831 L12:  -0.8801                                     
REMARK   3      L13:   0.9568 L23:  -2.0154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0626 S12:   0.0692 S13:  -0.2352                       
REMARK   3      S21:  -0.2256 S22:   0.0522 S23:   0.2185                       
REMARK   3      S31:   0.3749 S32:   0.0588 S33:  -0.1297                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID   47  THROUGH  102 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0808   3.5765   5.0837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1234 T22:   0.1201                                     
REMARK   3      T33:   0.0720 T12:   0.0022                                     
REMARK   3      T13:  -0.0056 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5648 L22:   0.5530                                     
REMARK   3      L33:   1.4838 L12:  -0.4324                                     
REMARK   3      L13:  -0.4021 L23:   0.0748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0447 S12:  -0.0644 S13:   0.0303                       
REMARK   3      S21:   0.0392 S22:  -0.0442 S23:   0.0583                       
REMARK   3      S31:  -0.0406 S32:   0.0406 S33:  -0.0157                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  103  THROUGH  194 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8043   4.1196  18.2105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0838 T22:   0.1015                                     
REMARK   3      T33:   0.1213 T12:   0.0289                                     
REMARK   3      T13:   0.0073 T23:   0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6272 L22:   0.0990                                     
REMARK   3      L33:   2.8992 L12:   0.3600                                     
REMARK   3      L13:  -0.0766 L23:   0.1188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0183 S12:  -0.0548 S13:   0.0345                       
REMARK   3      S21:  -0.0406 S22:  -0.0222 S23:   0.0228                       
REMARK   3      S31:  -0.0790 S32:   0.1279 S33:   0.0023                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  195  THROUGH  216 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9043  -4.6318  36.5299              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1175 T22:   0.3196                                     
REMARK   3      T33:   0.1798 T12:   0.0671                                     
REMARK   3      T13:   0.0111 T23:   0.0474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9788 L22:   6.8187                                     
REMARK   3      L33:   5.2865 L12:   4.5733                                     
REMARK   3      L13:  -1.4818 L23:  -4.3222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1571 S12:  -0.2859 S13:  -0.4137                       
REMARK   3      S21:   0.0864 S22:  -0.1315 S23:   0.0162                       
REMARK   3      S31:   0.0243 S32:   0.2769 S33:  -0.0052                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  217  THROUGH  285 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4131  -4.5171  36.3605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.1605                                     
REMARK   3      T33:   0.1492 T12:   0.0210                                     
REMARK   3      T13:   0.0032 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5151 L22:   2.3122                                     
REMARK   3      L33:   1.6548 L12:   0.4056                                     
REMARK   3      L13:   0.0578 L23:   0.6075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0678 S12:  -0.2173 S13:  -0.3097                       
REMARK   3      S21:   0.1165 S22:  -0.0369 S23:  -0.0261                       
REMARK   3      S31:   0.1583 S32:   0.0751 S33:  -0.0422                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  286  THROUGH  322 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5373   7.2225  17.3733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1192 T22:   0.1655                                     
REMARK   3      T33:   0.0543 T12:   0.0102                                     
REMARK   3      T13:   0.0231 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0632 L22:   2.7695                                     
REMARK   3      L33:   2.4699 L12:  -0.9080                                     
REMARK   3      L13:  -0.3670 L23:   0.8412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0299 S12:   0.1195 S13:   0.1312                       
REMARK   3      S21:  -0.0030 S22:  -0.0737 S23:  -0.0954                       
REMARK   3      S31:  -0.1369 S32:   0.1065 S33:   0.0817                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  323  THROUGH  346 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8953 -12.0712  13.0152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2151 T22:   0.1799                                     
REMARK   3      T33:   0.2013 T12:   0.0483                                     
REMARK   3      T13:  -0.0077 T23:   0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8286 L22:   5.6986                                     
REMARK   3      L33:   1.8017 L12:  -0.0642                                     
REMARK   3      L13:   0.8627 L23:   0.2195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0830 S12:  -0.1637 S13:  -0.6597                       
REMARK   3      S21:   0.4111 S22:  -0.0004 S23:  -0.2976                       
REMARK   3      S31:   0.3869 S32:  -0.0031 S33:   0.0668                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID    1  THROUGH   46 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6728  -6.7249  59.3775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1487 T22:   0.2865                                     
REMARK   3      T33:   0.2205 T12:  -0.0092                                     
REMARK   3      T13:   0.0098 T23:   0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0104 L22:   4.0741                                     
REMARK   3      L33:   2.0503 L12:   1.3202                                     
REMARK   3      L13:   1.3174 L23:   1.2607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0872 S12:  -0.2344 S13:  -0.3439                       
REMARK   3      S21:   0.2421 S22:   0.1262 S23:  -0.1472                       
REMARK   3      S31:   0.1093 S32:  -0.1337 S33:  -0.2048                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   47  THROUGH  102 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1141   3.4553  56.1757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1609 T22:   0.1995                                     
REMARK   3      T33:   0.0950 T12:   0.0109                                     
REMARK   3      T13:   0.0047 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1770 L22:   0.7334                                     
REMARK   3      L33:   1.5030 L12:   0.3928                                     
REMARK   3      L13:   0.5999 L23:  -0.0768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:  -0.2483 S13:   0.0456                       
REMARK   3      S21:   0.0038 S22:   0.0759 S23:   0.0012                       
REMARK   3      S31:  -0.1058 S32:  -0.0839 S33:  -0.0656                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  103  THROUGH  136 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9426   3.0638  56.5342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1459 T22:   0.2188                                     
REMARK   3      T33:   0.1100 T12:   0.0058                                     
REMARK   3      T13:   0.0352 T23:  -0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8300 L22:   2.9607                                     
REMARK   3      L33:   3.2286 L12:   0.7225                                     
REMARK   3      L13:  -0.1139 L23:  -0.8304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1083 S12:  -0.5407 S13:  -0.1259                       
REMARK   3      S21:  -0.0626 S22:  -0.0191 S23:  -0.2385                       
REMARK   3      S31:  -0.1170 S32:  -0.1645 S33:  -0.0689                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  137  THROUGH  195 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3893   4.2683  33.9382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0896 T22:   0.1047                                     
REMARK   3      T33:   0.1060 T12:  -0.0110                                     
REMARK   3      T13:   0.0006 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9664 L22:   1.0337                                     
REMARK   3      L33:   4.8178 L12:  -1.0562                                     
REMARK   3      L13:  -0.5357 L23:   0.6391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:   0.1125 S13:   0.0433                       
REMARK   3      S21:  -0.0214 S22:  -0.0550 S23:   0.0167                       
REMARK   3      S31:  -0.1130 S32:  -0.3539 S33:   0.0376                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  196  THROUGH  216 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5003  -4.5464  24.2978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1082 T22:   0.3273                                     
REMARK   3      T33:   0.1725 T12:  -0.0360                                     
REMARK   3      T13:  -0.0068 T23:  -0.0686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7882 L22:   6.4153                                     
REMARK   3      L33:   5.5026 L12:  -6.1092                                     
REMARK   3      L13:  -2.7699 L23:   4.8450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2115 S12:   0.5397 S13:  -0.4772                       
REMARK   3      S21:   0.0012 S22:  -0.4035 S23:   0.0422                       
REMARK   3      S31:   0.2777 S32:  -0.5564 S33:   0.1428                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  217  THROUGH  285 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7861  -4.5255  24.6773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0927 T22:   0.1351                                     
REMARK   3      T33:   0.1524 T12:  -0.0013                                     
REMARK   3      T13:  -0.0061 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2085 L22:   2.4852                                     
REMARK   3      L33:   2.1614 L12:  -0.4394                                     
REMARK   3      L13:  -0.0045 L23:  -0.1168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:   0.1736 S13:  -0.2811                       
REMARK   3      S21:  -0.0577 S22:  -0.0179 S23:   0.0321                       
REMARK   3      S31:   0.1683 S32:  -0.1173 S33:  -0.0830                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  286  THROUGH  322 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3602   6.9114  43.8262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1263 T22:   0.1392                                     
REMARK   3      T33:   0.0557 T12:  -0.0051                                     
REMARK   3      T13:   0.0195 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3304 L22:   3.6907                                     
REMARK   3      L33:   2.5570 L12:  -0.0890                                     
REMARK   3      L13:   0.4730 L23:  -1.1772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0724 S12:  -0.2433 S13:   0.1201                       
REMARK   3      S21:   0.0620 S22:   0.0795 S23:   0.0053                       
REMARK   3      S31:  -0.2410 S32:  -0.2073 S33:  -0.0339                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  323  THROUGH  346 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -19.8795 -12.2567  48.2572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2366 T22:   0.2552                                     
REMARK   3      T33:   0.3276 T12:  -0.0735                                     
REMARK   3      T13:  -0.0220 T23:   0.1027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4022 L22:   4.6585                                     
REMARK   3      L33:   7.5261 L12:   2.0453                                     
REMARK   3      L13:   2.6289 L23:  -1.4992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1160 S12:  -0.3628 S13:  -0.6449                       
REMARK   3      S21:  -0.6426 S22:  -0.0577 S23:  -0.3130                       
REMARK   3      S31:   0.7458 S32:  -0.2892 S33:  -0.0556                       
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 4UEK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-62614.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2814                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49264                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.45                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY                : 6.1                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4A2C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.44800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.7 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   OE1  GLN A    25     O    HOH A  2030              2.07            
REMARK 500   O    LYS A    31     O    HOH A  2040              2.00            
REMARK 500   O    HIS A   253     O    HOH A  2202              2.19            
REMARK 500   OE2  GLU A   300     O    HOH A  2227              2.18            
REMARK 500   O    HOH A  2003     O    HOH A  2071              2.15            
REMARK 500   O    HOH A  2010     O    HOH A  2040              2.18            
REMARK 500   O    HOH A  2017     O    HOH A  2047              2.17            
REMARK 500   O    HOH A  2026     O    HOH A  2079              2.19            
REMARK 500   O    HOH A  2029     O    HOH A  2030              2.14            
REMARK 500   O    HOH A  2035     O    HOH A  2039              2.19            
REMARK 500   O    HOH A  2046     O    HOH A  2108              2.14            
REMARK 500   O    HOH A  2091     O    HOH A  2183              2.17            
REMARK 500   O    HOH A  2110     O    HOH A  2113              2.10            
REMARK 500   O    HOH A  2115     O    HOH A  2231              2.07            
REMARK 500   O    HOH A  2134     O    HOH A  2230              2.16            
REMARK 500   O    HOH A  2201     O    HOH A  2203              2.16            
REMARK 500   O    HOH B  2025     O    HOH B  2028              2.18            
REMARK 500   O    HOH B  2026     O    HOH B  2027              2.16            
REMARK 500   O    HOH B  2055     O    HOH B  2131              2.12            
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   NZ   LYS A    97     OD2  ASP B     9     2556     2.20            
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    ASP A   9       49.32    -95.97                                   
REMARK 500    ASN A  48       46.47     38.79                                   
REMARK 500    PHE A  99       55.65    -92.73                                   
REMARK 500    SER A 111      -57.65   -150.49                                   
REMARK 500    ASN A 161       18.31     59.54                                   
REMARK 500    MET A 288     -141.47     51.51                                   
REMARK 500    ASN A 289       53.60   -162.72                                   
REMARK 500    SER A 322     -164.98    -76.96                                   
REMARK 500    ALA A 334     -136.83     49.91                                   
REMARK 500    ARG A 335       49.73   -100.31                                   
REMARK 500    LYS B 105       37.66   -151.00                                   
REMARK 500    SER B 111      -57.82   -144.08                                   
REMARK 500    ASN B 161       18.95     58.13                                   
REMARK 500    MET B 288     -142.32     59.26                                   
REMARK 500    ASN B 289       52.05   -161.90                                   
REMARK 500    SER B 322     -162.32    -75.39                                   
REMARK 500    ALA B 334     -141.12     51.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  196     LYS B  197                  139.20                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2061        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH A3214        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH A3215        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A3216        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A3217        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A3218        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A3219        DISTANCE =  6.12 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  59   NE2                                                    
REMARK 620 2 TRS A1350   O1   90.6                                              
REMARK 620 3 TRS A1350   O3   91.1  88.0                                        
REMARK 620 4 CYS A  38   SG  103.8 165.5  89.9                                  
REMARK 620 5 HOH A2051   O   108.2  79.1 156.7  97.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 103   SG                                                     
REMARK 620 2 CYS B  95   SG  104.0                                              
REMARK 620 3 CYS B  89   SG  106.2 121.0                                        
REMARK 620 4 CYS B  92   SG  113.7 104.5 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  92   SG                                                     
REMARK 620 2 CYS A  89   SG  106.9                                              
REMARK 620 3 CYS A 103   SG  117.9 101.2                                        
REMARK 620 4 CYS A  95   SG  104.8 120.7 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  38   SG                                                     
REMARK 620 2 HOH B2036   O    95.9                                              
REMARK 620 3 HIS B  59   NE2 103.1 105.9                                        
REMARK 620 4 TRS B1349   O1  169.0  81.5  87.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1349  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2211   O                                                      
REMARK 620 2 HIS B 267   ND1 108.8                                              
REMARK 620 3 HIS A 267   ND1 111.8 111.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B1349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A1350                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UEJ   RELATED DB: PDB                                   
REMARK 900  CLOSED STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE              
REMARK 900  FROM E. COLI IN COMPLEX WITH GLYCEROL.                              
REMARK 900 RELATED ID: 4UEO   RELATED DB: PDB                                   
REMARK 900  OPEN STATE OF GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE                
REMARK 900  FROM E. COLI, WITH ZINC IN THE CATALYTIC SITE.                      
DBREF  4UEK A    1   346  UNP    P0A9S3   GATD_ECOLI       1    346             
DBREF  4UEK B    1   346  UNP    P0A9S3   GATD_ECOLI       1    346             
SEQRES   1 A  346  MET LYS SER VAL VAL ASN ASP THR ASP GLY ILE VAL ARG          
SEQRES   2 A  346  VAL ALA GLU SER VAL ILE PRO GLU ILE LYS HIS GLN ASP          
SEQRES   3 A  346  GLU VAL ARG VAL LYS ILE ALA SER SER GLY LEU CYS GLY          
SEQRES   4 A  346  SER ASP LEU PRO ARG ILE PHE LYS ASN GLY ALA HIS TYR          
SEQRES   5 A  346  TYR PRO ILE THR LEU GLY HIS GLU PHE SER GLY TYR ILE          
SEQRES   6 A  346  ASP ALA VAL GLY SER GLY VAL ASP ASP LEU HIS PRO GLY          
SEQRES   7 A  346  ASP ALA VAL ALA CYS VAL PRO LEU LEU PRO CYS PHE THR          
SEQRES   8 A  346  CYS PRO GLU CYS LEU LYS GLY PHE TYR SER GLN CYS ALA          
SEQRES   9 A  346  LYS TYR ASP PHE ILE GLY SER ARG ARG ASP GLY GLY PHE          
SEQRES  10 A  346  ALA GLU TYR ILE VAL VAL LYS ARG LYS ASN VAL PHE ALA          
SEQRES  11 A  346  LEU PRO THR ASP MET PRO ILE GLU ASP GLY ALA PHE ILE          
SEQRES  12 A  346  GLU PRO ILE THR VAL GLY LEU HIS ALA PHE HIS LEU ALA          
SEQRES  13 A  346  GLN GLY CYS GLU ASN LYS ASN VAL ILE ILE ILE GLY ALA          
SEQRES  14 A  346  GLY THR ILE GLY LEU LEU ALA ILE GLN CYS ALA VAL ALA          
SEQRES  15 A  346  LEU GLY ALA LYS SER VAL THR ALA ILE ASP ILE SER SER          
SEQRES  16 A  346  GLU LYS LEU ALA LEU ALA LYS SER PHE GLY ALA MET GLN          
SEQRES  17 A  346  THR PHE ASN SER SER GLU MET SER ALA PRO GLN MET GLN          
SEQRES  18 A  346  SER VAL LEU ARG GLU LEU ARG PHE ASN GLN LEU ILE LEU          
SEQRES  19 A  346  GLU THR ALA GLY VAL PRO GLN THR VAL GLU LEU ALA VAL          
SEQRES  20 A  346  GLU ILE ALA GLY PRO HIS ALA GLN LEU ALA LEU VAL GLY          
SEQRES  21 A  346  THR LEU HIS GLN ASP LEU HIS LEU THR SER ALA THR PHE          
SEQRES  22 A  346  GLY LYS ILE LEU ARG LYS GLU LEU THR VAL ILE GLY SER          
SEQRES  23 A  346  TRP MET ASN TYR SER SER PRO TRP PRO GLY GLN GLU TRP          
SEQRES  24 A  346  GLU THR ALA SER ARG LEU LEU THR GLU ARG LYS LEU SER          
SEQRES  25 A  346  LEU GLU PRO LEU ILE ALA HIS ARG GLY SER PHE GLU SER          
SEQRES  26 A  346  PHE ALA GLN ALA VAL ARG ASP ILE ALA ARG ASN ALA MET          
SEQRES  27 A  346  PRO GLY LYS VAL LEU LEU ILE PRO                              
SEQRES   1 B  346  MET LYS SER VAL VAL ASN ASP THR ASP GLY ILE VAL ARG          
SEQRES   2 B  346  VAL ALA GLU SER VAL ILE PRO GLU ILE LYS HIS GLN ASP          
SEQRES   3 B  346  GLU VAL ARG VAL LYS ILE ALA SER SER GLY LEU CYS GLY          
SEQRES   4 B  346  SER ASP LEU PRO ARG ILE PHE LYS ASN GLY ALA HIS TYR          
SEQRES   5 B  346  TYR PRO ILE THR LEU GLY HIS GLU PHE SER GLY TYR ILE          
SEQRES   6 B  346  ASP ALA VAL GLY SER GLY VAL ASP ASP LEU HIS PRO GLY          
SEQRES   7 B  346  ASP ALA VAL ALA CYS VAL PRO LEU LEU PRO CYS PHE THR          
SEQRES   8 B  346  CYS PRO GLU CYS LEU LYS GLY PHE TYR SER GLN CYS ALA          
SEQRES   9 B  346  LYS TYR ASP PHE ILE GLY SER ARG ARG ASP GLY GLY PHE          
SEQRES  10 B  346  ALA GLU TYR ILE VAL VAL LYS ARG LYS ASN VAL PHE ALA          
SEQRES  11 B  346  LEU PRO THR ASP MET PRO ILE GLU ASP GLY ALA PHE ILE          
SEQRES  12 B  346  GLU PRO ILE THR VAL GLY LEU HIS ALA PHE HIS LEU ALA          
SEQRES  13 B  346  GLN GLY CYS GLU ASN LYS ASN VAL ILE ILE ILE GLY ALA          
SEQRES  14 B  346  GLY THR ILE GLY LEU LEU ALA ILE GLN CYS ALA VAL ALA          
SEQRES  15 B  346  LEU GLY ALA LYS SER VAL THR ALA ILE ASP ILE SER SER          
SEQRES  16 B  346  GLU LYS LEU ALA LEU ALA LYS SER PHE GLY ALA MET GLN          
SEQRES  17 B  346  THR PHE ASN SER SER GLU MET SER ALA PRO GLN MET GLN          
SEQRES  18 B  346  SER VAL LEU ARG GLU LEU ARG PHE ASN GLN LEU ILE LEU          
SEQRES  19 B  346  GLU THR ALA GLY VAL PRO GLN THR VAL GLU LEU ALA VAL          
SEQRES  20 B  346  GLU ILE ALA GLY PRO HIS ALA GLN LEU ALA LEU VAL GLY          
SEQRES  21 B  346  THR LEU HIS GLN ASP LEU HIS LEU THR SER ALA THR PHE          
SEQRES  22 B  346  GLY LYS ILE LEU ARG LYS GLU LEU THR VAL ILE GLY SER          
SEQRES  23 B  346  TRP MET ASN TYR SER SER PRO TRP PRO GLY GLN GLU TRP          
SEQRES  24 B  346  GLU THR ALA SER ARG LEU LEU THR GLU ARG LYS LEU SER          
SEQRES  25 B  346  LEU GLU PRO LEU ILE ALA HIS ARG GLY SER PHE GLU SER          
SEQRES  26 B  346  PHE ALA GLN ALA VAL ARG ASP ILE ALA ARG ASN ALA MET          
SEQRES  27 B  346  PRO GLY LYS VAL LEU LEU ILE PRO                              
HET     ZN  A1347       1                                                       
HET     ZN  A1348       1                                                       
HET     ZN  B1347       1                                                       
HET     ZN  B1348       1                                                       
HET     ZN  A1349       1                                                       
HET    TRS  B1349       8                                                       
HET    TRS  A1350       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   3   ZN    5(ZN 2+)                                                     
FORMUL   4  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   5  HOH   *471(H2 O)                                                    
HELIX    1   1 SER A   40  LYS A   47  1                                   8    
HELIX    2   2 CYS A   92  LYS A   97  1                                   6    
HELIX    3   3 PHE A   99  CYS A  103  5                                   5    
HELIX    4   4 PRO A  136  ALA A  141  5                                   6    
HELIX    5   5 PHE A  142  ALA A  156  1                                  15    
HELIX    6   6 GLY A  170  LEU A  183  1                                  14    
HELIX    7   7 SER A  194  GLY A  205  1                                  12    
HELIX    8   8 SER A  216  ARG A  225  1                                  10    
HELIX    9   9 GLU A  226  ARG A  228  5                                   3    
HELIX   10  10 VAL A  239  ALA A  250  1                                  12    
HELIX   11  11 THR A  269  LYS A  279  1                                  11    
HELIX   12  12 GLY A  296  GLU A  308  1                                  13    
HELIX   13  13 LEU A  313  PRO A  315  5                                   3    
HELIX   14  14 SER A  322  ALA A  334  1                                  13    
HELIX   15  15 THR B    8  GLY B   10  5                                   3    
HELIX   16  16 CYS B   38  SER B   40  5                                   3    
HELIX   17  17 ASP B   41  LYS B   47  1                                   7    
HELIX   18  18 CYS B   92  LYS B   97  1                                   6    
HELIX   19  19 PHE B   99  CYS B  103  5                                   5    
HELIX   20  20 PRO B  136  ALA B  141  5                                   6    
HELIX   21  21 PHE B  142  ALA B  156  1                                  15    
HELIX   22  22 GLY B  170  LEU B  183  1                                  14    
HELIX   23  23 LYS B  197  PHE B  204  1                                   8    
HELIX   24  24 SER B  216  ARG B  225  1                                  10    
HELIX   25  25 GLU B  226  ARG B  228  5                                   3    
HELIX   26  26 VAL B  239  ALA B  250  1                                  12    
HELIX   27  27 THR B  269  LYS B  279  1                                  11    
HELIX   28  28 GLY B  296  GLU B  308  1                                  13    
HELIX   29  29 LEU B  313  PRO B  315  5                                   3    
HELIX   30  30 SER B  322  ALA B  334  1                                  13    
SHEET    1  AA 2 LYS A   2  ASP A   7  0                                        
SHEET    2  AA 2 ILE A  11  GLU A  16 -1  O  ILE A  11   N  ASP A   7           
SHEET    1  AB 2 TYR A 120  LYS A 124  0                                        
SHEET    2  AB 2 GLU A  27  GLY A  36 -1  O  VAL A  28   N  VAL A 123           
SHEET    1  AC 6 VAL A 128  ALA A 130  0                                        
SHEET    2  AC 6 ALA A  80  CYS A  83 -1  O  ALA A  82   N  PHE A 129           
SHEET    3  AC 6 GLU A  60  VAL A  68 -1  O  PHE A  61   N  CYS A  83           
SHEET    4  AC 6 GLU A  27  GLY A  36 -1  O  ARG A  29   N  ASP A  66           
SHEET    5  AC 6 LYS A 341  LEU A 344 -1  O  LEU A 344   N  SER A  35           
SHEET    6  AC 6 ILE A 317  GLY A 321 -1  N  ALA A 318   O  LYS A 341           
SHEET    1  AD 5 VAL A 128  ALA A 130  0                                        
SHEET    2  AD 5 ALA A  80  CYS A  83 -1  O  ALA A  82   N  PHE A 129           
SHEET    3  AD 5 GLU A  60  VAL A  68 -1  O  PHE A  61   N  CYS A  83           
SHEET    4  AD 5 GLU A  27  GLY A  36 -1  O  ARG A  29   N  ASP A  66           
SHEET    5  AD 5 TYR A 120  LYS A 124 -1  O  ILE A 121   N  VAL A  30           
SHEET    1  AE 2 LEU A  86  LEU A  87  0                                        
SHEET    2  AE 2 ASP A 107  PHE A 108 -1  O  ASP A 107   N  LEU A  87           
SHEET    1  AF12 GLN A 208  ASN A 211  0                                        
SHEET    2  AF12 SER A 187  ASP A 192  1  O  ALA A 190   N  PHE A 210           
SHEET    3  AF12 ASN A 163  ILE A 167  1  O  VAL A 164   N  THR A 189           
SHEET    4  AF12 GLN A 231  GLU A 235  1  O  LEU A 232   N  ILE A 165           
SHEET    5  AF12 GLN A 255  LEU A 258  1  O  GLN A 255   N  ILE A 233           
SHEET    6  AF12 THR A 282  GLY A 285  1  O  THR A 282   N  LEU A 256           
SHEET    7  AF12 THR B 282  GLY B 285 -1  O  VAL B 283   N  VAL A 283           
SHEET    8  AF12 GLN B 255  LEU B 258  1  O  LEU B 256   N  ILE B 284           
SHEET    9  AF12 GLN B 231  GLU B 235  1  O  GLN B 231   N  GLN B 255           
SHEET   10  AF12 ASN B 163  ILE B 167  1  O  ASN B 163   N  LEU B 232           
SHEET   11  AF12 SER B 187  ASP B 192  1  O  SER B 187   N  VAL B 164           
SHEET   12  AF12 GLN B 208  ASN B 211  1  O  GLN B 208   N  ALA B 190           
SHEET    1  AG 2 LEU A 266  LEU A 268  0                                        
SHEET    2  AG 2 LEU B 266  LEU B 268 -1  O  LEU B 266   N  LEU A 268           
SHEET    1  BA 2 LYS B   2  ASP B   7  0                                        
SHEET    2  BA 2 ILE B  11  GLU B  16 -1  O  ILE B  11   N  ASP B   7           
SHEET    1  BB 2 TYR B 120  LYS B 124  0                                        
SHEET    2  BB 2 GLU B  27  GLY B  36 -1  O  VAL B  28   N  VAL B 123           
SHEET    1  BC 6 VAL B 128  ALA B 130  0                                        
SHEET    2  BC 6 ALA B  80  CYS B  83 -1  O  ALA B  82   N  PHE B 129           
SHEET    3  BC 6 GLU B  60  VAL B  68 -1  O  PHE B  61   N  CYS B  83           
SHEET    4  BC 6 GLU B  27  GLY B  36 -1  O  ARG B  29   N  ASP B  66           
SHEET    5  BC 6 LYS B 341  LEU B 344 -1  O  LEU B 344   N  SER B  35           
SHEET    6  BC 6 ILE B 317  GLY B 321 -1  N  ALA B 318   O  LYS B 341           
SHEET    1  BD 5 VAL B 128  ALA B 130  0                                        
SHEET    2  BD 5 ALA B  80  CYS B  83 -1  O  ALA B  82   N  PHE B 129           
SHEET    3  BD 5 GLU B  60  VAL B  68 -1  O  PHE B  61   N  CYS B  83           
SHEET    4  BD 5 GLU B  27  GLY B  36 -1  O  ARG B  29   N  ASP B  66           
SHEET    5  BD 5 TYR B 120  LYS B 124 -1  O  ILE B 121   N  VAL B  30           
SHEET    1  BE 2 LEU B  86  LEU B  87  0                                        
SHEET    2  BE 2 ASP B 107  PHE B 108 -1  O  ASP B 107   N  LEU B  87           
LINK        ZN    ZN A1347                 NE2 HIS A  59     1555   1555  2.25  
LINK        ZN    ZN A1347                 O1  TRS A1350     1555   1555  2.26  
LINK        ZN    ZN A1347                 O3  TRS A1350     1555   1555  2.70  
LINK        ZN    ZN A1347                 SG  CYS A  38     1555   1555  2.41  
LINK        ZN    ZN A1347                 O   HOH A2051     1555   1555  2.11  
LINK        ZN    ZN A1348                 SG  CYS A  92     1555   1555  2.35  
LINK        ZN    ZN A1348                 SG  CYS A  89     1555   1555  2.40  
LINK        ZN    ZN A1348                 SG  CYS A 103     1555   1555  2.41  
LINK        ZN    ZN A1348                 SG  CYS A  95     1555   1555  2.34  
LINK        ZN    ZN A1349                 ND1 HIS A 267     1555   1555  2.09  
LINK        ZN    ZN A1349                 ND1 HIS B 267     1555   1555  2.04  
LINK        ZN    ZN A1349                 O   HOH A2211     1555   1555  2.19  
LINK        ZN    ZN B1347                 SG  CYS B  92     1555   1555  2.35  
LINK        ZN    ZN B1347                 SG  CYS B  89     1555   1555  2.34  
LINK        ZN    ZN B1347                 SG  CYS B  95     1555   1555  2.38  
LINK        ZN    ZN B1347                 SG  CYS B 103     1555   1555  2.47  
LINK        ZN    ZN B1348                 O1  TRS B1349     1555   1555  2.22  
LINK        ZN    ZN B1348                 NE2 HIS B  59     1555   1555  2.15  
LINK        ZN    ZN B1348                 O   HOH B2036     1555   1555  1.97  
LINK        ZN    ZN B1348                 SG  CYS B  38     1555   1555  2.40  
CISPEP   1 TYR A   53    PRO A   54          0        -4.26                     
CISPEP   2 SER A  292    PRO A  293          0        -2.09                     
CISPEP   3 TRP A  294    PRO A  295          0         1.58                     
CISPEP   4 TYR B   53    PRO B   54          0        -5.43                     
CISPEP   5 SER B  292    PRO B  293          0        -0.18                     
CISPEP   6 TRP B  294    PRO B  295          0         0.63                     
SITE     1 AC1  4 CYS A  38  HIS A  59  TRS A1350  HOH A2051                    
SITE     1 AC2  4 CYS A  89  CYS A  92  CYS A  95  CYS A 103                    
SITE     1 AC3  4 CYS B  89  CYS B  92  CYS B  95  CYS B 103                    
SITE     1 AC4  5 CYS B  38  SER B  40  HIS B  59  TRS B1349                    
SITE     2 AC4  5 HOH B2036                                                     
SITE     1 AC5  3 HIS A 267  HOH A2211  HIS B 267                               
SITE     1 AC6  7 CYS B  38  SER B  40  HIS B  59  GLU B 144                    
SITE     2 AC6  7 MET B 288   ZN B1348  HOH B2036                               
SITE     1 AC7  6 CYS A  38  SER A  40  HIS A  59  GLU A 144                    
SITE     2 AC7  6  ZN A1347  HOH A2051                                          
CRYST1   65.568   78.896   68.572  90.00  94.59  90.00 P 1 21 1      4          
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      0.015251  0.000000  0.001224        0.00000                         
SCALE2      0.000000  0.012675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014630        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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