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Database: PDB
Entry: 5U0L
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HEADER    OXIDOREDUCTASE                          24-NOV-16   5U0L              
TITLE     X-RAY CRYSTAL STRUCTURE OF FATTY ALDEHYDE DEHYDROGENASE ENZYMES FROM  
TITLE    2 MARINOBACTER AQUAEOLEI VT8 COMPLEXED WITH A SUBSTRATE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-SUCCINYLGLUTAMATE 5-SEMIALDEHYDE DEHYDROGENASE;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SUCCINYLGLUTAMIC SEMIALDEHYDE DEHYDROGENASE,SGSD;           
COMPND   5 EC: 1.2.1.71;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MARINOBACTER HYDROCARBONOCLASTICUS (STRAIN ATCC 
SOURCE   3 700491 / DSM 11845 / VT8);                                           
SOURCE   4 ORGANISM_TAXID: 351348;                                              
SOURCE   5 STRAIN: ATCC 700491 / DSM 11845 / VT8;                               
SOURCE   6 GENE: ASTD, MAQU_3316;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHYDROGENASE, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SHI,K.MULLINER,B.M.BARNEY,H.AIHARA                                  
REVDAT   5   04-OCT-23 5U0L    1       REMARK                                   
REVDAT   4   27-NOV-19 5U0L    1       REMARK                                   
REVDAT   3   13-SEP-17 5U0L    1       REMARK                                   
REVDAT   2   14-JUN-17 5U0L    1       JRNL                                     
REVDAT   1   26-APR-17 5U0L    0                                                
JRNL        AUTH   J.H.BERTRAM,K.M.MULLINER,K.SHI,M.H.PLUNKETT,P.NIXON,         
JRNL        AUTH 2 N.A.SERRATORE,C.J.DOUGLAS,H.AIHARA,B.M.BARNEY                
JRNL        TITL   FIVE FATTY ALDEHYDE DEHYDROGENASE ENZYMES FROM MARINOBACTER  
JRNL        TITL 2 AND ACINETOBACTER SPP. AND STRUCTURAL INSIGHTS INTO THE      
JRNL        TITL 3 ALDEHYDE BINDING POCKET.                                     
JRNL        REF    APPL. ENVIRON. MICROBIOL.     V.  83       2017              
JRNL        REFN                   ESSN 1098-5336                               
JRNL        PMID   28389542                                                     
JRNL        DOI    10.1128/AEM.00018-17                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2706                                      
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) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 56469                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2742                            
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 34.9033 -  6.1921    1.00     2999   165  0.1812 0.2295        
REMARK   3     2  6.1921 -  4.9192    1.00     2883   123  0.1934 0.2486        
REMARK   3     3  4.9192 -  4.2987    0.99     2804   137  0.1585 0.1979        
REMARK   3     4  4.2987 -  3.9062    1.00     2794   134  0.1725 0.2372        
REMARK   3     5  3.9062 -  3.6265    1.00     2777   144  0.1906 0.2491        
REMARK   3     6  3.6265 -  3.4129    1.00     2736   144  0.2075 0.2845        
REMARK   3     7  3.4129 -  3.2421    0.99     2703   174  0.2100 0.2818        
REMARK   3     8  3.2421 -  3.1011    0.99     2723   124  0.2252 0.2593        
REMARK   3     9  3.1011 -  2.9818    0.99     2719   144  0.2407 0.2898        
REMARK   3    10  2.9818 -  2.8789    0.99     2743   132  0.2505 0.3044        
REMARK   3    11  2.8789 -  2.7889    0.99     2696   134  0.2512 0.3745        
REMARK   3    12  2.7889 -  2.7093    0.99     2703   145  0.2590 0.3373        
REMARK   3    13  2.7093 -  2.6380    0.99     2680   145  0.2658 0.3003        
REMARK   3    14  2.6380 -  2.5736    0.99     2702   118  0.2932 0.3465        
REMARK   3    15  2.5736 -  2.5151    0.98     2644   154  0.3134 0.4311        
REMARK   3    16  2.5151 -  2.4616    0.95     2542   145  0.3505 0.3703        
REMARK   3    17  2.4616 -  2.4124    0.96     2589   136  0.3680 0.4076        
REMARK   3    18  2.4124 -  2.3669    0.95     2594   109  0.3965 0.4463        
REMARK   3    19  2.3669 -  2.3246    0.92     2494   130  0.4180 0.4388        
REMARK   3    20  2.3246 -  2.2852    0.81     2202   105  0.4148 0.4872        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.500           
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      :  0.009           7563                                  
REMARK   3   ANGLE     :  1.045          10257                                  
REMARK   3   CHIRALITY :  0.057           1135                                  
REMARK   3   PLANARITY :  0.007           1352                                  
REMARK   3   DIHEDRAL  :  9.214           4478                                  
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 3 THROUGH 62 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1290  10.4617  57.2727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7598 T22:   0.5103                                     
REMARK   3      T33:   0.5180 T12:   0.0299                                     
REMARK   3      T13:   0.0039 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5965 L22:   0.3860                                     
REMARK   3      L33:   1.0194 L12:   0.4653                                     
REMARK   3      L13:   0.4956 L23:   0.1574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1608 S12:  -0.4554 S13:   0.1237                       
REMARK   3      S21:   0.4203 S22:   0.1928 S23:  -0.0804                       
REMARK   3      S31:  -0.1730 S32:   0.0326 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 279 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6509   1.9589  43.5632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5870 T22:   0.4022                                     
REMARK   3      T33:   0.5396 T12:  -0.0368                                     
REMARK   3      T13:  -0.0249 T23:   0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7387 L22:   0.4997                                     
REMARK   3      L33:   1.4155 L12:  -0.1650                                     
REMARK   3      L13:   0.0802 L23:   0.1257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0027 S12:  -0.1631 S13:  -0.0611                       
REMARK   3      S21:   0.0610 S22:   0.0527 S23:   0.1023                       
REMARK   3      S31:  -0.0240 S32:  -0.0192 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0896  17.8809  25.6188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6830 T22:   0.5719                                     
REMARK   3      T33:   0.6673 T12:   0.1592                                     
REMARK   3      T13:  -0.0875 T23:   0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2838 L22:   1.9253                                     
REMARK   3      L33:   0.6486 L12:   0.1276                                     
REMARK   3      L13:   0.1935 L23:   0.1070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0409 S12:   0.0840 S13:   0.1839                       
REMARK   3      S21:  -0.1652 S22:   0.1089 S23:   0.0612                       
REMARK   3      S31:  -0.1218 S32:   0.0489 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 490 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2157  -7.0781  28.5871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7114 T22:   0.5271                                     
REMARK   3      T33:   0.5559 T12:   0.0232                                     
REMARK   3      T13:  -0.1140 T23:   0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4844 L22:   0.2456                                     
REMARK   3      L33:   0.2962 L12:  -0.8300                                     
REMARK   3      L13:  -0.4547 L23:  -0.3157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1724 S12:   0.1816 S13:  -0.1552                       
REMARK   3      S21:  -0.0831 S22:  -0.0793 S23:   0.1184                       
REMARK   3      S31:   0.1276 S32:   0.1407 S33:   0.0148                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 120 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  61.7411 -11.7949  13.6759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6438 T22:   0.6612                                     
REMARK   3      T33:   0.5213 T12:   0.1048                                     
REMARK   3      T13:  -0.0425 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7604 L22:   0.3484                                     
REMARK   3      L33:   1.1591 L12:  -0.3098                                     
REMARK   3      L13:  -0.5262 L23:  -0.0992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0599 S12:   0.1691 S13:  -0.0249                       
REMARK   3      S21:  -0.1324 S22:  -0.0760 S23:   0.0575                       
REMARK   3      S31:   0.3544 S32:   0.4472 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 121 THROUGH 153 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0110  -8.7807  24.0162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6270 T22:   0.5595                                     
REMARK   3      T33:   0.6093 T12:   0.0472                                     
REMARK   3      T13:  -0.0690 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0329 L22:   0.1511                                     
REMARK   3      L33:   0.6221 L12:   0.0510                                     
REMARK   3      L13:  -0.1488 L23:  -0.2364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2197 S12:  -0.1834 S13:  -0.1383                       
REMARK   3      S21:  -0.0173 S22:  -0.0491 S23:   0.0212                       
REMARK   3      S31:   0.1250 S32:   0.0866 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 154 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  59.4441  -3.3227  19.2098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5360 T22:   0.6066                                     
REMARK   3      T33:   0.4914 T12:   0.0790                                     
REMARK   3      T13:  -0.0469 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3993 L22:   0.2864                                     
REMARK   3      L33:   0.8977 L12:   0.2871                                     
REMARK   3      L13:  -0.2481 L23:  -0.4743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0123 S12:   0.0162 S13:  -0.0471                       
REMARK   3      S21:   0.0064 S22:  -0.1131 S23:   0.0876                       
REMARK   3      S31:   0.1377 S32:   0.5380 S33:   0.0002                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 249 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3657 -22.0962  42.7466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8180 T22:   1.1608                                     
REMARK   3      T33:   0.6893 T12:   0.3028                                     
REMARK   3      T13:  -0.0759 T23:   0.1075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3798 L22:   0.0827                                     
REMARK   3      L33:   0.2068 L12:   0.1323                                     
REMARK   3      L13:  -0.0662 L23:   0.1448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1223 S12:  -0.4105 S13:  -0.0618                       
REMARK   3      S21:   0.4166 S22:   0.1027 S23:   0.0099                       
REMARK   3      S31:  -0.1086 S32:   0.4376 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  76.8514 -21.2071  45.7217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8927 T22:   1.1521                                     
REMARK   3      T33:   0.7251 T12:   0.2018                                     
REMARK   3      T13:  -0.2152 T23:   0.1269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0630 L22:   0.1076                                     
REMARK   3      L33:   0.0159 L12:  -0.1961                                     
REMARK   3      L13:   0.0901 L23:  -0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1226 S12:   0.0469 S13:  -0.1390                       
REMARK   3      S21:   0.3199 S22:  -0.0989 S23:  -0.1256                       
REMARK   3      S31:  -0.1428 S32:   0.4487 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 310 THROUGH 345 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  83.1150 -14.1377  31.0473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6549 T22:   1.4244                                     
REMARK   3      T33:   0.9000 T12:   0.2125                                     
REMARK   3      T13:  -0.0139 T23:   0.0801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2010 L22:   0.1216                                     
REMARK   3      L33:   0.0613 L12:   0.1622                                     
REMARK   3      L13:  -0.1357 L23:  -0.0785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2590 S12:   0.2262 S13:   0.0088                       
REMARK   3      S21:   0.1423 S22:  -0.3347 S23:  -0.7985                       
REMARK   3      S31:   0.4636 S32:   1.0790 S33:   0.0002                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 346 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  79.0268 -12.1576  43.9254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8153 T22:   1.3815                                     
REMARK   3      T33:   0.7699 T12:   0.2589                                     
REMARK   3      T13:  -0.1989 T23:   0.1122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2349 L22:   1.0885                                     
REMARK   3      L33:   0.1041 L12:   0.0994                                     
REMARK   3      L13:  -0.1083 L23:   0.3391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2901 S12:  -0.2804 S13:  -0.1067                       
REMARK   3      S21:   0.2366 S22:  -0.1232 S23:  -0.0693                       
REMARK   3      S31:  -0.0815 S32:   0.6815 S33:   0.0059                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 401 THROUGH 443 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  61.4852 -17.9708  46.0991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8976 T22:   0.7554                                     
REMARK   3      T33:   0.6367 T12:   0.2219                                     
REMARK   3      T13:  -0.0986 T23:   0.0956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4543 L22:   0.2414                                     
REMARK   3      L33:   0.2302 L12:   0.1887                                     
REMARK   3      L13:   0.1795 L23:  -0.1331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:  -0.1564 S13:  -0.2551                       
REMARK   3      S21:  -0.0000 S22:  -0.3037 S23:   0.4621                       
REMARK   3      S31:   0.0713 S32:   0.1578 S33:  -0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 444 THROUGH 490 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5201  -4.4320  29.7670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5745 T22:   0.3930                                     
REMARK   3      T33:   0.5007 T12:  -0.0243                                     
REMARK   3      T13:  -0.0329 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3358 L22:   0.2415                                     
REMARK   3      L33:   0.5951 L12:  -0.8237                                     
REMARK   3      L13:   0.0625 L23:  -0.0717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2921 S12:  -0.3240 S13:  -0.1073                       
REMARK   3      S21:   0.0061 S22:  -0.1367 S23:   0.0324                       
REMARK   3      S31:   0.1331 S32:  -0.0248 S33:   0.0000                       
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 5U0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224474.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57651                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.285                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.041                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 14.60                              
REMARK 200  R MERGE                    (I) : 0.17100                            
REMARK 200  R SYM                      (I) : 0.17100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 5.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
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: 3JU8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50%MPD, PH 7, VAPOR DIFFUSION, SITTING   
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      127.36250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.35500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.35500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       63.68125            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.35500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.35500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      191.04375            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.35500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.35500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       63.68125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.35500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.35500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      191.04375            
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      127.36250            
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: 10140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A   491                                                      
REMARK 465     MET B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     ASP B   491                                                      
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   OE2  GLU B    98     OG   SER B   277              2.03            
REMARK 500   O    GLY A   279     NH2  ARG A   286              2.11            
REMARK 500   OE2  GLU B   314     NZ   LYS B   357              2.14            
REMARK 500   NH2  ARG A    60     OE1  GLU B   425              2.15            
REMARK 500   NZ   LYS A   477     OG   SER B   261              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 165   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 121       45.40   -141.00                                   
REMARK 500    GLN A 240       63.27   -118.82                                   
REMARK 500    ASN A 259       64.20     76.20                                   
REMARK 500    ASP A 359       60.07   -109.83                                   
REMARK 500    LYS A 391      -83.79   -108.87                                   
REMARK 500    THR A 403      146.21   -174.32                                   
REMARK 500    LEU A 407      -73.05    -90.21                                   
REMARK 500    VAL A 449     -166.89   -109.89                                   
REMARK 500    SER A 458     -147.78   -101.29                                   
REMARK 500    ALA A 459     -126.98     47.93                                   
REMARK 500    GLU B 176       -7.70    -59.56                                   
REMARK 500    ASN B 259       64.97     72.42                                   
REMARK 500    ASP B 359       65.55   -116.73                                   
REMARK 500    LYS B 391      -78.61   -107.06                                   
REMARK 500    THR B 403      148.59   -173.84                                   
REMARK 500    LEU B 407      -75.30    -91.53                                   
REMARK 500    VAL B 449     -166.97   -107.89                                   
REMARK 500    SER B 458     -148.83   -102.63                                   
REMARK 500    ALA B 459     -123.31     43.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     8YP A  507                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8YP A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5U0M   RELATED DB: PDB                                   
DBREF  5U0L A    2   491  UNP    A1U5W8   ASTD_MARHV       2    491             
DBREF  5U0L B    2   491  UNP    A1U5W8   ASTD_MARHV       2    491             
SEQADV 5U0L MET A   -5  UNP  A1U5W8              INITIATING METHIONINE          
SEQADV 5U0L HIS A   -4  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS A   -3  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS A   -2  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS A   -1  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS A    0  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS A    1  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L MET B   -5  UNP  A1U5W8              INITIATING METHIONINE          
SEQADV 5U0L HIS B   -4  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS B   -3  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS B   -2  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS B   -1  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS B    0  UNP  A1U5W8              EXPRESSION TAG                 
SEQADV 5U0L HIS B    1  UNP  A1U5W8              EXPRESSION TAG                 
SEQRES   1 A  497  MET HIS HIS HIS HIS HIS HIS ALA ASN LEU THR GLY ASN          
SEQRES   2 A  497  VAL TYR ILE ASP GLY LEU TRP LEU PRO GLY HIS GLY ALA          
SEQRES   3 A  497  PRO PHE GLU SER VAL GLN PRO VAL THR GLY GLU THR VAL          
SEQRES   4 A  497  TRP ASP GLY ASN ALA ALA SER LEU GLU ASP VAL ASP ALA          
SEQRES   5 A  497  ALA VAL ARG GLU ALA ARG LYS ALA PHE LEU ALA TRP ARG          
SEQRES   6 A  497  ARG LYS SER LEU ALA GLU ARG GLN ALA VAL ILE GLU ALA          
SEQRES   7 A  497  PHE GLY GLU LEU LEU GLU ALA ASN LYS GLU GLU LEU ALA          
SEQRES   8 A  497  HIS GLN ILE GLY LEU GLU THR GLY LYS PRO LEU TRP GLU          
SEQRES   9 A  497  SER ARG THR GLU VAL ALA ALA MET MET GLY LYS ILE PRO          
SEQRES  10 A  497  ILE SER VAL LYS ALA TYR ASN GLU ARG THR GLY HIS THR          
SEQRES  11 A  497  GLU SER ASP VAL ALA GLY GLY HIS ALA VAL LEU ARG HIS          
SEQRES  12 A  497  ARG PRO HIS GLY VAL VAL ALA VAL PHE GLY PRO TYR ASN          
SEQRES  13 A  497  PHE PRO GLY HIS LEU PRO ASN GLY HIS ILE VAL PRO ALA          
SEQRES  14 A  497  LEU LEU ALA GLY ASN THR VAL VAL PHE LYS PRO SER GLU          
SEQRES  15 A  497  LEU THR PRO GLY VAL ALA GLU LEU THR VAL ARG LEU TRP          
SEQRES  16 A  497  GLU LYS ALA GLY LEU PRO ASP GLY VAL ILE ASN LEU VAL          
SEQRES  17 A  497  GLN GLY GLY SER ASP THR GLY LYS CYS LEU ALA ARG HIS          
SEQRES  18 A  497  SER LEU ILE ASP GLY LEU PHE PHE THR GLY SER SER THR          
SEQRES  19 A  497  VAL GLY HIS LEU LEU HIS GLU GLN PHE GLY GLY GLN PRO          
SEQRES  20 A  497  GLU LYS ILE LEU ALA LEU GLU MET GLY GLY ASN ASN PRO          
SEQRES  21 A  497  LEU ILE VAL GLN ASN VAL SER ASP LEU ASP GLY ALA VAL          
SEQRES  22 A  497  HIS HIS ALA LEU GLN SER ALA PHE LEU SER ALA GLY GLN          
SEQRES  23 A  497  ARG CYS THR CYS ALA ARG ARG LEU LEU VAL PRO LYS GLY          
SEQRES  24 A  497  LYS LYS GLY ASP GLU PHE LEU ALA ARG LEU VAL GLU VAL          
SEQRES  25 A  497  ALA ALA ARG ILE THR VAL ALA GLU PHE ASP ALA ASP PRO          
SEQRES  26 A  497  GLN PRO PHE MET GLY SER VAL ILE SER ALA GLU ALA ALA          
SEQRES  27 A  497  ASN GLN LEU LEU LYS ALA GLN ALA ALA MET LEU GLU LYS          
SEQRES  28 A  497  GLY ALA THR SER LEU LEU GLU MET LYS GLN LEU LYS PRO          
SEQRES  29 A  497  ASP THR GLY LEU LEU SER PRO GLY ILE VAL ASP ALA THR          
SEQRES  30 A  497  GLY ILE GLU LEU GLU ASP GLN GLU PHE PHE GLY PRO LEU          
SEQRES  31 A  497  LEU THR VAL TYR ARG TYR LYS GLY PHE ASP GLU ALA LEU          
SEQRES  32 A  497  GLU LEU ALA ASN ASN THR ARG TYR GLY LEU SER ALA GLY          
SEQRES  33 A  497  ILE LEU SER ASP ASP ARG LYS LEU TYR ASN ARG LEU VAL          
SEQRES  34 A  497  GLU GLU VAL ARG ALA GLY ILE VAL ASN TRP ASN ARG PRO          
SEQRES  35 A  497  LEU THR GLY ALA SER SER ALA ALA PRO PHE GLY GLY VAL          
SEQRES  36 A  497  GLY ALA SER GLY ASN HIS ARG PRO SER ALA TYR TYR ALA          
SEQRES  37 A  497  ALA ASP TYR CYS ALA TRP PRO MET ALA SER LEU GLU ALA          
SEQRES  38 A  497  GLY LYS SER GLU LEU PRO ASP SER LEU ALA PRO GLY LEU          
SEQRES  39 A  497  ASN PHE ASP                                                  
SEQRES   1 B  497  MET HIS HIS HIS HIS HIS HIS ALA ASN LEU THR GLY ASN          
SEQRES   2 B  497  VAL TYR ILE ASP GLY LEU TRP LEU PRO GLY HIS GLY ALA          
SEQRES   3 B  497  PRO PHE GLU SER VAL GLN PRO VAL THR GLY GLU THR VAL          
SEQRES   4 B  497  TRP ASP GLY ASN ALA ALA SER LEU GLU ASP VAL ASP ALA          
SEQRES   5 B  497  ALA VAL ARG GLU ALA ARG LYS ALA PHE LEU ALA TRP ARG          
SEQRES   6 B  497  ARG LYS SER LEU ALA GLU ARG GLN ALA VAL ILE GLU ALA          
SEQRES   7 B  497  PHE GLY GLU LEU LEU GLU ALA ASN LYS GLU GLU LEU ALA          
SEQRES   8 B  497  HIS GLN ILE GLY LEU GLU THR GLY LYS PRO LEU TRP GLU          
SEQRES   9 B  497  SER ARG THR GLU VAL ALA ALA MET MET GLY LYS ILE PRO          
SEQRES  10 B  497  ILE SER VAL LYS ALA TYR ASN GLU ARG THR GLY HIS THR          
SEQRES  11 B  497  GLU SER ASP VAL ALA GLY GLY HIS ALA VAL LEU ARG HIS          
SEQRES  12 B  497  ARG PRO HIS GLY VAL VAL ALA VAL PHE GLY PRO TYR ASN          
SEQRES  13 B  497  PHE PRO GLY HIS LEU PRO ASN GLY HIS ILE VAL PRO ALA          
SEQRES  14 B  497  LEU LEU ALA GLY ASN THR VAL VAL PHE LYS PRO SER GLU          
SEQRES  15 B  497  LEU THR PRO GLY VAL ALA GLU LEU THR VAL ARG LEU TRP          
SEQRES  16 B  497  GLU LYS ALA GLY LEU PRO ASP GLY VAL ILE ASN LEU VAL          
SEQRES  17 B  497  GLN GLY GLY SER ASP THR GLY LYS CYS LEU ALA ARG HIS          
SEQRES  18 B  497  SER LEU ILE ASP GLY LEU PHE PHE THR GLY SER SER THR          
SEQRES  19 B  497  VAL GLY HIS LEU LEU HIS GLU GLN PHE GLY GLY GLN PRO          
SEQRES  20 B  497  GLU LYS ILE LEU ALA LEU GLU MET GLY GLY ASN ASN PRO          
SEQRES  21 B  497  LEU ILE VAL GLN ASN VAL SER ASP LEU ASP GLY ALA VAL          
SEQRES  22 B  497  HIS HIS ALA LEU GLN SER ALA PHE LEU SER ALA GLY GLN          
SEQRES  23 B  497  ARG CYS THR CYS ALA ARG ARG LEU LEU VAL PRO LYS GLY          
SEQRES  24 B  497  LYS LYS GLY ASP GLU PHE LEU ALA ARG LEU VAL GLU VAL          
SEQRES  25 B  497  ALA ALA ARG ILE THR VAL ALA GLU PHE ASP ALA ASP PRO          
SEQRES  26 B  497  GLN PRO PHE MET GLY SER VAL ILE SER ALA GLU ALA ALA          
SEQRES  27 B  497  ASN GLN LEU LEU LYS ALA GLN ALA ALA MET LEU GLU LYS          
SEQRES  28 B  497  GLY ALA THR SER LEU LEU GLU MET LYS GLN LEU LYS PRO          
SEQRES  29 B  497  ASP THR GLY LEU LEU SER PRO GLY ILE VAL ASP ALA THR          
SEQRES  30 B  497  GLY ILE GLU LEU GLU ASP GLN GLU PHE PHE GLY PRO LEU          
SEQRES  31 B  497  LEU THR VAL TYR ARG TYR LYS GLY PHE ASP GLU ALA LEU          
SEQRES  32 B  497  GLU LEU ALA ASN ASN THR ARG TYR GLY LEU SER ALA GLY          
SEQRES  33 B  497  ILE LEU SER ASP ASP ARG LYS LEU TYR ASN ARG LEU VAL          
SEQRES  34 B  497  GLU GLU VAL ARG ALA GLY ILE VAL ASN TRP ASN ARG PRO          
SEQRES  35 B  497  LEU THR GLY ALA SER SER ALA ALA PRO PHE GLY GLY VAL          
SEQRES  36 B  497  GLY ALA SER GLY ASN HIS ARG PRO SER ALA TYR TYR ALA          
SEQRES  37 B  497  ALA ASP TYR CYS ALA TRP PRO MET ALA SER LEU GLU ALA          
SEQRES  38 B  497  GLY LYS SER GLU LEU PRO ASP SER LEU ALA PRO GLY LEU          
SEQRES  39 B  497  ASN PHE ASP                                                  
HET    EDO  A 501      10                                                       
HET    EDO  A 502      10                                                       
HET    EDO  A 503      10                                                       
HET    EDO  A 504      10                                                       
HET    EDO  A 505      10                                                       
HET    EDO  A 506      10                                                       
HET    8YP  A 507      25                                                       
HET    EDO  A 508      10                                                       
HET    EDO  A 509      10                                                       
HET    MPD  B 501       8                                                       
HET    MPD  B 502       8                                                       
HET     CL  B 503       1                                                       
HET    PO4  B 504       5                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     8YP DECANAL                                                          
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    8(C2 H6 O2)                                                  
FORMUL   9  8YP    C10 H20 O                                                    
FORMUL  12  MPD    2(C6 H14 O2)                                                 
FORMUL  14   CL    CL 1-                                                        
FORMUL  15  PO4    O4 P 3-                                                      
FORMUL  16  HOH   *60(H2 O)                                                     
HELIX    1 AA1 SER A   40  ARG A   59  1                                  20    
HELIX    2 AA2 SER A   62  ASN A   80  1                                  19    
HELIX    3 AA3 ASN A   80  GLY A   93  1                                  14    
HELIX    4 AA4 PRO A   95  THR A  121  1                                  27    
HELIX    5 AA5 GLY A  153  ALA A  166  1                                  14    
HELIX    6 AA6 THR A  178  ALA A  192  1                                  15    
HELIX    7 AA7 GLY A  205  ARG A  214  1                                  10    
HELIX    8 AA8 SER A  226  PHE A  237  1                                  12    
HELIX    9 AA9 ASP A  262  LEU A  276  1                                  15    
HELIX   10 AB1 SER A  277  GLN A  280  5                                   4    
HELIX   11 AB2 GLY A  293  ALA A  308  1                                  16    
HELIX   12 AB3 SER A  328  LYS A  345  1                                  18    
HELIX   13 AB4 GLY A  392  ASN A  401  1                                  10    
HELIX   14 AB5 ASP A  415  VAL A  426  1                                  12    
HELIX   15 AB6 VAL A  449  GLY A  453  5                                   5    
HELIX   16 AB7 TYR A  461  CYS A  466  1                                   6    
HELIX   17 AB8 SER B   40  ARG B   59  1                                  20    
HELIX   18 AB9 SER B   62  ASN B   80  1                                  19    
HELIX   19 AC1 ASN B   80  GLY B   93  1                                  14    
HELIX   20 AC2 PRO B   95  THR B  121  1                                  27    
HELIX   21 AC3 GLY B  153  ALA B  166  1                                  14    
HELIX   22 AC4 THR B  178  ALA B  192  1                                  15    
HELIX   23 AC5 GLY B  205  ARG B  214  1                                  10    
HELIX   24 AC6 SER B  226  PHE B  237  1                                  12    
HELIX   25 AC7 ASP B  262  LEU B  276  1                                  15    
HELIX   26 AC8 SER B  277  GLY B  279  5                                   3    
HELIX   27 AC9 GLY B  293  ALA B  308  1                                  16    
HELIX   28 AD1 SER B  328  LYS B  345  1                                  18    
HELIX   29 AD2 GLY B  392  ASN B  401  1                                  10    
HELIX   30 AD3 ASP B  415  VAL B  426  1                                  12    
HELIX   31 AD4 VAL B  449  GLY B  453  5                                   5    
HELIX   32 AD5 TYR B  461  CYS B  466  1                                   6    
SHEET    1 AA1 2 VAL A   8  ILE A  10  0                                        
SHEET    2 AA1 2 LEU A  13  LEU A  15 -1  O  LEU A  13   N  ILE A  10           
SHEET    1 AA2 2 PRO A  21  VAL A  25  0                                        
SHEET    2 AA2 2 THR A  32  ASN A  37 -1  O  VAL A  33   N  SER A  24           
SHEET    1 AA3 3 THR A 124  VAL A 128  0                                        
SHEET    2 AA3 3 GLY A 131  PRO A 139 -1  O  ALA A 133   N  SER A 126           
SHEET    3 AA3 3 ALA A 467  GLU A 474 -1  O  GLU A 474   N  HIS A 132           
SHEET    1 AA4 5 ILE A 199  LEU A 201  0                                        
SHEET    2 AA4 5 THR A 169  LYS A 173  1  N  PHE A 172   O  ASN A 200           
SHEET    3 AA4 5 VAL A 142  PHE A 146  1  N  VAL A 145   O  LYS A 173           
SHEET    4 AA4 5 GLY A 220  THR A 224  1  O  PHE A 222   N  ALA A 144           
SHEET    5 AA4 5 ILE A 244  GLU A 248  1  O  ALA A 246   N  PHE A 223           
SHEET    1 AA5 7 THR A 348  LEU A 351  0                                        
SHEET    2 AA5 7 GLY A 366  ASP A 369 -1  O  ASP A 369   N  THR A 348           
SHEET    3 AA5 7 LEU A 384  TYR A 390  1  O  VAL A 387   N  VAL A 368           
SHEET    4 AA5 7 ALA A 285  PRO A 291  1  N  LEU A 288   O  THR A 386           
SHEET    5 AA5 7 ASN A 253  VAL A 257  1  N  LEU A 255   O  LEU A 289           
SHEET    6 AA5 7 SER A 408  LEU A 412  1  O  LEU A 412   N  ILE A 256           
SHEET    7 AA5 7 ILE A 430  TRP A 433  1  O  ASN A 432   N  ILE A 411           
SHEET    1 AA6 2 PRO A 445  PHE A 446  0                                        
SHEET    2 AA6 2 SER A 458  ALA A 459 -1  O  SER A 458   N  PHE A 446           
SHEET    1 AA7 2 VAL B   8  ILE B  10  0                                        
SHEET    2 AA7 2 LEU B  13  LEU B  15 -1  O  LEU B  15   N  VAL B   8           
SHEET    1 AA8 2 PRO B  21  VAL B  25  0                                        
SHEET    2 AA8 2 THR B  32  ASN B  37 -1  O  VAL B  33   N  SER B  24           
SHEET    1 AA9 3 THR B 124  VAL B 128  0                                        
SHEET    2 AA9 3 GLY B 131  PRO B 139 -1  O  ALA B 133   N  SER B 126           
SHEET    3 AA9 3 ALA B 467  GLU B 474 -1  O  GLU B 474   N  HIS B 132           
SHEET    1 AB1 5 ILE B 199  LEU B 201  0                                        
SHEET    2 AB1 5 THR B 169  LYS B 173  1  N  PHE B 172   O  ASN B 200           
SHEET    3 AB1 5 VAL B 142  PHE B 146  1  N  VAL B 145   O  LYS B 173           
SHEET    4 AB1 5 GLY B 220  THR B 224  1  O  PHE B 222   N  ALA B 144           
SHEET    5 AB1 5 ILE B 244  GLU B 248  1  O  ALA B 246   N  PHE B 223           
SHEET    1 AB2 7 THR B 348  LEU B 351  0                                        
SHEET    2 AB2 7 GLY B 366  ASP B 369 -1  O  ASP B 369   N  THR B 348           
SHEET    3 AB2 7 LEU B 384  TYR B 390  1  O  LEU B 385   N  GLY B 366           
SHEET    4 AB2 7 ALA B 285  PRO B 291  1  N  LEU B 288   O  THR B 386           
SHEET    5 AB2 7 ASN B 253  VAL B 257  1  N  LEU B 255   O  LEU B 289           
SHEET    6 AB2 7 SER B 408  LEU B 412  1  O  GLY B 410   N  ILE B 256           
SHEET    7 AB2 7 ILE B 430  TRP B 433  1  O  ASN B 432   N  ILE B 411           
SHEET    1 AB3 2 PRO B 445  PHE B 446  0                                        
SHEET    2 AB3 2 SER B 458  ALA B 459 -1  O  SER B 458   N  PHE B 446           
SITE     1 AC1  3 PHE A 393  ASP A 394  ARG A 421                               
SITE     1 AC2  7 GLY A 147  LYS A 173  PRO A 174  SER A 175                    
SITE     2 AC2  7 GLU A 176  EDO A 508  HOH A 622                               
SITE     1 AC3  4 SER A 441  SER A 442  HOH A 608  VAL B 128                    
SITE     1 AC4  3 HIS A 123  ARG A 136  ARG A 138                               
SITE     1 AC5  5 ASN A 252  ARG A 287  GLU A 376  TYR A 388                    
SITE     2 AC5  5 ASN A 402                                                     
SITE     1 AC6  5 PRO A 457  TYR A 461  ASP A 464  ASP B 464                    
SITE     2 AC6  5 PRO B 469                                                     
SITE     1 AC7  8 LYS A 109  HIS A 154  LEU A 155  GLY A 158                    
SITE     2 AC7  8 HIS A 159  THR A 224  SER A 458  ALA A 459                    
SITE     1 AC8  2 SER A 206  EDO A 502                                          
SITE     1 AC9  3 CYS A 282  THR A 283  THR A 438                               
SITE     1 AD1  3 GLN B 258  PHE B 393  ARG B 421                               
SITE     1 AD2  5 HIS A 234  ASN A 454  ARG A 456  LEU B 245                    
SITE     2 AD2  5 ARG B 456                                                     
SITE     1 AD3  1 ARG B 138                                                     
SITE     1 AD4  4 ASP A 359  ARG A 416  GLU B 125  GLU B 474                    
CRYST1   98.710   98.710  254.725  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010131  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010131  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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