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LongText Report for: 4ARA-pdb

Name Class
4ARA-pdb
HEADER    HYDROLASE                               23-APR-12   4ARA              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-C5685 AT 2.5 A  
TITLE    2 RESOLUTION.                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: HEK293F                                   
KEYWDS    HYDROLASE, ENATIOMERS, INHIBITOR, CHEMICAL LEAD                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNGSTAFSHEDE,F.EKSTROM, 
AUTHOR   2 A.LINUSSON                                                           
REVDAT   1   28-NOV-12 4ARA    0                                                
JRNL        AUTH   L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNG-STAFSHEDE, 
JRNL        AUTH 2 F.EKSTROM,A.LINUSSON                                         
JRNL        TITL   SIMILAR BUT DIFFERENT: THERMODYNAMIC AND STRUCTURAL          
JRNL        TITL 2 CHARACTERIZATION OF A PAIR OF ENANTIOMERS BINDING TO         
JRNL        TITL 3 ACETYLCHOLINESTERASE.                                        
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.                    2012              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   23161758                                                     
JRNL        DOI    10.1002/ANIE.201205113                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.BERG,C.D.ANDERSSON,E.ARTURSSON,A.HORNBERG,A.TUNEMALM,      
REMARK   1  AUTH 2 A.LINUSSON,F.EKSTROM                                         
REMARK   1  TITL   TARGETING ACETYLCHOLINESTERASE: IDENTIFICATION OF CHEMICAL   
REMARK   1  TITL 2 LEADS BY HIGH THROUGHPUT SCREENING, STRUCTURE DETERMINATION  
REMARK   1  TITL 3 AND MOLECULAR MODELING.                                      
REMARK   1  REF    PLOS ONE                      V.   6 26039 2011              
REMARK   1  REFN                   ISSN 1932-6203                               
REMARK   1  PMID   22140425                                                     
REMARK   1  DOI    10.1371/JOURNAL.PONE.0026039                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.855                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.79                          
REMARK   3   NUMBER OF REFLECTIONS             : 70252                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1834                          
REMARK   3   R VALUE            (WORKING SET) : 0.1826                          
REMARK   3   FREE R VALUE                     : 0.2220                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1416                            
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 28.8570 -  5.3757    0.99     7189   143  0.1885 0.2164        
REMARK   3     2  5.3757 -  4.2713    1.00     6985   132  0.1405 0.1623        
REMARK   3     3  4.2713 -  3.7327    1.00     6914   140  0.1496 0.1868        
REMARK   3     4  3.7327 -  3.3920    1.00     6867   141  0.1836 0.2211        
REMARK   3     5  3.3920 -  3.1492    1.00     6883   130  0.2051 0.2611        
REMARK   3     6  3.1492 -  2.9637    1.00     6812   152  0.2038 0.2251        
REMARK   3     7  2.9637 -  2.8154    1.00     6822   136  0.2017 0.2763        
REMARK   3     8  2.8154 -  2.6929    1.00     6819   134  0.2188 0.2521        
REMARK   3     9  2.6929 -  2.5893    1.00     6773   154  0.2283 0.2913        
REMARK   3    10  2.5893 -  2.5000    1.00     6772   154  0.2516 0.3072        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.346                                         
REMARK   3   B_SOL              : 60.440                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.25             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.96            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.8219                                              
REMARK   3    B22 (A**2) : 12.8430                                              
REMARK   3    B33 (A**2) : -23.6649                                             
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
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      :  0.004           8837                                  
REMARK   3   ANGLE     :  0.898          12028                                  
REMARK   3   CHIRALITY :  0.062           1284                                  
REMARK   3   PLANARITY :  0.005           1569                                  
REMARK   3   DIHEDRAL  : 15.764           3242                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:142)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3331  15.4227  32.1785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2680 T22:   0.2377                                     
REMARK   3      T33:   0.2733 T12:   0.0043                                     
REMARK   3      T13:  -0.0062 T23:   0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1653 L22:   0.1515                                     
REMARK   3      L33:   1.1039 L12:  -0.0646                                     
REMARK   3      L13:  -0.0023 L23:  -0.0362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0523 S12:  -0.0982 S13:   0.0348                       
REMARK   3      S21:   0.1247 S22:   0.0154 S23:  -0.0733                       
REMARK   3      S31:  -0.0659 S32:   0.0513 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 143:223)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2478   4.1202  24.0344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2888 T22:   0.1961                                     
REMARK   3      T33:   0.2787 T12:   0.0377                                     
REMARK   3      T13:  -0.0043 T23:   0.0419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1483 L22:   0.5967                                     
REMARK   3      L33:   0.8150 L12:   0.2277                                     
REMARK   3      L13:   0.3633 L23:   0.1429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:  -0.0490 S13:  -0.0278                       
REMARK   3      S21:   0.1101 S22:   0.0576 S23:  -0.0461                       
REMARK   3      S31:   0.1922 S32:   0.0234 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 224:341)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  37.7919  10.9019  10.3854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1622 T22:   0.1245                                     
REMARK   3      T33:   0.2217 T12:   0.0429                                     
REMARK   3      T13:   0.0319 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8001 L22:   0.0000                                     
REMARK   3      L33:   1.3220 L12:   0.3229                                     
REMARK   3      L13:   0.2284 L23:  -0.3981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0884 S12:   0.1377 S13:   0.0056                       
REMARK   3      S21:  -0.0313 S22:   0.0118 S23:  -0.0087                       
REMARK   3      S31:   0.1742 S32:   0.1599 S33:  -0.0002                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 342:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5229  17.1741   6.3422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1834 T22:   0.2424                                     
REMARK   3      T33:   0.2619 T12:  -0.0244                                     
REMARK   3      T13:  -0.0065 T23:   0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2268 L22:   0.5033                                     
REMARK   3      L33:   1.4203 L12:  -0.0797                                     
REMARK   3      L13:   0.3579 L23:   0.1415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0342 S12:   0.1124 S13:   0.0048                       
REMARK   3      S21:  -0.1121 S22:   0.0327 S23:   0.0835                       
REMARK   3      S31:   0.0444 S32:  -0.2615 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8700   1.4649  13.7085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3515 T22:   0.4830                                     
REMARK   3      T33:   0.4191 T12:  -0.2953                                     
REMARK   3      T13:   0.0134 T23:   0.0765                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2896 L22:   0.3384                                     
REMARK   3      L33:   0.8203 L12:  -0.2812                                     
REMARK   3      L13:  -0.1398 L23:   0.0446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0970 S12:   0.4955 S13:  -0.1487                       
REMARK   3      S21:  -0.0701 S22:  -0.0042 S23:   0.5685                       
REMARK   3      S31:   0.3724 S32:  -1.0654 S33:   0.0012                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6550   6.3933  -1.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2660 T22:   0.4620                                     
REMARK   3      T33:   0.2711 T12:  -0.0665                                     
REMARK   3      T13:  -0.0476 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0313 L22:   0.0090                                     
REMARK   3      L33:   0.6534 L12:  -0.0093                                     
REMARK   3      L13:   0.1462 L23:  -0.0442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0674 S12:  -0.1576 S13:   0.0765                       
REMARK   3      S21:  -0.3743 S22:  -0.0490 S23:   0.1712                       
REMARK   3      S31:   0.2459 S32:   0.2076 S33:   0.0094                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6357   6.1103 -61.5447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2640 T22:   0.4445                                     
REMARK   3      T33:   0.3153 T12:   0.0732                                     
REMARK   3      T13:  -0.0824 T23:  -0.0849                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1856 L22:   0.7024                                     
REMARK   3      L33:   0.9043 L12:  -0.1066                                     
REMARK   3      L13:   0.2767 L23:  -0.0168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0747 S12:   0.3060 S13:   0.0863                       
REMARK   3      S21:  -0.3115 S22:  -0.1366 S23:   0.0126                       
REMARK   3      S31:  -0.1399 S32:  -0.3327 S33:  -0.0008                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:86)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2890  -4.2856 -52.9246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3597 T22:   0.3593                                     
REMARK   3      T33:   0.3143 T12:  -0.0442                                     
REMARK   3      T13:  -0.0313 T23:  -0.0629                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0538 L22:   0.5770                                     
REMARK   3      L33:   0.5359 L12:  -0.0542                                     
REMARK   3      L13:  -0.1648 L23:   0.4534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0781 S12:   0.2434 S13:  -0.0439                       
REMARK   3      S21:  -0.1155 S22:  -0.1693 S23:   0.0386                       
REMARK   3      S31:   0.5495 S32:   0.0695 S33:  -0.0074                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 87:142)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3090   4.6399 -50.3098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1961 T22:   0.3488                                     
REMARK   3      T33:   0.2721 T12:   0.0221                                     
REMARK   3      T13:  -0.0882 T23:  -0.0881                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5536 L22:   0.1622                                     
REMARK   3      L33:   0.6006 L12:   0.3230                                     
REMARK   3      L13:   0.2268 L23:   0.1461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:   0.1752 S13:  -0.1582                       
REMARK   3      S21:  -0.2557 S22:  -0.2172 S23:   0.0825                       
REMARK   3      S31:   0.3045 S32:  -0.4991 S33:  -0.0120                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 143:190)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3105   6.7368 -54.0317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3099 T22:   0.3635                                     
REMARK   3      T33:   0.2861 T12:   0.0174                                     
REMARK   3      T13:  -0.0322 T23:  -0.0648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1282 L22:   0.1281                                     
REMARK   3      L33:   0.7286 L12:   0.1347                                     
REMARK   3      L13:  -0.0386 L23:  -0.0379                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1592 S12:   0.3240 S13:  -0.1130                       
REMARK   3      S21:  -0.2351 S22:  -0.0886 S23:   0.0934                       
REMARK   3      S31:  -0.1263 S32:   0.2206 S33:   0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 191:255)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1798   8.2124 -44.1651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2267 T22:   0.3075                                     
REMARK   3      T33:   0.2643 T12:   0.0043                                     
REMARK   3      T13:  -0.0305 T23:  -0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0075 L22:   0.2716                                     
REMARK   3      L33:   0.9570 L12:  -0.1866                                     
REMARK   3      L13:   0.0636 L23:   0.2967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0677 S12:  -0.0016 S13:  -0.0485                       
REMARK   3      S21:   0.0236 S22:   0.0025 S23:  -0.0339                       
REMARK   3      S31:  -0.0771 S32:   0.2105 S33:   0.0001                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 256:297)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4756  -9.8867 -46.8130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4227 T22:   0.3671                                     
REMARK   3      T33:   0.3215 T12:   0.1473                                     
REMARK   3      T13:  -0.0921 T23:  -0.0778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2412 L22:   0.2535                                     
REMARK   3      L33:   0.1356 L12:  -0.2569                                     
REMARK   3      L13:   0.1066 L23:   0.0365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0622 S12:   0.0922 S13:  -0.1681                       
REMARK   3      S21:   0.0286 S22:  -0.0414 S23:  -0.0218                       
REMARK   3      S31:   0.3512 S32:   0.5162 S33:  -0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 298:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2876  14.2963 -40.1912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1739 T22:   0.2684                                     
REMARK   3      T33:   0.2728 T12:  -0.0455                                     
REMARK   3      T13:  -0.0219 T23:  -0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4274 L22:   0.3005                                     
REMARK   3      L33:   0.7741 L12:  -0.2992                                     
REMARK   3      L13:   0.0964 L23:   0.2516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1014 S12:   0.2486 S13:   0.1285                       
REMARK   3      S21:   0.0067 S22:   0.1129 S23:  -0.0960                       
REMARK   3      S31:   0.0292 S32:   0.3509 S33:  -0.0001                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 332:382)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8485  -6.1946 -22.0912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5538 T22:   0.2004                                     
REMARK   3      T33:   0.3377 T12:   0.0191                                     
REMARK   3      T13:  -0.0361 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1683 L22:   0.3401                                     
REMARK   3      L33:   0.2821 L12:   0.0680                                     
REMARK   3      L13:  -0.0702 L23:   0.0906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1290 S12:  -0.1209 S13:   0.0046                       
REMARK   3      S21:   0.2211 S22:   0.0258 S23:  -0.0245                       
REMARK   3      S31:   0.5619 S32:   0.2245 S33:   0.0006                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 383:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7352   5.8360 -29.0308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1865 T22:   0.2232                                     
REMARK   3      T33:   0.2259 T12:  -0.0454                                     
REMARK   3      T13:  -0.0048 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1448 L22:   0.6458                                     
REMARK   3      L33:   1.4030 L12:   0.3314                                     
REMARK   3      L13:  -0.1232 L23:   0.3301                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1272 S12:  -0.0905 S13:   0.0418                       
REMARK   3      S21:   0.1870 S22:  -0.1625 S23:   0.0317                       
REMARK   3      S31:   0.0814 S32:  -0.1277 S33:  -0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0503  22.4945 -28.6338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3733 T22:   0.3490                                     
REMARK   3      T33:   0.3594 T12:   0.0523                                     
REMARK   3      T13:  -0.0191 T23:  -0.0593                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1012 L22:   0.1330                                     
REMARK   3      L33:   0.3725 L12:  -0.0023                                     
REMARK   3      L13:  -0.1959 L23:   0.0712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0429 S12:  -0.5460 S13:   0.2598                       
REMARK   3      S21:   0.0021 S22:  -0.0191 S23:   0.3205                       
REMARK   3      S31:  -0.3827 S32:  -0.4171 S33:   0.0010                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:543)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3573  11.4043 -21.5981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3900 T22:   0.4073                                     
REMARK   3      T33:   0.2502 T12:  -0.0125                                     
REMARK   3      T13:  -0.0043 T23:  -0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0023 L22:  -0.0104                                     
REMARK   3      L33:   0.4414 L12:  -0.0212                                     
REMARK   3      L13:   0.0037 L23:  -0.0913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:   0.0358 S13:  -0.0356                       
REMARK   3      S21:   0.1517 S22:  -0.0224 S23:   0.1543                       
REMARK   3      S31:   0.0937 S32:   0.2484 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 4ARA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52170.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-12                          
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               : MAX II                             
REMARK 200  BEAMLINE                       : I911-5                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : RH-COATED SI MIRROR, BENT FOR      
REMARK 200                                   VERTICAL COLLIMATION               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70472                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.98                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.56                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 30 % (V/V)                  
REMARK 280  POLYETHELENEGLYCOLEMONOMETHYLETHER, PH 7                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.38200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.67000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.00600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.67000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.38200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.00600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.2 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     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  23    CG   CD   CE   NZ                                   
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 268    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 268    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 496    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   285     O    HOH A  2223              2.19            
REMARK 500   NH1  ARG B   274     O    HOH B  2037              2.19            
REMARK 500   ND2  ASN B   350     O5   NAG B  1552              1.32            
REMARK 500   OH7  1PE B  1546     O    HOH B  2266              2.15            
REMARK 500   O    HOH B  2026     O    HOH B  2089              2.11            
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   NH1  ARG A    13     O    SER B    57     2555     2.16            
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    PHE A  47      -10.11     71.89                                   
REMARK 500    ALA A  62       52.11   -119.48                                   
REMARK 500    ALA A 167       72.36   -155.87                                   
REMARK 500    SER A 203     -118.29     59.00                                   
REMARK 500    PRO A 217        2.48    -67.65                                   
REMARK 500    ASP A 306      -85.30   -133.61                                   
REMARK 500    HIS A 387       57.31   -143.74                                   
REMARK 500    VAL A 407      -66.15   -126.45                                   
REMARK 500    ARG A 493       50.43   -115.59                                   
REMARK 500    ASP A 494       91.17   -160.67                                   
REMARK 500    SER A 541       46.35    -89.92                                   
REMARK 500    ALA B  62       52.18   -118.38                                   
REMARK 500    ALA B 167       70.08   -150.67                                   
REMARK 500    SER B 203     -119.33     55.59                                   
REMARK 500    ASP B 306      -78.00   -121.57                                   
REMARK 500    ASN B 350     -167.19   -128.83                                   
REMARK 500    VAL B 407      -65.39   -127.24                                   
REMARK 500    SER B 497      125.90     65.05                                   
REMARK 500    SER B 541       31.90    -82.58                                   
REMARK 500    ALA B 542      -13.97   -163.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR B 337        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-                        
REMARK 600  2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE (568):                      
REMARK 600  CORRESPONDING TO LIGAND C56 IN THE RACEMIC STRUCTURE 4A23           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1555                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1556                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1549 BOUND TO ASN A 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1553 BOUND TO ASN A 464                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B1552 BOUND TO ASN B 350                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE              
REMARK 900  APOFORM                                                             
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  DECIDIUM COMPLEX                                                    
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  GALLAMINE COMPLEX                                                   
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  PROPIDIUM COMPLEX                                                   
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6SYN COMPLEX                                                   
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6ANTI COMPLEX                                                  
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY                
REMARK 900  TABUN                                                               
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY            
REMARK 900   TABUN                                                              
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)                            
REMARK 900  TRIFLUOROACETOPHENONE                                               
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                           
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH SUCCINYLCHOLINE                                       
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH CHOLINE                                               
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE              
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE                
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE            
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE         
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7             
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND HLO-7                                                           
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND ORTHO-7                                                         
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED METHAMIDOPHOS                                           
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED FENAMIPHOS                                              
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED SARIN                                                   
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED VX                                                      
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                       
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED METHAMIDOPHOS                                               
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED FENAMIPHOS                                                  
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED VX AND SARIN                                                
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                           
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN AND IN COMPLEX WITH HI-6                                     
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN (AGED) IN COMPLEX WITH HI-6                                  
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH           
REMARK 900   K027                                                               
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN           
REMARK 900   COMPLEX WITH AMTS13                                                
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND HI-6                                           
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND ORTHO-7                                        
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE                      
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 MTH)                                                              
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 WK)                                                               
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   WK)                                                                
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   MTH)                                                               
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (               
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX                  
REMARK 900  WITH SOAKED TZ2PA6 ANTI INHIBITOR                                   
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 SYN INHIBITOR                                   
REMARK 900 RELATED ID: 2XUQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS                             
REMARK 900 RELATED ID: 4A16   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH                
REMARK 900  HUPRINE DERIVATIVE                                                  
REMARK 900 RELATED ID: 4A23   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC           
REMARK 900   C5685                                                              
REMARK 900 RELATED ID: 4ARB   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-              
REMARK 900  C5685 AT 2.25 A RESOLUTION.                                         
DBREF  4ARA A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4ARA B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 4ARA ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARA PRO B  548  UNP  P21836              EXPRESSION TAG                 
SEQRES   1 A  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  548  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 A  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 A  548  ALA PRO                                                      
SEQRES   1 B  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  548  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 B  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 B  548  ALA PRO                                                      
HET    C56  A 600      50                                                       
HET    PEG  A1544       7                                                       
HET    EDO  A1545       4                                                       
HET    PEG  A1546       7                                                       
HET    PEG  A1547       7                                                       
HET    EDO  A1548       4                                                       
HET    NAG  A1549      14                                                       
HET    EDO  A1550       4                                                       
HET    EDO  A1551       4                                                       
HET    EDO  A1552       4                                                       
HET    NAG  A1553      14                                                       
HET    C56  B 600      50                                                       
HET    PEG  B1545       7                                                       
HET    1PE  B1546      16                                                       
HET    PEG  B1547       7                                                       
HET    PEG  B1548       7                                                       
HET    EDO  B1549       4                                                       
HET    PEG  B1550       7                                                       
HET    PEG  B1551       7                                                       
HET    NAG  B1552      14                                                       
HET    EDO  B1553       4                                                       
HET    PEG  B1554       7                                                       
HET     CL  B1555       1                                                       
HET    EDO  B1556       4                                                       
HETNAM     C56 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-                    
HETNAM   2 C56  2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     1PE PEG400                                                           
FORMUL   3  C56    2(C17 H26 N4 O4)                                             
FORMUL   4  PEG    9(C4 H10 O3)                                                 
FORMUL   5  EDO    8(C2 H6 O2)                                                  
FORMUL   6  NAG    3(C8 H15 N O6)                                               
FORMUL   7  1PE    C10 H22 O6                                                   
FORMUL   8   CL    CL 1-                                                        
FORMUL   9  HOH   *628(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLU A  142  1                                   8    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SER A  203  SER A  215  1                                  13    
HELIX   10  10 LEU A  216  ARG A  219  5                                   4    
HELIX   11  11 SER A  240  GLY A  256  1                                  17    
HELIX   12  12 ASN A  265  ARG A  274  1                                  10    
HELIX   13  13 PRO A  277  HIS A  284  1                                   8    
HELIX   14  14 GLU A  285  LEU A  289  5                                   5    
HELIX   15  15 THR A  311  THR A  318  1                                   8    
HELIX   16  16 GLY A  335  GLY A  342  5                                   8    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  SER A  541  1                                   8    
HELIX   28  28 VAL B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  GLU B  142  1                                   8    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  ILE B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 SER B  203  LEU B  214  1                                  12    
HELIX   36  36 SER B  215  LEU B  221  5                                   7    
HELIX   37  37 SER B  240  GLY B  256  1                                  17    
HELIX   38  38 ASN B  265  THR B  275  1                                  11    
HELIX   39  39 PRO B  277  ASP B  283  1                                   7    
HELIX   40  40 HIS B  284  LEU B  289  5                                   6    
HELIX   41  41 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  GLY B  342  5                                   8    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  PHE B  455  1                                   6    
HELIX   49  49 GLY B  456  ASP B  460  5                                   5    
HELIX   50  50 ASP B  460  ASN B  464  5                                   5    
HELIX   51  51 THR B  466  GLY B  487  1                                  22    
HELIX   52  52 ARG B  525  ARG B  534  1                                  10    
HELIX   53  53 PHE B  535  SER B  541  1                                   7    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.04  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
LINK         ND2 ASN A 350                 C1  NAG A1549     1555   1555  1.47  
LINK         ND2 ASN A 464                 C1  NAG A1553     1555   1555  1.46  
LINK         ND2 ASN B 350                 C1  NAG B1552     1555   1555  1.47  
CISPEP   1 TYR A  105    PRO A  106          0        -0.99                     
CISPEP   2 TYR B  105    PRO B  106          0         1.55                     
CISPEP   3 SER B  497    PRO B  498          0        11.72                     
SITE     1 AC1 13 TYR A  72  ASP A  74  TRP A  86  TYR A 124                    
SITE     2 AC1 13 TRP A 286  ILE A 294  PHE A 295  ARG A 296                    
SITE     3 AC1 13 TYR A 337  PHE A 338  TYR A 341  HOH A2236                    
SITE     4 AC1 13 HOH A2258                                                     
SITE     1 AC2  3 ASP A 304  SER A 309  ASP A 310                               
SITE     1 AC3  1 GLU A 313                                                     
SITE     1 AC4  2 ASP A 323  PEG A1547                                          
SITE     1 AC5  5 ILE A 213  ARG A 219  PHE A 222  ASP A 323                    
SITE     2 AC5  5 PEG A1546                                                     
SITE     1 AC6  1 GLU A 313                                                     
SITE     1 AC7  1 ASP A   5                                                     
SITE     1 AC8  3 SER A  57  VAL A  59  HOH A2346                               
SITE     1 AC9  2 THR A  63  HOH A2347                                          
SITE     1 BC1 15 TYR B  72  ASP B  74  TRP B  86  GLY B 121                    
SITE     2 BC1 15 GLY B 122  TYR B 124  TRP B 286  SER B 293                    
SITE     3 BC1 15 ILE B 294  PHE B 295  ARG B 296  TYR B 337                    
SITE     4 BC1 15 PHE B 338  TYR B 341  HOH B2176                               
SITE     1 BC2  6 THR B 112  PRO B 113  GLU B 142  GLY B 143                    
SITE     2 BC2  6 ALA B 144  ARG B 485                                          
SITE     1 BC3 11 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 BC3 11 ALA B 377  LEU B 380  HIS B 381  PHE B 531                    
SITE     3 BC3 11 PHE B 535  HOH B2203  HOH B2266                               
SITE     1 BC4  2 ASP B 323  EDO B1549                                          
SITE     1 BC5  3 HIS B 381  TYR B 382  HOH B2268                               
SITE     1 BC6  2 ARG B 219  PEG B1547                                          
SITE     1 BC7  3 ARG B  11  GLU B 185  HOH B2269                               
SITE     1 BC8  5 LYS B 332  ASP B 333  ASP B 396  LEU B 441                    
SITE     2 BC8  5 TRP B 442                                                     
SITE     1 BC9  1 GLU B 313                                                     
SITE     1 CC1  1 SER B 309                                                     
SITE     1 CC2  1 SER B 240                                                     
SITE     1 CC3  1 LYS B 516                                                     
SITE     1 CC4  5 SER A 347  ASN A 350  HOH A2261  HOH A2344                    
SITE     2 CC4  5 HOH A2345                                                     
SITE     1 CC5  1 ASN A 464                                                     
SITE     1 CC6  3 SER B 347  ASN B 350  HOH B2270                               
CRYST1   78.764  112.012  227.340  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012696  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004399        0.00000                         
TER    4174      ALA A 542                                                      
TER    8338      THR B 543                                                      
MASTER      867    0   24   53   32    0   36    6 9218    2  268   86          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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