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LongText Report for: 4B83-pdb

Name Class
4B83-pdb
HEADER    HYDROLASE                               24-AUG-12   4B83              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-               
TITLE    2 DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE                     
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;                                                     
COMPND   8 OTHER_DETAILS: LIGAND N-(2-DIETHYLAMINO-ETHYL)-3-METHOXY-            
COMPND   9  BENZENESULFONAMIDE                                                  
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_CELL_LINE: HEK 293F;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    HYDROLASE, INHIBITOR                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,W.QIAN,         
AUTHOR   2 F.EKSTROM,A.LINUSSON                                                 
REVDAT   1   04-SEP-13 4B83    0                                                
JRNL        AUTH   C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,       
JRNL        AUTH 2 W.QIAN,F.EKSTROM,A.LINUSSON                                  
JRNL        TITL   DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY   
JRNL        TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.400                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.042                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.69                          
REMARK   3   NUMBER OF REFLECTIONS             : 80034                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1937                          
REMARK   3   R VALUE            (WORKING SET) : 0.1931                          
REMARK   3   FREE R VALUE                     : 0.2223                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1582                            
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 29.0445 -  5.3276    0.99     7439   146  0.1810 0.2045        
REMARK   3     2  5.3276 -  4.2328    1.00     7247   145  0.1416 0.1377        
REMARK   3     3  4.2328 -  3.6990    1.00     7167   141  0.1659 0.2047        
REMARK   3     4  3.6990 -  3.3613    1.00     7132   137  0.2026 0.2489        
REMARK   3     5  3.3613 -  3.1207    1.00     7128   144  0.2185 0.2467        
REMARK   3     6  3.1207 -  2.9369    1.00     7065   153  0.2281 0.2288        
REMARK   3     7  2.9369 -  2.7899    1.00     7097   143  0.2314 0.3040        
REMARK   3     8  2.7899 -  2.6686    1.00     7042   142  0.2357 0.2960        
REMARK   3     9  2.6686 -  2.5659    1.00     7037   160  0.2353 0.2787        
REMARK   3    10  2.5659 -  2.4774    1.00     7045   132  0.2453 0.2735        
REMARK   3    11  2.4774 -  2.4000    1.00     7053   139  0.2709 0.3258        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.352                                         
REMARK   3   B_SOL              : 52.824                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.33             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.68            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.29                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.7734                                              
REMARK   3    B22 (A**2) : 13.5417                                              
REMARK   3    B33 (A**2) : -24.3150                                             
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      :  0.007           8845                                  
REMARK   3   ANGLE     :  1.074          12039                                  
REMARK   3   CHIRALITY :  0.076           1282                                  
REMARK   3   PLANARITY :  0.005           1565                                  
REMARK   3   DIHEDRAL  : 14.926           3256                                  
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):  30.5140  15.3713  32.3561              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3504 T22:   0.3204                                     
REMARK   3      T33:   0.3403 T12:   0.0137                                     
REMARK   3      T13:  -0.0227 T23:   0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0882 L22:   0.6209                                     
REMARK   3      L33:   0.9298 L12:  -0.1891                                     
REMARK   3      L13:   0.0422 L23:  -0.4553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1079 S12:  -0.0722 S13:   0.0888                       
REMARK   3      S21:   0.1630 S22:   0.0427 S23:  -0.0774                       
REMARK   3      S31:  -0.0704 S32:   0.0251 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 143:255)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9392   5.6878  19.8220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2718 T22:   0.2013                                     
REMARK   3      T33:   0.2767 T12:   0.0445                                     
REMARK   3      T13:   0.0056 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0212 L22:   0.5173                                     
REMARK   3      L33:   0.9571 L12:   0.3645                                     
REMARK   3      L13:   0.1725 L23:  -0.2813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0528 S12:   0.0619 S13:  -0.0707                       
REMARK   3      S21:   0.0269 S22:   0.0048 S23:  -0.0634                       
REMARK   3      S31:   0.1791 S32:   0.0484 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 256:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0350   9.2175  11.5148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2774 T22:   0.2346                                     
REMARK   3      T33:   0.3358 T12:   0.0461                                     
REMARK   3      T13:   0.0219 T23:   0.0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6431 L22:  -0.0548                                     
REMARK   3      L33:   0.8776 L12:   0.1829                                     
REMARK   3      L13:   0.0285 L23:  -0.2827                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0844 S12:   0.1380 S13:   0.0085                       
REMARK   3      S21:  -0.0079 S22:   0.0119 S23:  -0.0284                       
REMARK   3      S31:   0.1691 S32:   0.2361 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 332:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9126  17.4918   6.4022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2709 T22:   0.2749                                     
REMARK   3      T33:   0.3392 T12:  -0.0200                                     
REMARK   3      T13:  -0.0013 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3586 L22:   0.1749                                     
REMARK   3      L33:   1.5274 L12:  -0.1109                                     
REMARK   3      L13:   0.5146 L23:  -0.1664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0642 S12:   0.0997 S13:  -0.0011                       
REMARK   3      S21:  -0.1081 S22:  -0.0044 S23:   0.0546                       
REMARK   3      S31:   0.0338 S32:  -0.2414 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7079   1.3122  13.9330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5266 T22:   0.5897                                     
REMARK   3      T33:   0.5448 T12:  -0.1847                                     
REMARK   3      T13:   0.0031 T23:   0.0442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0896 L22:   0.1913                                     
REMARK   3      L33:   0.1822 L12:  -0.1257                                     
REMARK   3      L13:   0.1629 L23:  -0.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1931 S12:   0.2274 S13:  -0.2053                       
REMARK   3      S21:   0.0360 S22:   0.2206 S23:   0.3257                       
REMARK   3      S31:   0.5216 S32:  -0.9062 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6258   6.4360  -1.0784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3042 T22:   0.4207                                     
REMARK   3      T33:   0.3341 T12:  -0.0372                                     
REMARK   3      T13:  -0.0498 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1427 L22:  -0.0562                                     
REMARK   3      L33:   0.6037 L12:  -0.0107                                     
REMARK   3      L13:   0.3453 L23:  -0.0225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0527 S12:  -0.1029 S13:   0.0946                       
REMARK   3      S21:  -0.2995 S22:  -0.1137 S23:   0.2343                       
REMARK   3      S31:   0.0565 S32:   0.0858 S33:  -0.0065                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6788   6.2755 -61.8803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3910 T22:   0.5126                                     
REMARK   3      T33:   0.4021 T12:   0.0724                                     
REMARK   3      T13:  -0.0790 T23:  -0.1016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1498 L22:   0.4826                                     
REMARK   3      L33:   0.6522 L12:   0.0654                                     
REMARK   3      L13:   0.1695 L23:  -0.0155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0541 S12:   0.4536 S13:  -0.0278                       
REMARK   3      S21:  -0.3975 S22:  -0.1261 S23:   0.0691                       
REMARK   3      S31:  -0.0372 S32:  -0.2271 S33:  -0.0001                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:71)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1549   0.3329 -61.5622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4617 T22:   0.4768                                     
REMARK   3      T33:   0.3254 T12:   0.0427                                     
REMARK   3      T13:  -0.0513 T23:  -0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1708 L22:   0.0941                                     
REMARK   3      L33:   0.2390 L12:  -0.2345                                     
REMARK   3      L13:  -0.1502 L23:   0.2794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1084 S12:   0.1843 S13:  -0.0680                       
REMARK   3      S21:  -0.2331 S22:  -0.0933 S23:  -0.0308                       
REMARK   3      S31:   0.5073 S32:   0.0669 S33:  -0.0001                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 72:158)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9996   1.6023 -48.4748              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2973 T22:   0.3152                                     
REMARK   3      T33:   0.3107 T12:  -0.0068                                     
REMARK   3      T13:  -0.0403 T23:  -0.0760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0280 L22:   0.1674                                     
REMARK   3      L33:   1.2167 L12:   0.2851                                     
REMARK   3      L13:   0.2863 L23:   0.5573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0849 S12:   0.2240 S13:  -0.0605                       
REMARK   3      S21:  -0.0853 S22:  -0.1558 S23:   0.0736                       
REMARK   3      S31:   0.2988 S32:  -0.1731 S33:  -0.0013                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 159:190)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3671   8.8665 -55.7789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3859 T22:   0.5112                                     
REMARK   3      T33:   0.3684 T12:   0.0256                                     
REMARK   3      T13:  -0.0128 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2281 L22:   0.1385                                     
REMARK   3      L33:   0.1599 L12:   0.2385                                     
REMARK   3      L13:   0.0589 L23:  -0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0813 S12:   0.1554 S13:   0.1923                       
REMARK   3      S21:  -0.2409 S22:  -0.0100 S23:  -0.1086                       
REMARK   3      S31:  -0.1368 S32:   0.2165 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 191:237)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9667  14.1142 -44.0985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3084 T22:   0.3720                                     
REMARK   3      T33:   0.3159 T12:   0.0216                                     
REMARK   3      T13:  -0.0190 T23:  -0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1203 L22:   0.2426                                     
REMARK   3      L33:   0.2367 L12:  -0.2217                                     
REMARK   3      L13:  -0.0434 L23:   0.2723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:   0.0414 S13:   0.0247                       
REMARK   3      S21:   0.0903 S22:  -0.0062 S23:   0.0170                       
REMARK   3      S31:  -0.1769 S32:  -0.0121 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 238:300)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4339  -8.1447 -46.1979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4629 T22:   0.5156                                     
REMARK   3      T33:   0.3921 T12:   0.1680                                     
REMARK   3      T13:  -0.0846 T23:  -0.0767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2530 L22:   0.3351                                     
REMARK   3      L33:   0.2370 L12:  -0.2332                                     
REMARK   3      L13:   0.3166 L23:  -0.0210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0763 S12:   0.0167 S13:   0.0480                       
REMARK   3      S21:   0.1456 S22:   0.1572 S23:  -0.0698                       
REMARK   3      S31:   0.4089 S32:   0.7032 S33:  -0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 301:341)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0852  10.9454 -36.8177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3667 T22:   0.3652                                     
REMARK   3      T33:   0.3917 T12:  -0.0572                                     
REMARK   3      T13:  -0.0147 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5166 L22:   0.3090                                     
REMARK   3      L33:   0.8588 L12:  -0.2779                                     
REMARK   3      L13:  -0.0005 L23:   0.4931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1348 S12:   0.0392 S13:   0.0297                       
REMARK   3      S21:   0.1591 S22:  -0.1044 S23:  -0.0447                       
REMARK   3      S31:   0.0124 S32:   0.2991 S33:  -0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 342:406)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1444  -5.0184 -18.0758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6577 T22:   0.3704                                     
REMARK   3      T33:   0.3813 T12:  -0.0312                                     
REMARK   3      T13:  -0.0633 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4501 L22:   0.2681                                     
REMARK   3      L33:   0.2378 L12:   0.3368                                     
REMARK   3      L13:   0.1479 L23:   0.2937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1618 S12:  -0.3365 S13:   0.0765                       
REMARK   3      S21:   0.0909 S22:  -0.0661 S23:  -0.0217                       
REMARK   3      S31:   0.6967 S32:   0.1631 S33:   0.0001                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 407:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4825   8.5069 -33.4091              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2791 T22:   0.3417                                     
REMARK   3      T33:   0.3745 T12:  -0.0412                                     
REMARK   3      T13:  -0.0064 T23:  -0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0530 L22:   0.5182                                     
REMARK   3      L33:   1.1179 L12:   0.0406                                     
REMARK   3      L13:  -0.0627 L23:   0.5884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0900 S12:  -0.0389 S13:   0.0157                       
REMARK   3      S21:   0.1474 S22:  -0.1603 S23:   0.0532                       
REMARK   3      S31:  -0.0214 S32:  -0.2438 S33:  -0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1337  22.5060 -28.8858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4178 T22:   0.3452                                     
REMARK   3      T33:   0.3862 T12:   0.0021                                     
REMARK   3      T13:   0.0281 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0483 L22:   0.1184                                     
REMARK   3      L33:   0.1853 L12:  -0.0703                                     
REMARK   3      L13:  -0.1147 L23:   0.1224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0542 S12:  -0.3598 S13:   0.0701                       
REMARK   3      S21:   0.2920 S22:   0.0667 S23:   0.1847                       
REMARK   3      S31:  -0.3250 S32:  -0.3585 S33:   0.0001                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5741  11.8498 -21.5916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3902 T22:   0.4943                                     
REMARK   3      T33:   0.3012 T12:  -0.0092                                     
REMARK   3      T13:   0.0003 T23:  -0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0047 L22:  -0.0665                                     
REMARK   3      L33:   0.2546 L12:  -0.0278                                     
REMARK   3      L13:   0.1103 L23:  -0.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1635 S12:  -0.2322 S13:  -0.0195                       
REMARK   3      S21:   0.1935 S22:   0.1085 S23:   0.1046                       
REMARK   3      S31:  -0.0286 S32:   0.1715 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DUE TO INSUFFICIENT ELECTRON              
REMARK   3    DENSITY THE FOLLOWING RESIDUES WERE NOT MODELED CHAIN A           
REMARK   3    259-263 AND 543-548, CHAIN B 1-3, 259-264 AND 543-548.            
REMARK   3    DUE TO INSUFFICIENT ELECTRON DENSITY THE FOLLOWING                
REMARK   3    RESIDUES WERE MODELED AS ALANINES, CHAIN A 496 AND CHAIN          
REMARK   3    B 493 AND 496.                                                    
REMARK   4                                                                      
REMARK   4 4B83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-53845.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.041                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 80333                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.22                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS 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   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (W/V) PEG750MME, 0.1 M           
REMARK 280  HEPES PH 7.0-7.1                                                    
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       39.79150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.89150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.92800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.89150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.79150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.92800            
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: 8410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.6 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   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   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     THR B   543                                                      
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 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 258    CG   CD                                             
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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 258   N   -  CA  -  CB  ANGL. DEV. =   7.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -6.19     76.20                                   
REMARK 500    PHE A 158       -3.19   -141.68                                   
REMARK 500    ALA A 167       70.35   -153.29                                   
REMARK 500    SER A 203     -121.93     57.12                                   
REMARK 500    ASP A 306      -82.85   -124.03                                   
REMARK 500    VAL A 407      -59.91   -125.34                                   
REMARK 500    ASP A 494       59.75   -159.38                                   
REMARK 500    LEU A 518      127.70    -38.14                                   
REMARK 500    ARG A 525       53.83     38.82                                   
REMARK 500    PHE B  47       -4.14     72.48                                   
REMARK 500    CYS B  96       11.92   -143.47                                   
REMARK 500    ALA B 167       75.01   -156.81                                   
REMARK 500    SER B 203     -120.46     52.70                                   
REMARK 500    ASP B 306      -85.44   -117.33                                   
REMARK 500    VAL B 407      -62.78   -125.66                                   
REMARK 500    SER B 497      -79.41   -106.06                                   
REMARK 500    ASN B 514     -166.66   -162.72                                   
REMARK 500    SER B 541        8.11    -64.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     B3V A 1553                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO 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 EDO A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V A1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 A1556                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3V B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1545                 
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 B3V B1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1546 BOUND TO ASN A 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1549 BOUND TO ASN A 464                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B1546 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: 4ARA   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-              
REMARK 900  C5685 AT 2.5 A RESOLUTION.                                          
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.                                         
REMARK 900 RELATED ID: 4B7Z   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE           
REMARK 900 RELATED ID: 4B80   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE          
REMARK 900 RELATED ID: 4B81   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH C-(4-             
REMARK 900  CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE          
REMARK 900 RELATED ID: 4B82   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE                  
REMARK 900 RELATED ID: 4B84   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE            
REMARK 900 RELATED ID: 4B85   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-                
REMARK 900  CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE               
DBREF  4B83 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4B83 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 4B83 ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B83 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    B3V  A1543      19                                                       
HET    EDO  A1544       4                                                       
HET    EDO  A1545       4                                                       
HET    NAG  A1546      14                                                       
HET    PEG  A1547       7                                                       
HET    PEG  A1548       7                                                       
HET    NAG  A1549      14                                                       
HET    EDO  A1550       4                                                       
HET    EDO  A1551       4                                                       
HET    EDO  A1552       4                                                       
HET    B3V  A1553      12                                                       
HET    SO4  A1554       5                                                       
HET    EDO  A1555       4                                                       
HET    PE8  A1556      25                                                       
HET    EDO  B1543       4                                                       
HET    B3V  B1544      19                                                       
HET    EDO  B1545       4                                                       
HET    NAG  B1546      14                                                       
HET    PEG  B1547       7                                                       
HET    EDO  B1548       4                                                       
HET    B3V  B1549      19                                                       
HET    SO4  B1550       5                                                       
HET    EDO  B1551       4                                                       
HET    PG4  B1552      13                                                       
HET    EDO  B1553       4                                                       
HET    EDO  B2000       4                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     B3V N-[2-(DIETHYLAMINO)ETHYL]-3-METHOXY-                             
HETNAM   2 B3V  BENZENESULFONAMIDE                                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  PG4    C8 H18 O5                                                    
FORMUL   4  B3V    4(C13 H22 N2 O3 S)                                           
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   6  EDO    12(C2 H6 O2)                                                 
FORMUL   7  PEG    3(C4 H10 O3)                                                 
FORMUL   8  PE8    C16 H34 O9                                                   
FORMUL   9  NAG    3(C8 H15 N O6)                                               
FORMUL  10  HOH   *374(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  GLY A  143  1                                   9    
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  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  PHE A  222  5                                   8    
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  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
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  ALA A  542  1                                   9    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 SER B  203  LEU B  214  1                                  12    
HELIX   37  37 SER B  215  PHE B  222  5                                   8    
HELIX   38  38 ALA B  241  VAL B  255  1                                  15    
HELIX   39  39 ASN B  265  THR B  275  1                                  11    
HELIX   40  40 PRO B  277  ASP B  283  1                                   7    
HELIX   41  41 HIS B  284  LEU B  289  5                                   6    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 GLY B  335  VAL B  340  1                                   6    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  PHE B  455  1                                   6    
HELIX   50  50 GLY B  456  ASP B  460  5                                   5    
HELIX   51  51 ASP B  460  ASN B  464  5                                   5    
HELIX   52  52 THR B  466  GLY B  487  1                                  22    
HELIX   53  53 ARG B  525  ARG B  534  1                                  10    
HELIX   54  54 ARG B  534  SER B  541  1                                   8    
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           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.05  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.05  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.05  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         ND2 ASN A 350                 C1  NAG A1546     1555   1555  1.45  
LINK         ND2 ASN A 464                 C1  NAG A1549     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B1546     1555   1555  1.45  
CISPEP   1 TYR A  105    PRO A  106          0        -5.12                     
CISPEP   2 TYR B  105    PRO B  106          0        -0.14                     
CISPEP   3 CYS B  257    PRO B  258          0         0.57                     
CISPEP   4 SER B  497    PRO B  498          0        -8.64                     
SITE     1 AC1 13 TRP A  86  GLY A 120  GLY A 121  GLY A 122                    
SITE     2 AC1 13 TYR A 124  TRP A 286  PHE A 297  TYR A 337                    
SITE     3 AC1 13 PHE A 338  TYR A 341  HIS A 447  GLY A 448                    
SITE     4 AC1 13 HOH A2154                                                     
SITE     1 AC2  2 GLY A 163  ARG A 165                                          
SITE     1 AC3  2 SER A  57  VAL A  59                                          
SITE     1 AC4  1 ASP A   5                                                     
SITE     1 AC5  3 ILE A  20  THR A  63  PRO B 492                               
SITE     1 AC6  4 THR A 112  GLU A 142  GLY A 143  ARG A 485                    
SITE     1 AC7  7 ILE A 213  ARG A 219  PHE A 222  PHE A 321                    
SITE     2 AC7  7 GLN A 322  ASP A 323  LEU A 324                               
SITE     1 AC8  5 LYS A  23  ALA A  24  PRO A  25  ARG A 136                    
SITE     2 AC8  5 ASP A 460                                                     
SITE     1 AC9 14 ALA A 377  LEU A 380  HIS A 381  GLN A 527                    
SITE     2 AC9 14 PHE A 531  PHE A 535  HOH A2212  ALA B 377                    
SITE     3 AC9 14 LEU B 380  HIS B 381  GLN B 527  PHE B 531                    
SITE     4 AC9 14 PHE B 535  PG4 B1552                                          
SITE     1 BC1  5 PRO B 113  GLU B 142  GLY B 143  ALA B 144                    
SITE     2 BC1  5 ARG B 485                                                     
SITE     1 BC2  9 TRP B  86  TYR B 124  TRP B 286  PHE B 297                    
SITE     2 BC2  9 TYR B 337  PHE B 338  TYR B 341  HIS B 447                    
SITE     3 BC2  9 HOH B2115                                                     
SITE     1 BC3  2 ARG B 356  GLU B 389                                          
SITE     1 BC4  3 ARG B  11  ARG B  13  GLU B 185                               
SITE     1 BC5  8 ILE B 213  ARG B 219  PHE B 222  ASP B 320                    
SITE     2 BC5  8 PHE B 321  GLN B 322  ASP B 323  LEU B 324                    
SITE     1 BC6  4 LYS B  23  PRO B  25  ARG B 136  ASP B 460                    
SITE     1 BC7  5 GLN A 527  PE8 A1556  HIS B 381  TYR B 382                    
SITE     2 BC7  5 ASP B 384                                                     
SITE     1 BC8  1 THR B 486                                                     
SITE     1 BC9  1 GLN B 413                                                     
SITE     1 CC1  3 SER A 347  ASN A 350  HOH A2166                               
SITE     1 CC2  2 SER A 462  ASN A 464                                          
SITE     1 CC3  2 SER B 347  ASN B 350                                          
CRYST1   79.583  111.856  227.783  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      0.012565  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004390        0.00000                         
TER    4197      ALA A 542                                                      
TER    8375      ALA B 542                                                      
MASTER      830    0   26   54   34    0   34    6 8975    2  243   86          
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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