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LongText Report for: 4B81-pdb

Name Class
4B81-pdb
HEADER    HYDROLASE                               24-AUG-12   4B81              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH                     
TITLE    2 1-(4-CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE      
CAVEAT     4B81    NAG A 1549  PLANAR AT ATOM C1                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_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 4B81    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.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.003                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.71                          
REMARK   3   NUMBER OF REFLECTIONS             : 48890                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1973                          
REMARK   3   R VALUE            (WORKING SET) : 0.1965                          
REMARK   3   FREE R VALUE                     : 0.2391                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 963                             
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 29.0043 -  5.3466    0.99     7109   137  0.1751 0.2029        
REMARK   3     2  5.3466 -  4.2481    1.00     6913   137  0.1548 0.1824        
REMARK   3     3  4.2481 -  3.7123    1.00     6834   125  0.1722 0.2263        
REMARK   3     4  3.7123 -  3.3734    1.00     6809   150  0.2048 0.2473        
REMARK   3     5  3.3734 -  3.1320    1.00     6793   115  0.2351 0.3018        
REMARK   3     6  3.1320 -  2.9475    1.00     6757   158  0.2763 0.2958        
REMARK   3     7  2.9475 -  2.8000    1.00     6712   141  0.3288 0.4254        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.328                                         
REMARK   3   B_SOL              : 43.069                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.39             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.25            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.86                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.0                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 17.9764                                              
REMARK   3    B22 (A**2) : 9.7384                                               
REMARK   3    B33 (A**2) : -27.7148                                             
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      :  0.005           8745                                  
REMARK   3   ANGLE     :  0.920          11910                                  
REMARK   3   CHIRALITY :  0.066           1276                                  
REMARK   3   PLANARITY :  0.005           1551                                  
REMARK   3   DIHEDRAL  : 17.241           3187                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:71)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2320  12.9230  38.3778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4112 T22:   0.4272                                     
REMARK   3      T33:   0.3326 T12:  -0.0032                                     
REMARK   3      T13:  -0.0495 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0995 L22:   0.2052                                     
REMARK   3      L33:   0.8735 L12:   0.0115                                     
REMARK   3      L13:  -0.4680 L23:  -0.3248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0978 S12:  -0.2145 S13:   0.1629                       
REMARK   3      S21:   0.2589 S22:   0.1120 S23:  -0.1084                       
REMARK   3      S31:   0.1459 S32:   0.1254 S33:  -0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 72:158)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3653  16.1540  26.1251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3947 T22:   0.3250                                     
REMARK   3      T33:   0.3962 T12:  -0.0110                                     
REMARK   3      T13:  -0.0164 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6897 L22:   0.2696                                     
REMARK   3      L33:   0.9070 L12:  -0.3060                                     
REMARK   3      L13:   0.7414 L23:  -0.0211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0790 S12:  -0.0418 S13:   0.0776                       
REMARK   3      S21:   0.0516 S22:  -0.0077 S23:  -0.1416                       
REMARK   3      S31:  -0.0417 S32:   0.0493 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 159:190)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0856   3.2553  25.7345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4011 T22:   0.2834                                     
REMARK   3      T33:   0.3345 T12:   0.1255                                     
REMARK   3      T13:  -0.0334 T23:   0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1628 L22:   0.7217                                     
REMARK   3      L33:   0.4572 L12:   0.2493                                     
REMARK   3      L13:   0.0760 L23:  -0.3549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1963 S12:  -0.4937 S13:   0.1543                       
REMARK   3      S21:   0.0881 S22:   0.0405 S23:   0.0154                       
REMARK   3      S31:   0.6820 S32:   0.4420 S33:   0.0456                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 191:228)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7237   0.6290  21.6739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3654 T22:   0.2656                                     
REMARK   3      T33:   0.3409 T12:  -0.0506                                     
REMARK   3      T13:  -0.0061 T23:   0.0536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1248 L22:   0.0963                                     
REMARK   3      L33:   0.0516 L12:   0.0444                                     
REMARK   3      L13:  -0.0143 L23:   0.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0118 S12:   0.0111 S13:  -0.1559                       
REMARK   3      S21:   0.2509 S22:  -0.0485 S23:   0.0432                       
REMARK   3      S31:   0.3062 S32:  -0.2064 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 229:255)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  42.1335  10.5019   7.4723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4947 T22:   0.3598                                     
REMARK   3      T33:   0.3701 T12:   0.1073                                     
REMARK   3      T13:   0.0418 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1542 L22:   0.1282                                     
REMARK   3      L33:   0.6156 L12:  -0.2292                                     
REMARK   3      L13:   0.0735 L23:  -0.2355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1152 S12:   0.5208 S13:  -0.3887                       
REMARK   3      S21:  -0.0601 S22:  -0.0933 S23:  -0.0057                       
REMARK   3      S31:   0.2950 S32:   0.1734 S33:   0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 256:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2580   8.6738  11.6868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3536 T22:   0.3560                                     
REMARK   3      T33:   0.4104 T12:   0.0221                                     
REMARK   3      T13:   0.0269 T23:   0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2197 L22:   0.3102                                     
REMARK   3      L33:   1.4783 L12:   0.1504                                     
REMARK   3      L13:   0.0026 L23:  -0.4649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0165 S12:   0.3033 S13:   0.0176                       
REMARK   3      S21:   0.0704 S22:  -0.0042 S23:  -0.0775                       
REMARK   3      S31:   0.2492 S32:   0.2731 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 332:382)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0377  21.4594  -3.9128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4459 T22:   0.5083                                     
REMARK   3      T33:   0.4973 T12:   0.0109                                     
REMARK   3      T13:   0.0019 T23:   0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2959 L22:   0.3115                                     
REMARK   3      L33:   0.4102 L12:   0.0743                                     
REMARK   3      L13:  -0.4416 L23:  -0.1460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:   0.2986 S13:   0.2406                       
REMARK   3      S21:  -0.3732 S22:   0.0318 S23:  -0.0661                       
REMARK   3      S31:  -0.2938 S32:   0.0117 S33:  -0.0001                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 383:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9948  15.0292  10.8805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3193 T22:   0.3830                                     
REMARK   3      T33:   0.3703 T12:  -0.0370                                     
REMARK   3      T13:  -0.0115 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8540 L22:   0.4875                                     
REMARK   3      L33:   1.0139 L12:  -0.0024                                     
REMARK   3      L13:   0.4250 L23:   0.0542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0843 S12:   0.0576 S13:  -0.0679                       
REMARK   3      S21:  -0.1021 S22:   0.0282 S23:   0.1461                       
REMARK   3      S31:   0.0125 S32:  -0.3155 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0937   0.9211  13.9493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5830 T22:   0.4938                                     
REMARK   3      T33:   0.5577 T12:  -0.1834                                     
REMARK   3      T13:  -0.0504 T23:   0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0873 L22:   0.1171                                     
REMARK   3      L33:   0.1056 L12:  -0.0290                                     
REMARK   3      L13:   0.1523 L23:  -0.0670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2503 S12:   0.4204 S13:  -0.4885                       
REMARK   3      S21:  -0.0167 S22:   0.0865 S23:   0.4509                       
REMARK   3      S31:   0.1399 S32:  -0.0862 S33:   0.0004                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3335   5.9990  -1.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3021 T22:   0.7316                                     
REMARK   3      T33:   0.4202 T12:  -0.0691                                     
REMARK   3      T13:  -0.1465 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1973 L22:   0.6111                                     
REMARK   3      L33:   0.5266 L12:  -0.6018                                     
REMARK   3      L13:   0.1005 L23:  -0.5408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2806 S12:  -0.4191 S13:   0.2948                       
REMARK   3      S21:  -0.5544 S22:  -0.0697 S23:   0.0241                       
REMARK   3      S31:   0.3979 S32:   0.0179 S33:   0.0667                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6238   6.2001 -62.0388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4734 T22:   0.6004                                     
REMARK   3      T33:   0.4989 T12:   0.0393                                     
REMARK   3      T13:  -0.0689 T23:  -0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2556 L22:   0.1867                                     
REMARK   3      L33:   0.7611 L12:  -0.0508                                     
REMARK   3      L13:   0.3377 L23:   0.4231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1383 S12:   0.4436 S13:  -0.1002                       
REMARK   3      S21:  -0.1818 S22:  -0.0667 S23:  -0.0378                       
REMARK   3      S31:  -0.0404 S32:  -0.1534 S33:   0.0002                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:158)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4853   1.1728 -51.7948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3391 T22:   0.3753                                     
REMARK   3      T33:   0.3184 T12:  -0.0053                                     
REMARK   3      T13:  -0.0367 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1329 L22:   1.0579                                     
REMARK   3      L33:   1.4818 L12:   0.1189                                     
REMARK   3      L13:   0.2871 L23:   0.6744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1559 S12:   0.3308 S13:  -0.0746                       
REMARK   3      S21:  -0.1535 S22:  -0.2017 S23:   0.0103                       
REMARK   3      S31:   0.3093 S32:   0.0644 S33:  -0.0011                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 159:324)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9093   5.0111 -46.9468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3682 T22:   0.4489                                     
REMARK   3      T33:   0.4089 T12:   0.0412                                     
REMARK   3      T13:  -0.0543 T23:  -0.0507                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2388 L22:   0.5533                                     
REMARK   3      L33:   1.3784 L12:  -0.5546                                     
REMARK   3      L13:  -0.0287 L23:  -0.0753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0516 S12:   0.0756 S13:  -0.0552                       
REMARK   3      S21:  -0.0834 S22:   0.0137 S23:   0.0438                       
REMARK   3      S31:   0.0591 S32:   0.2793 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 325:355)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3549  -4.2751 -27.2483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7887 T22:   0.3995                                     
REMARK   3      T33:   0.5309 T12:  -0.0622                                     
REMARK   3      T13:  -0.0365 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1972 L22:   0.1623                                     
REMARK   3      L33:   0.1836 L12:   0.1925                                     
REMARK   3      L13:   0.0734 L23:   0.0759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:  -0.5281 S13:  -0.0799                       
REMARK   3      S21:   0.2614 S22:   0.0649 S23:  -0.0613                       
REMARK   3      S31:   0.5913 S32:  -0.1267 S33:   0.0051                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 356:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4208   3.7837 -27.5554              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4174 T22:   0.3689                                     
REMARK   3      T33:   0.3773 T12:  -0.0219                                     
REMARK   3      T13:  -0.0069 T23:  -0.0646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1416 L22:   0.6691                                     
REMARK   3      L33:   1.7568 L12:   0.2362                                     
REMARK   3      L13:   0.0797 L23:  -0.0336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1996 S12:  -0.0722 S13:   0.0727                       
REMARK   3      S21:   0.1523 S22:  -0.2018 S23:  -0.0239                       
REMARK   3      S31:   0.2806 S32:  -0.0546 S33:   0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:543)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5618  16.1061 -24.8741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6508 T22:   0.4764                                     
REMARK   3      T33:   0.4262 T12:  -0.0295                                     
REMARK   3      T13:  -0.0240 T23:  -0.0485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3633 L22:   0.2060                                     
REMARK   3      L33:   0.8020 L12:   0.3407                                     
REMARK   3      L13:  -0.1501 L23:   0.0993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1023 S12:  -0.2372 S13:   0.0670                       
REMARK   3      S21:  -0.0608 S22:  -0.0259 S23:   0.0998                       
REMARK   3      S31:  -0.0256 S32:   0.0309 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4B81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-53843.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JAN-11                          
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                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.039                              
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   : 49067                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.30                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.1                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.80                               
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   (%): 41                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (W/V)PEG750 MME, 0.1 M HEPES PH  
REMARK 280  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       38.97950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.96300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.93800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.96300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.97950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.93800            
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: 6640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A   238     O    HOH A  2050              2.19            
REMARK 500   SG   CYS B    69     CB   CYS B    96              1.74            
REMARK 500   OD1  ASP B    95     OH   TYR B    98              2.14            
REMARK 500   ND2  ASN B   350     C2   NAG B  1549              1.95            
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       -4.50     70.75                                   
REMARK 500    ALA A 167       72.90   -160.43                                   
REMARK 500    SER A 196       53.40   -140.42                                   
REMARK 500    SER A 203     -119.23     55.59                                   
REMARK 500    ASP A 306      -79.68   -143.94                                   
REMARK 500    ASP A 310     -158.90   -137.94                                   
REMARK 500    ASP A 323       58.98   -107.29                                   
REMARK 500    VAL A 407      -65.11   -123.39                                   
REMARK 500    ALA B  62       56.64   -111.44                                   
REMARK 500    ARG B  90     -165.63   -117.95                                   
REMARK 500    LEU B  97       73.85    -68.34                                   
REMARK 500    PHE B 123       19.16     57.34                                   
REMARK 500    ASP B 134      105.16    -56.70                                   
REMARK 500    PHE B 158       -1.14   -140.74                                   
REMARK 500    ALA B 167       64.47   -155.65                                   
REMARK 500    SER B 203     -115.06     53.81                                   
REMARK 500    ASP B 266      -71.56    -57.35                                   
REMARK 500    VAL B 303       98.52    -68.10                                   
REMARK 500    ASP B 306      -85.08   -113.41                                   
REMARK 500    ASP B 333       78.05   -108.98                                   
REMARK 500    ASN B 350     -128.95   -104.68                                   
REMARK 500    SER B 355     -155.57    -73.31                                   
REMARK 500    VAL B 407      -69.04   -123.80                                   
REMARK 500    PRO B 492       32.47    -76.25                                   
REMARK 500    LYS B 496      -28.13     65.30                                   
REMARK 500    PRO B 498     -150.35    -91.16                                   
REMARK 500    ALA B 506      -80.78    -69.26                                   
REMARK 500    ALA B 542     -114.15    -85.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER B 497        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN4 A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN4 B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1544 BOUND TO ASN A 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1546 BOUND TO ASN A 464                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B1549 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: 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: 4B83   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-3-METHOXY-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  4B81 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4B81 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 4B81 ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B81 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    P6G  B1546      19                                                       
HET    ZN4  A 600      19                                                       
HET    SO4  A1543       5                                                       
HET    NAG  A1544      14                                                       
HET    PEG  A1545       7                                                       
HET    NAG  A1546      14                                                       
HET    PEG  A1547       7                                                       
HET    PEG  A1548       7                                                       
HET    ZN4  B 600      19                                                       
HET    PEG  B1544       7                                                       
HET    SO4  B1545       5                                                       
HET    PEG  B1547       7                                                       
HET    PEG  B1548       7                                                       
HET    NAG  B1549      14                                                       
HET    PEG  B1550       7                                                       
HET    PEG  B1551       7                                                       
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3  P6G    C12 H26 O7                                                   
FORMUL   4  ZN4                                                                 
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   6  NAG    3(C8 H15 N O6)                                               
FORMUL   7  PEG    8(C4 H10 O3)                                                 
FORMUL   8  HOH   *180(H2 O)                                                    
HELIX    1   1 VAL A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  GLU A  142  1                                   8    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  ILE A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 SER A  203  SER A  215  1                                  13    
HELIX    9   9 LEU A  216  LEU A  221  5                                   6    
HELIX   10  10 SER A  240  GLY A  256  1                                  17    
HELIX   11  11 ASN A  265  ARG A  274  1                                  10    
HELIX   12  12 PRO A  277  ASP A  283  1                                   7    
HELIX   13  13 HIS A  284  LEU A  289  5                                   6    
HELIX   14  14 THR A  311  GLY A  319  1                                   9    
HELIX   15  15 GLY A  335  VAL A  340  1                                   6    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  GLN A  421  1                                  15    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 ASP A  460  ASN A  464  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  SER A  541  1                                  17    
HELIX   26  26 ASP B    5  GLN B    7  5                                   3    
HELIX   27  27 VAL B   42  ARG B   46  5                                   5    
HELIX   28  28 LEU B  130  ASP B  134  5                                   5    
HELIX   29  29 GLY B  135  GLY B  143  1                                   9    
HELIX   30  30 VAL B  153  LEU B  159  1                                   7    
HELIX   31  31 ASN B  170  ILE B  187  1                                  18    
HELIX   32  32 ALA B  188  PHE B  190  5                                   3    
HELIX   33  33 SER B  203  SER B  215  1                                  13    
HELIX   34  34 LEU B  216  LEU B  221  5                                   6    
HELIX   35  35 SER B  240  GLY B  256  1                                  17    
HELIX   36  36 ASP B  266  THR B  275  1                                  10    
HELIX   37  37 PRO B  277  ASP B  283  1                                   7    
HELIX   38  38 HIS B  284  LEU B  289  5                                   6    
HELIX   39  39 THR B  311  ASN B  317  1                                   7    
HELIX   40  40 GLY B  335  VAL B  340  5                                   6    
HELIX   41  41 ARG B  356  VAL B  367  1                                  12    
HELIX   42  42 SER B  371  THR B  383  1                                  13    
HELIX   43  43 ASP B  390  VAL B  407  1                                  18    
HELIX   44  44 VAL B  407  GLN B  421  1                                  15    
HELIX   45  45 PRO B  440  GLY B  444  5                                   5    
HELIX   46  46 GLU B  450  GLY B  456  1                                   7    
HELIX   47  47 LEU B  457  ASN B  464  5                                   8    
HELIX   48  48 THR B  466  GLY B  487  1                                  22    
HELIX   49  49 ARG B  525  ARG B  534  1                                  10    
HELIX   50  50 ARG B  534  ALA B  542  1                                   9    
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 VAL A 520  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.04  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
LINK         ND2 ASN A 350                 C1  NAG A1544     1555   1555  1.44  
LINK         ND2 ASN A 464                 C1  NAG A1546     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B1549     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0        -0.41                     
CISPEP   2 TYR B  105    PRO B  106          0         2.74                     
CISPEP   3 SER B  497    PRO B  498          0         6.94                     
SITE     1 AC1 10 HIS A 381  GLN A 527  PHE A 535  HOH A2080                    
SITE     2 AC1 10 HOH A2099  LEU B 380  HIS B 381  GLN B 527                    
SITE     3 AC1 10 PHE B 535  PEG B1547                                          
SITE     1 AC2 11 TRP A  86  GLY A 121  TYR A 124  GLU A 202                    
SITE     2 AC2 11 TRP A 286  TYR A 337  PHE A 338  TYR A 341                    
SITE     3 AC2 11 HIS A 447  HOH A2022  HOH A2033                               
SITE     1 AC3  5 LYS A  23  PRO A  25  ARG A 136  PHE A 137                    
SITE     2 AC3  5 ASP A 460                                                     
SITE     1 AC4  4 ASP A 304  GLY A 305  SER A 309  ASP A 310                    
SITE     1 AC5  3 HIS A 381  TYR A 382  ASP A 384                               
SITE     1 AC6  3 GLY A 234  PRO A 235  GLU A 313                               
SITE     1 AC7  8 TRP B  86  GLY B 121  TYR B 124  TYR B 337                    
SITE     2 AC7  8 PHE B 338  TYR B 341  HIS B 447  HOH B2047                    
SITE     1 AC8  4 LYS B 332  ASP B 333  ASP B 396  TRP B 442                    
SITE     1 AC9  4 LYS B  23  ARG B 136  PHE B 137  ASP B 460                    
SITE     1 BC1  4 GLN A 527  HIS B 381  ASP B 384  P6G B1546                    
SITE     1 BC2  1 ASP B 304                                                     
SITE     1 BC3  2 ARG B  11  ALA B 188                                          
SITE     1 BC4  2 GLY B 234  PRO B 235                                          
SITE     1 BC5  4 SER A 347  ASN A 350  HOH A2074  HOH A2100                    
SITE     1 BC6  2 SER A 462  ASN A 464                                          
SITE     1 BC7  4 SER B 347  ASN B 350  HOH B2054  HOH B2076                    
CRYST1   77.959  109.876  227.926  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      0.012827  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004387        0.00000                         
TER    4178      ALA A 542                                                      
TER    8338      THR B 543                                                      
MASTER      800    0   16   50   32    0   22    6 8681    2  180   86          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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