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LongText Report for: 4B84-pdb

Name Class
4B84-pdb
HEADER    HYDROLASE                               24-AUG-12   4B84              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-DIETHYLAMINO-  
TITLE    2 ETHYL)-3-TRIFLUOROMETHYL-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                                                      
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 4B84    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.082                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.60                          
REMARK   3   NUMBER OF REFLECTIONS             : 57214                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1775                          
REMARK   3   R VALUE            (WORKING SET) : 0.1764                          
REMARK   3   FREE R VALUE                     : 0.2355                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1133                            
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 29.0837 -  5.1914    0.85     6893   143  0.1666 0.2151        
REMARK   3     2  5.1914 -  4.1243    0.89     6938   136  0.1260 0.1513        
REMARK   3     3  4.1243 -  3.6041    0.90     6950   138  0.1476 0.2448        
REMARK   3     4  3.6041 -  3.2751    0.91     7024   134  0.1925 0.2694        
REMARK   3     5  3.2751 -  3.0406    0.92     7035   144  0.1981 0.2730        
REMARK   3     6  3.0406 -  2.8615    0.92     7077   141  0.2274 0.2698        
REMARK   3     7  2.8615 -  2.7183    0.93     7083   146  0.2605 0.3391        
REMARK   3     8  2.7183 -  2.6000    0.93     7081   151  0.2827 0.3233        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.11                                          
REMARK   3   K_SOL              : 0.307                                         
REMARK   3   B_SOL              : 54.455                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.38             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.10            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.4353                                              
REMARK   3    B22 (A**2) : 0.3214                                               
REMARK   3    B33 (A**2) : 0.1139                                               
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      :  0.009           8731                                  
REMARK   3   ANGLE     :  1.212          11922                                  
REMARK   3   CHIRALITY :  0.078           1274                                  
REMARK   3   PLANARITY :  0.005           1557                                  
REMARK   3   DIHEDRAL  : 16.202           3195                                  
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 1:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9961  12.9494  41.4493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3050 T22:   0.1662                                     
REMARK   3      T33:   0.1624 T12:  -0.0251                                     
REMARK   3      T13:  -0.0367 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7382 L22:   2.1587                                     
REMARK   3      L33:   4.5265 L12:  -0.5745                                     
REMARK   3      L13:  -1.7736 L23:  -0.6047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1756 S12:  -0.1443 S13:   0.1772                       
REMARK   3      S21:   0.5574 S22:   0.2205 S23:   0.0033                       
REMARK   3      S31:   0.0926 S32:  -0.0222 S33:  -0.0559                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 46:118)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.6108  16.6464  29.2931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2747 T22:   0.3205                                     
REMARK   3      T33:   0.2249 T12:   0.0445                                     
REMARK   3      T13:  -0.0239 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3114 L22:   1.7226                                     
REMARK   3      L33:   1.9496 L12:  -0.1147                                     
REMARK   3      L13:   0.3456 L23:  -0.0261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:  -0.0624 S13:   0.3870                       
REMARK   3      S21:   0.1912 S22:  -0.0874 S23:  -0.1067                       
REMARK   3      S31:  -0.2273 S32:   0.0334 S33:   0.0508                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 119:255)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1035   7.7230  20.8056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3272 T22:   0.1422                                     
REMARK   3      T33:   0.2638 T12:   0.0592                                     
REMARK   3      T13:   0.0143 T23:   0.0253                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0818 L22:   0.6266                                     
REMARK   3      L33:   2.3170 L12:   0.1156                                     
REMARK   3      L13:  -0.1527 L23:  -0.5740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:  -0.0496 S13:  -0.2539                       
REMARK   3      S21:   0.0371 S22:   0.0115 S23:  -0.0960                       
REMARK   3      S31:   0.3490 S32:   0.1347 S33:   0.0092                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 256:288)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6097  17.6363  15.2458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1660 T22:   0.4905                                     
REMARK   3      T33:   0.4136 T12:  -0.0116                                     
REMARK   3      T13:   0.0752 T23:   0.1167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4395 L22:   4.3939                                     
REMARK   3      L33:   4.2703 L12:   1.3923                                     
REMARK   3      L13:   0.8758 L23:  -2.4581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:   1.2233 S13:   0.6550                       
REMARK   3      S21:   0.5179 S22:  -0.5735 S23:  -0.9114                       
REMARK   3      S31:  -0.0111 S32:   0.1942 S33:   0.3559                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 289:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1527   3.6658   9.2119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4406 T22:   0.2163                                     
REMARK   3      T33:   0.2277 T12:   0.0062                                     
REMARK   3      T13:   0.0857 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3773 L22:   1.0806                                     
REMARK   3      L33:   2.1066 L12:   0.0559                                     
REMARK   3      L13:   0.4773 L23:   0.4151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:   0.3287 S13:  -0.6454                       
REMARK   3      S21:   0.1370 S22:   0.1986 S23:  -0.2752                       
REMARK   3      S31:   0.6216 S32:   0.1226 S33:  -0.0756                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 332:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1390  17.6242   6.3495              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1806 T22:   0.2707                                     
REMARK   3      T33:   0.2523 T12:  -0.0405                                     
REMARK   3      T13:  -0.0105 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2943 L22:   0.8977                                     
REMARK   3      L33:   3.9305 L12:  -0.0666                                     
REMARK   3      L13:   0.0928 L23:  -0.0492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0699 S12:   0.2047 S13:   0.0095                       
REMARK   3      S21:  -0.0476 S22:   0.0661 S23:   0.1448                       
REMARK   3      S31:   0.0561 S32:  -0.2628 S33:  -0.0066                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3339   1.5656  13.5677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3868 T22:   0.5574                                     
REMARK   3      T33:   0.5331 T12:  -0.2426                                     
REMARK   3      T13:   0.0394 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2650 L22:   9.0656                                     
REMARK   3      L33:   4.3818 L12:  -0.9087                                     
REMARK   3      L13:  -1.0690 L23:  -2.7241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1051 S12:  -0.0588 S13:  -1.0102                       
REMARK   3      S21:   0.5290 S22:  -0.1494 S23:   1.1246                       
REMARK   3      S31:   0.9417 S32:  -1.7414 S33:   0.1388                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:541)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2771   6.6048  -0.7575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3858 T22:   0.5122                                     
REMARK   3      T33:   0.2698 T12:  -0.0446                                     
REMARK   3      T13:  -0.1240 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1820 L22:   1.7345                                     
REMARK   3      L33:   4.9543 L12:  -0.3832                                     
REMARK   3      L13:  -3.5969 L23:   0.7055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4698 S12:  -0.1215 S13:   0.1982                       
REMARK   3      S21:  -0.4095 S22:   0.3769 S23:   0.2703                       
REMARK   3      S31:   0.6213 S32:   0.0357 S33:   0.1100                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3705   6.3352 -61.6727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3240 T22:   0.7106                                     
REMARK   3      T33:   0.2308 T12:   0.1138                                     
REMARK   3      T13:  -0.1202 T23:  -0.1586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9402 L22:   1.5835                                     
REMARK   3      L33:   1.8159 L12:   0.4573                                     
REMARK   3      L13:  -0.2875 L23:  -0.1676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:   0.2851 S13:   0.5466                       
REMARK   3      S21:  -0.4133 S22:  -0.0178 S23:   0.0152                       
REMARK   3      S31:  -0.2134 S32:  -0.6896 S33:   0.0540                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:111)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6682  -0.9027 -53.8257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3394 T22:   0.4608                                     
REMARK   3      T33:   0.3518 T12:   0.0597                                     
REMARK   3      T13:  -0.0813 T23:  -0.1566                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0493 L22:   2.4696                                     
REMARK   3      L33:   3.7175 L12:   0.2186                                     
REMARK   3      L13:   0.4001 L23:   0.1011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1232 S12:   0.2669 S13:  -0.1476                       
REMARK   3      S21:  -0.2788 S22:  -0.2846 S23:   0.2925                       
REMARK   3      S31:   0.5960 S32:  -0.1659 S33:   0.0718                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 112:170)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8216   4.4042 -48.8618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3162 T22:   0.4749                                     
REMARK   3      T33:   0.2223 T12:  -0.0426                                     
REMARK   3      T13:  -0.0302 T23:  -0.0674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1876 L22:   2.4082                                     
REMARK   3      L33:   2.4243 L12:  -0.6154                                     
REMARK   3      L13:   1.5589 L23:   0.8525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3168 S12:   0.6874 S13:  -0.2269                       
REMARK   3      S21:  -0.2347 S22:  -0.3025 S23:   0.1743                       
REMARK   3      S31:   0.1484 S32:   0.1750 S33:  -0.0004                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 171:255)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4418   9.6034 -47.3642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2103 T22:   0.2595                                     
REMARK   3      T33:   0.2263 T12:  -0.0423                                     
REMARK   3      T13:  -0.0000 T23:  -0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2631 L22:   2.3917                                     
REMARK   3      L33:   4.0551 L12:  -0.1952                                     
REMARK   3      L13:   0.3413 L23:   0.4579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0543 S12:   0.0850 S13:   0.0470                       
REMARK   3      S21:  -0.1597 S22:   0.0016 S23:  -0.1354                       
REMARK   3      S31:  -0.1477 S32:   0.2673 S33:  -0.0072                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 256:300)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7587  -9.2444 -46.8229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5657 T22:   0.4859                                     
REMARK   3      T33:   0.2727 T12:   0.2317                                     
REMARK   3      T13:  -0.1059 T23:  -0.1455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6626 L22:   3.4676                                     
REMARK   3      L33:   6.2155 L12:  -1.0494                                     
REMARK   3      L13:  -0.5172 L23:   2.1951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1446 S12:  -0.0674 S13:  -0.5093                       
REMARK   3      S21:   0.1626 S22:   0.1330 S23:   0.2146                       
REMARK   3      S31:   0.9742 S32:   1.2605 S33:   0.0154                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 301:340)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5620  11.6610 -36.9279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2746 T22:   0.4115                                     
REMARK   3      T33:   0.2938 T12:  -0.1066                                     
REMARK   3      T13:  -0.0501 T23:  -0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5826 L22:   2.2681                                     
REMARK   3      L33:   3.1923 L12:  -1.4689                                     
REMARK   3      L13:   0.5406 L23:   0.9746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1398 S12:   0.4169 S13:   0.4567                       
REMARK   3      S21:  -0.1454 S22:  -0.0715 S23:   0.0391                       
REMARK   3      S31:  -0.0697 S32:   0.2640 S33:  -0.0875                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 341:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8672   2.7017 -26.8263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3101 T22:   0.1800                                     
REMARK   3      T33:   0.2804 T12:  -0.1140                                     
REMARK   3      T13:   0.0207 T23:  -0.1202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3359 L22:   1.4370                                     
REMARK   3      L33:   4.0142 L12:   0.2141                                     
REMARK   3      L13:   0.8594 L23:   0.4900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2687 S12:  -0.1998 S13:  -0.3026                       
REMARK   3      S21:   0.3545 S22:  -0.1751 S23:   0.3290                       
REMARK   3      S31:   0.6950 S32:  -0.2693 S33:  -0.0981                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3554  22.4320 -28.8043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3607 T22:   0.5615                                     
REMARK   3      T33:   0.3660 T12:   0.0654                                     
REMARK   3      T13:   0.0031 T23:  -0.1205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3150 L22:   4.7723                                     
REMARK   3      L33:   8.2754 L12:  -0.4506                                     
REMARK   3      L13:   2.2703 L23:  -3.0144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2851 S12:  -0.7358 S13:   1.0677                       
REMARK   3      S21:   0.0525 S22:   0.1938 S23:   0.3031                       
REMARK   3      S31:  -0.0868 S32:  -1.5625 S33:   0.0266                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2848  12.0875 -21.5280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4630 T22:   0.7140                                     
REMARK   3      T33:   0.2607 T12:  -0.0755                                     
REMARK   3      T13:   0.0209 T23:  -0.1378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2539 L22:   0.9255                                     
REMARK   3      L33:   3.2806 L12:  -0.1328                                     
REMARK   3      L13:   3.7298 L23:  -1.0085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0517 S12:  -0.2798 S13:   0.1665                       
REMARK   3      S21:   0.0252 S22:  -0.1883 S23:  -0.0648                       
REMARK   3      S31:  -0.0531 S32:   0.2338 S33:   0.1575                       
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 4B84 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-53846.                                       
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   : 57324                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.75                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 5.0                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.48                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.50                               
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   (%): 70.7                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.2                      
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       39.57900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.62000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.17800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.62000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.57900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.17800            
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: 6170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.8 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     ALA A   263                                                      
REMARK 465     ALA A   542                                                      
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     ALA B   542                                                      
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   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO A 258    CG   CD                                             
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 494    CG   OD1  OD2                                       
REMARK 470     SER A 495    OG                                                  
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     SER A 541    OG                                                  
REMARK 470     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     GLU B 268    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 494    CG   OD1  OD2                                       
REMARK 470     SER B 495    OG                                                  
REMARK 470     LYS B 496    CG   CD   CE   NZ                                   
REMARK 470     SER B 497    OG                                                  
REMARK 470     SER B 541    OG                                                  
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   O    ASN B   482     OG1  THR B   486              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 368   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
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    PRO A   6        0.59    -66.23                                   
REMARK 500    PHE A  47      -12.51     79.56                                   
REMARK 500    ALA A  62       50.08   -111.15                                   
REMARK 500    PRO A 104      163.94    -44.59                                   
REMARK 500    ALA A 167       71.35   -150.56                                   
REMARK 500    ASN A 170       11.52     60.00                                   
REMARK 500    SER A 203     -112.61     34.94                                   
REMARK 500    ASP A 306      -84.92   -146.63                                   
REMARK 500    ASP A 310     -166.73   -128.82                                   
REMARK 500    VAL A 407      -65.25   -122.89                                   
REMARK 500    ASP A 494       41.93    -92.31                                   
REMARK 500    ARG A 525       50.88     27.44                                   
REMARK 500    PRO B  40      107.60    -45.29                                   
REMARK 500    PHE B  47       -8.99     70.45                                   
REMARK 500    THR B  75       23.49   -144.52                                   
REMARK 500    ALA B 167       65.57   -168.02                                   
REMARK 500    SER B 203     -122.97     50.41                                   
REMARK 500    ALA B 264     -109.15   -118.52                                   
REMARK 500    PRO B 301      152.33    -47.82                                   
REMARK 500    ASP B 306      -79.09   -126.03                                   
REMARK 500    TYR B 341       46.73   -101.32                                   
REMARK 500    GLU B 351        6.29    -65.96                                   
REMARK 500    VAL B 367       62.83   -150.41                                   
REMARK 500    TRP B 385        2.27    -62.86                                   
REMARK 500    VAL B 407      -63.27   -121.95                                   
REMARK 500    SER B 495      166.92     88.28                                   
REMARK 500    SER B 497     -153.93   -109.59                                   
REMARK 500    PRO B 498        4.18    -52.70                                   
REMARK 500    GLN B 499      134.17     76.76                                   
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     P3G A 1542                                                       
REMARK 610     P3G A 1543                                                       
REMARK 610     P3G A 1545                                                       
REMARK 610     P3G B 1542                                                       
REMARK 610     P6G B 1546                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1542                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K B1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A 701 BOUND TO ASN A 464                                       
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: 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: 4B85   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-                
REMARK 900  CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE               
DBREF  4B84 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4B84 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 4B84 ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 ALA A  263  UNP  P21836    GLY   294 CONFLICT                       
SEQADV 4B84 ALA A  264  UNP  P21836    GLY   295 CONFLICT                       
SEQADV 4B84 ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 PRO B  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B84 ALA B  263  UNP  P21836    GLY   294 CONFLICT                       
SEQADV 4B84 ALA B  264  UNP  P21836    GLY   295 CONFLICT                       
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 ALA ALA 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 ALA ALA 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    NAG  A 701      14                                                       
HET    P3G  B1542       7                                                       
HET    P3G  A1542       9                                                       
HET    P3G  A1543       9                                                       
HET    Z5K  B1543      21                                                       
HET    SO4  B1544       5                                                       
HET    SO4  A1544       5                                                       
HET    P3G  A1545       6                                                       
HET    Z5K  A1546      21                                                       
HET    Z5K  B1545      21                                                       
HET    P6G  B1546      17                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     P3G 3,6,9,12,15-PENTAOXAHEPTADECANE                                  
HETNAM     Z5K N-[2-(DIETHYLAMINO)ETHYL]-3-(TRIFLUOROMETHYL)                    
HETNAM   2 Z5K  BENZENESULFONAMIDE                                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   6  Z5K    3(C13 H19 F3 N2 O2 S)                                        
FORMUL   7  SO4    2(O4 S 2-)                                                   
FORMUL   8  P6G    C12 H26 O7                                                   
FORMUL   9  HOH   *384(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  GLY A  143  1                                   9    
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  ARG A  219  5                                   4    
HELIX   10  10 SER A  240  VAL A  255  1                                  16    
HELIX   11  11 ALA A  264  ARG A  274  1                                  11    
HELIX   12  12 PRO A  277  GLU A  285  1                                   9    
HELIX   13  13 TRP A  286  LEU A  289  5                                   4    
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  PHE A  535  1                                  11    
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 PHE B   80  MET B   85  1                                   6    
HELIX   29  29 LEU B  130  ASP B  134  5                                   5    
HELIX   30  30 GLY B  135  GLU B  142  1                                   8    
HELIX   31  31 VAL B  153  LEU B  159  1                                   7    
HELIX   32  32 ASN B  170  ILE B  187  1                                  18    
HELIX   33  33 ALA B  188  PHE B  190  5                                   3    
HELIX   34  34 SER B  203  LEU B  214  1                                  12    
HELIX   35  35 SER B  215  ARG B  219  5                                   5    
HELIX   36  36 ALA B  241  GLY B  256  1                                  16    
HELIX   37  37 ASN B  265  THR B  275  1                                  11    
HELIX   38  38 PRO B  277  TRP B  286  1                                  10    
HELIX   39  39 HIS B  287  LEU B  289  5                                   3    
HELIX   40  40 THR B  311  GLY B  319  1                                   9    
HELIX   41  41 GLY B  335  VAL B  340  1                                   6    
HELIX   42  42 SER B  355  VAL B  367  1                                  13    
HELIX   43  43 SER B  371  THR B  383  1                                  13    
HELIX   44  44 ASP B  390  VAL B  407  1                                  18    
HELIX   45  45 VAL B  407  GLN B  421  1                                  15    
HELIX   46  46 PRO B  440  GLY B  444  5                                   5    
HELIX   47  47 GLU B  450  PHE B  455  1                                   6    
HELIX   48  48 GLY B  456  ASP B  460  5                                   5    
HELIX   49  49 ASP B  460  ASN B  464  5                                   5    
HELIX   50  50 THR B  466  GLY B  487  1                                  22    
HELIX   51  51 ARG B  525  ARG B  534  1                                  10    
HELIX   52  52 PHE B  535  SER B  541  1                                   7    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
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  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.07  
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  2.05  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         ND2 ASN A 464                 C1  NAG A 701     1555   1555  1.46  
CISPEP   1 TYR A  105    PRO A  106          0         3.71                     
CISPEP   2 TYR B  105    PRO B  106          0         3.60                     
CISPEP   3 ASP B  494    SER B  495          0        11.56                     
CISPEP   4 LYS B  496    SER B  497          0         4.67                     
SITE     1 AC1  4 GLN A 527  HOH A2209  HIS B 381  TYR B 382                    
SITE     1 AC2  3 HIS A 381  THR A 383  GLN B 527                               
SITE     1 AC3 13 TRP B  86  GLY B 121  GLY B 122  TYR B 124                    
SITE     2 AC3 13 TYR B 133  GLU B 202  TRP B 286  TYR B 337                    
SITE     3 AC3 13 PHE B 338  TYR B 341  HIS B 447  HOH B2061                    
SITE     4 AC3 13 HOH B2122                                                     
SITE     1 AC4  5 LYS B  23  ALA B  24  PRO B  25  ASP B 460                    
SITE     2 AC4  5 HOH B2173                                                     
SITE     1 AC5  6 LYS A  23  ALA A  24  PRO A  25  ARG A 136                    
SITE     2 AC5  6 PHE A 137  ASP A 460                                          
SITE     1 AC6  2 GLY A 305  SER A 309                                          
SITE     1 AC7 11 TRP A  86  GLY A 120  GLY A 121  TYR A 124                    
SITE     2 AC7 11 GLU A 202  SER A 203  TRP A 286  PHE A 297                    
SITE     3 AC7 11 TYR A 337  TYR A 341  HIS A 447                               
SITE     1 AC8  9 GLY B  79  GLU B  81  GLU B  84  MET B  85                    
SITE     2 AC8  9 ASP B 131  LEU B 457  LEU B 463  HOH B2043                    
SITE     3 AC8  9 HOH B2049                                                     
SITE     1 AC9  9 LEU A 380  HIS A 381  GLN A 527  PHE A 531                    
SITE     2 AC9  9 HOH A2164  ALA B 377  LEU B 380  HIS B 381                    
SITE     3 AC9  9 PHE B 535                                                     
SITE     1 BC1  4 SER A 462  ASN A 464  HOH A2207  HOH A2208                    
CRYST1   79.158  112.356  227.240  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      0.012633  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004401        0.00000                         
TER    4194      SER A 541                                                      
TER    8346      SER B 541                                                      
MASTER      811    0   11   52   34    0   21    6 8863    2  148   86          
END                                                                             

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