Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4ARB-pdb

Name Class
4ARB-pdb
HEADER    HYDROLASE                               23-APR-12   4ARB              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-C5685 AT 2.25 A 
TITLE    2 RESOLUTION.                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: HEK293F                                   
KEYWDS    HYDROLASE, ENATIOMERS, INHIBITOR, CHEMICAL LEAD                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNGSTAFSHEDE,F.EKSTROM, 
AUTHOR   2 A.LINUSSON                                                           
REVDAT   1   28-NOV-12 4ARB    0                                                
JRNL        AUTH   L.BERG,M.S.NIEMIEC,W.QIAN,C.D.ANDERSSON,P.WITTUNG-STAFSHEDE, 
JRNL        AUTH 2 F.EKSTROM,A.LINUSSON                                         
JRNL        TITL   SIMILAR BUT DIFFERENT: THERMODYNAMIC AND STRUCTURAL          
JRNL        TITL 2 CHARACTERIZATION OF A PAIR OF ENANTIOMERS BINDING TO         
JRNL        TITL 3 ACETYLCHOLINESTERASE.                                        
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.                    2012              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   23161758                                                     
JRNL        DOI    10.1002/ANIE.201205113                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.BERG,C.D.ANDERSSON,E.ARTURSSON,A.HORNBERG,A.TUNEMALM,      
REMARK   1  AUTH 2 A.LINUSSON,F.EKSTROM                                         
REMARK   1  TITL   TARGETING ACETYLCHOLINESTERASE: IDENTIFICATION OF CHEMICAL   
REMARK   1  TITL 2 LEADS BY HIGH THROUGHPUT SCREENING, STRUCTURE DETERMINATION  
REMARK   1  TITL 3 AND MOLECULAR MODELING.                                      
REMARK   1  REF    PLOS ONE                      V.   6 26039 2011              
REMARK   1  REFN                   ISSN 1932-6203                               
REMARK   1  PMID   22140425                                                     
REMARK   1  DOI    10.1371/JOURNAL.PONE.0026039                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.250                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.806                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.89                          
REMARK   3   NUMBER OF REFLECTIONS             : 95904                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1722                          
REMARK   3   R VALUE            (WORKING SET) : 0.1715                          
REMARK   3   FREE R VALUE                     : 0.2091                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1893                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.8081 -  5.4117    0.99     7053   137  0.1742 0.2016        
REMARK   3     2  5.4117 -  4.3000    1.00     6819   133  0.1288 0.1495        
REMARK   3     3  4.3000 -  3.7578    1.00     6779   131  0.1354 0.1770        
REMARK   3     4  3.7578 -  3.4148    1.00     6713   148  0.1627 0.1970        
REMARK   3     5  3.4148 -  3.1704    1.00     6729   115  0.1804 0.2124        
REMARK   3     6  3.1704 -  2.9837    1.00     6685   153  0.1752 0.2106        
REMARK   3     7  2.9837 -  2.8344    1.00     6704   133  0.1808 0.2343        
REMARK   3     8  2.8344 -  2.7111    1.00     6650   138  0.2025 0.2370        
REMARK   3     9  2.7111 -  2.6068    1.00     6664   150  0.2006 0.2734        
REMARK   3    10  2.6068 -  2.5169    1.00     6676   138  0.2015 0.2633        
REMARK   3    11  2.5169 -  2.4382    1.00     6652   119  0.2191 0.2571        
REMARK   3    12  2.4382 -  2.3686    1.00     6642   133  0.2287 0.2770        
REMARK   3    13  2.3686 -  2.3063    1.00     6643   134  0.2439 0.2971        
REMARK   3    14  2.3063 -  2.2500    1.00     6602   131  0.2599 0.3242        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.342                                         
REMARK   3   B_SOL              : 70.323                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.30             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.24            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.3384                                               
REMARK   3    B22 (A**2) : 2.5156                                               
REMARK   3    B33 (A**2) : -3.8539                                              
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      :  0.008           8776                                  
REMARK   3   ANGLE     :  1.090          11969                                  
REMARK   3   CHIRALITY :  0.078           1284                                  
REMARK   3   PLANARITY :  0.005           1571                                  
REMARK   3   DIHEDRAL  : 16.664           3166                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:228)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2088  11.2991  28.9999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2646 T22:   0.2397                                     
REMARK   3      T33:   0.2736 T12:   0.0076                                     
REMARK   3      T13:  -0.0112 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2391 L22:   0.1750                                     
REMARK   3      L33:   1.0047 L12:   0.0017                                     
REMARK   3      L13:  -0.0694 L23:  -0.0483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:  -0.0881 S13:   0.0254                       
REMARK   3      S21:   0.0719 S22:   0.0221 S23:  -0.0443                       
REMARK   3      S31:   0.0516 S32:   0.0421 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 229:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5221   9.9315  10.2869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2642 T22:   0.2348                                     
REMARK   3      T33:   0.3165 T12:   0.0414                                     
REMARK   3      T13:   0.0194 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0184 L22:   0.0643                                     
REMARK   3      L33:   1.2735 L12:   0.2585                                     
REMARK   3      L13:  -0.1056 L23:  -0.4797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0891 S12:   0.2130 S13:  -0.0890                       
REMARK   3      S21:  -0.0831 S22:  -0.0196 S23:  -0.0817                       
REMARK   3      S31:   0.2389 S32:   0.2579 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 332:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7065  17.4241   6.4363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2307 T22:   0.2595                                     
REMARK   3      T33:   0.2875 T12:  -0.0206                                     
REMARK   3      T13:  -0.0072 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4685 L22:   0.3454                                     
REMARK   3      L33:   1.8033 L12:  -0.0506                                     
REMARK   3      L13:   0.2512 L23:  -0.2481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0321 S12:   0.0905 S13:   0.0152                       
REMARK   3      S21:  -0.0809 S22:   0.0074 S23:   0.0865                       
REMARK   3      S31:   0.0158 S32:  -0.2667 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9359   1.3383  13.5125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3952 T22:   0.5363                                     
REMARK   3      T33:   0.4444 T12:  -0.1935                                     
REMARK   3      T13:  -0.0118 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1025 L22:   0.1980                                     
REMARK   3      L33:   0.1138 L12:  -0.1197                                     
REMARK   3      L13:   0.1317 L23:  -0.0917                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0452 S12:   0.1980 S13:  -0.1113                       
REMARK   3      S21:  -0.1038 S22:   0.0938 S23:   0.5021                       
REMARK   3      S31:   0.6675 S32:  -0.8945 S33:   0.0004                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2854   6.3249  -1.0277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3523 T22:   0.4280                                     
REMARK   3      T33:   0.3840 T12:  -0.0561                                     
REMARK   3      T13:  -0.0580 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2836 L22:  -0.0757                                     
REMARK   3      L33:   0.5231 L12:  -0.1560                                     
REMARK   3      L13:   0.4453 L23:  -0.1300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1991 S12:  -0.0153 S13:   0.0005                       
REMARK   3      S21:  -0.2693 S22:  -0.1343 S23:   0.2499                       
REMARK   3      S31:  -0.0638 S32:   0.0471 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6209   6.1949 -61.7900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3031 T22:   0.4555                                     
REMARK   3      T33:   0.3374 T12:   0.0569                                     
REMARK   3      T13:  -0.0669 T23:  -0.0760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2470 L22:   0.4960                                     
REMARK   3      L33:   0.7685 L12:  -0.0083                                     
REMARK   3      L13:   0.3197 L23:   0.1435                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:   0.2933 S13:  -0.0210                       
REMARK   3      S21:  -0.2022 S22:  -0.0718 S23:  -0.0605                       
REMARK   3      S31:  -0.0268 S32:  -0.2764 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:86)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2144  -4.2019 -52.9520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4212 T22:   0.4162                                     
REMARK   3      T33:   0.3377 T12:  -0.0010                                     
REMARK   3      T13:  -0.0408 T23:  -0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1448 L22:   0.4353                                     
REMARK   3      L33:   0.4277 L12:   0.0640                                     
REMARK   3      L13:   0.1585 L23:   0.1880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:   0.2136 S13:  -0.1023                       
REMARK   3      S21:  -0.0542 S22:  -0.0798 S23:   0.0205                       
REMARK   3      S31:   0.2582 S32:   0.0331 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 87:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9177   4.0898 -50.9208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2692 T22:   0.3304                                     
REMARK   3      T33:   0.2832 T12:   0.0047                                     
REMARK   3      T13:  -0.0364 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1928 L22:   0.3626                                     
REMARK   3      L33:   1.4111 L12:   0.2255                                     
REMARK   3      L13:   0.4407 L23:   0.2671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0477 S12:   0.1461 S13:  -0.1781                       
REMARK   3      S21:  -0.0732 S22:  -0.0485 S23:   0.0562                       
REMARK   3      S31:   0.1067 S32:  -0.1163 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 171:237)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1949  13.3797 -48.2655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3195 T22:   0.3344                                     
REMARK   3      T33:   0.3006 T12:   0.0167                                     
REMARK   3      T13:  -0.0162 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2609 L22:   0.2579                                     
REMARK   3      L33:   0.4760 L12:   0.0051                                     
REMARK   3      L13:  -0.3360 L23:   0.2790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0297 S12:   0.1080 S13:  -0.0077                       
REMARK   3      S21:  -0.0268 S22:   0.0297 S23:   0.0254                       
REMARK   3      S31:  -0.1421 S32:   0.0455 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 238:300)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0118  -8.3606 -45.9560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4050 T22:   0.4446                                     
REMARK   3      T33:   0.3683 T12:   0.1291                                     
REMARK   3      T13:  -0.0919 T23:  -0.0748                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2473 L22:   0.4135                                     
REMARK   3      L33:   0.2147 L12:  -0.2345                                     
REMARK   3      L13:   0.2420 L23:  -0.1041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0813 S12:   0.1012 S13:  -0.0585                       
REMARK   3      S21:   0.2057 S22:   0.0516 S23:  -0.1090                       
REMARK   3      S31:   0.3595 S32:   0.6006 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 301:341)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8863  10.7038 -36.7752              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2984 T22:   0.2801                                     
REMARK   3      T33:   0.3343 T12:  -0.0390                                     
REMARK   3      T13:  -0.0315 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6304 L22:   0.5318                                     
REMARK   3      L33:   1.1269 L12:  -0.3974                                     
REMARK   3      L13:   0.1829 L23:   0.6252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0742 S12:   0.0264 S13:   0.0674                       
REMARK   3      S21:   0.0471 S22:   0.0090 S23:  -0.0498                       
REMARK   3      S31:   0.0264 S32:   0.1718 S33:  -0.0001                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 342:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6017   2.4875 -26.6503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3423 T22:   0.2729                                     
REMARK   3      T33:   0.3089 T12:  -0.0500                                     
REMARK   3      T13:  -0.0111 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4761 L22:   0.2269                                     
REMARK   3      L33:   1.5145 L12:   0.0122                                     
REMARK   3      L13:   0.2987 L23:   0.4391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1166 S12:  -0.0545 S13:  -0.0072                       
REMARK   3      S21:   0.1840 S22:  -0.1111 S23:   0.0591                       
REMARK   3      S31:   0.2369 S32:  -0.1260 S33:  -0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4034  22.5491 -28.6421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3392 T22:   0.2581                                     
REMARK   3      T33:   0.3472 T12:   0.0112                                     
REMARK   3      T13:   0.0035 T23:  -0.0540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1251 L22:   0.2306                                     
REMARK   3      L33:   0.3656 L12:  -0.0622                                     
REMARK   3      L13:  -0.2261 L23:   0.1440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0779 S12:  -0.1933 S13:   0.5080                       
REMARK   3      S21:   0.1458 S22:  -0.0633 S23:   0.3032                       
REMARK   3      S31:  -0.2831 S32:  -0.1344 S33:  -0.0002                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:543)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1696  11.3791 -21.5857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3579 T22:   0.4036                                     
REMARK   3      T33:   0.2966 T12:   0.0065                                     
REMARK   3      T13:  -0.0014 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0624 L22:   0.0994                                     
REMARK   3      L33:   0.5935 L12:   0.0085                                     
REMARK   3      L13:   0.2249 L23:  -0.0175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1209 S12:  -0.0032 S13:  -0.0857                       
REMARK   3      S21:   0.0694 S22:  -0.1010 S23:   0.1504                       
REMARK   3      S31:  -0.0121 S32:   0.1605 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 4ARB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52169.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
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                  : RH-COATED SI MIRROR, BENT          
REMARK 200                                   FOR VERTICAL COLLIMATION           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96077                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.25                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.10                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.7                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.48                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 30 % (V/V)                  
REMARK 280  POLYETHELENEGLYCOLEMONOMETHYLETHER                                  
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       39.46300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.53550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.89050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.53550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.46300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.89050            
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: 4220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  23    CG   CD   CE   NZ                                   
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 322    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 323    CG   OD1  OD2                                       
REMARK 470     ASN A 464    ND2                                                 
REMARK 470     ASP A 491    CG   OD1  OD2                                       
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     LYS B 478    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   ND1  ASN A   464     O    A2G A  1547              1.80            
REMARK 500   O    HOH A  2042     O    HOH A  2101              2.20            
REMARK 500   O    HOH A  2202     O    HOH A  2392              2.19            
REMARK 500   O    HOH A  2238     O    HOH A  2492              2.19            
REMARK 500   O    HOH B  2142     O    HOH B  2287              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -5.86     74.63                                   
REMARK 500    PHE A 158       -7.58   -140.61                                   
REMARK 500    ALA A 167       68.72   -156.94                                   
REMARK 500    SER A 203     -124.47     53.42                                   
REMARK 500    ASP A 306      -85.67   -127.94                                   
REMARK 500    HIS A 387       59.73   -140.60                                   
REMARK 500    VAL A 407      -60.79   -130.27                                   
REMARK 500    ARG A 493       43.10   -109.99                                   
REMARK 500    ASP A 494      -62.88   -132.65                                   
REMARK 500    SER A 495      -45.86     57.84                                   
REMARK 500    PHE B  47       -5.17     73.88                                   
REMARK 500    ALA B  62       50.28   -116.59                                   
REMARK 500    ALA B 167       70.66   -150.35                                   
REMARK 500    ASN B 170       16.37     57.56                                   
REMARK 500    SER B 203     -125.12     52.23                                   
REMARK 500    ASP B 306      -84.69   -117.65                                   
REMARK 500    VAL B 407      -58.18   -130.18                                   
REMARK 500    SER B 541       41.72    -75.54                                   
REMARK 500    ALA B 542      -11.70   -170.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-                        
REMARK 600  2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE (568):                      
REMARK 600  CORRESPONDING TO LIGAND C57 IN THE RACEMIC STRUCTURE 4A23           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C57 A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C57 B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1545 BOUND TO ASN A 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1547 BOUND TO ASN A 464                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B1547 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.                                          
DBREF  4ARB A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4ARB B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 4ARB ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4ARB 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                                                      
MODRES 4ARB ASN A  350  ASN  GLYCOSYLATION SITE                                 
MODRES 4ARB ASN B  350  ASN  GLYCOSYLATION SITE                                 
HET    C57  A1543      25                                                       
HET    PEG  A1544       7                                                       
HET    NAG  A1545      14                                                       
HET    PEG  A1546       7                                                       
HET    NAG  A1547      14                                                       
HET    PEG  A1548       7                                                       
HET    PEG  A1549       7                                                       
HET    C57  B1544      25                                                       
HET    P6G  B1545      19                                                       
HET    PEG  B1546       7                                                       
HET    NAG  B1547      14                                                       
HET    PEG  B1548       7                                                       
HETNAM     C57 4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-                    
HETNAM   2 C57  2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3  C57    2(C17 H26 N4 O4)                                             
FORMUL   4  PEG    6(C4 H10 O3)                                                 
FORMUL   5  NAG    3(C8 H15 N O6)                                               
FORMUL   6  P6G    C12 H26 O7                                                   
FORMUL   7  HOH   *989(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SER A  203  SER A  215  1                                  13    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  VAL A  255  1                                  16    
HELIX   12  12 ASN A  265  THR A  275  1                                  11    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  SER A  541  1                                   8    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 SER B  203  LEU B  214  1                                  12    
HELIX   37  37 SER B  215  SER B  220  1                                   6    
HELIX   38  38 SER B  240  VAL B  255  1                                  16    
HELIX   39  39 ASN B  265  ARG B  276  1                                  12    
HELIX   40  40 PRO B  277  TRP B  286  1                                  10    
HELIX   41  41 HIS B  287  LEU B  289  5                                   3    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 GLY B  335  VAL B  340  1                                   6    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  PHE B  455  1                                   6    
HELIX   50  50 GLY B  456  ASP B  460  5                                   5    
HELIX   51  51 ASP B  460  ASN B  464  5                                   5    
HELIX   52  52 THR B  466  GLY B  487  1                                  22    
HELIX   53  53 ARG B  525  ARG B  534  1                                  10    
HELIX   54  54 ARG B  534  SER B  541  1                                   8    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.05  
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  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05  
LINK         ND2 ASN A 350                 C1  NAG A1545     1555   1555  1.48  
LINK         ND2 ASN A 464                 C1  NAG A1547     1555   1555  1.51  
LINK         ND2 ASN B 350                 C1  NAG B1547     1555   1555  1.41  
CISPEP   1 TYR A  105    PRO A  106          0        -1.33                     
CISPEP   2 TYR B  105    PRO B  106          0         0.77                     
CISPEP   3 SER B  497    PRO B  498          0         5.67                     
SITE     1 AC1 14 TYR A  72  ASP A  74  TRP A  86  TYR A 124                    
SITE     2 AC1 14 TRP A 286  SER A 293  ILE A 294  PHE A 295                    
SITE     3 AC1 14 ARG A 296  TYR A 337  PHE A 338  TYR A 341                    
SITE     4 AC1 14 HOH A2367  HOH A2368                                          
SITE     1 AC2  3 ASP A 304  GLY A 305  SER A 309                               
SITE     1 AC3  3 HIS A 381  HIS A 393  HOH A2431                               
SITE     1 AC4  3 GLN A 413  ARG A 417  HOH A2535                               
SITE     1 AC5 11 TYR B  72  ASP B  74  TYR B 124  TRP B 286                    
SITE     2 AC5 11 SER B 293  ILE B 294  PHE B 295  ARG B 296                    
SITE     3 AC5 11 TYR B 337  PHE B 338  TYR B 341                               
SITE     1 AC6 13 ALA A 377  LEU A 380  HIS A 381  GLN A 527                    
SITE     2 AC6 13 PHE A 531  PHE A 535  HOH A2430  LEU B 380                    
SITE     3 AC6 13 HIS B 381  THR B 528  PHE B 531  HOH B2341                    
SITE     4 AC6 13 HOH B2447                                                     
SITE     1 AC7  3 HIS B 381  ASP B 384  HOH B2449                               
SITE     1 AC8  3 GLY B 305  SER B 309  HOH B2451                               
SITE     1 AC9  7 SER A 347  ASN A 350  HOH A2398  HOH A2399                    
SITE     2 AC9  7 HOH A2532  HOH A2533  HOH A2534                               
SITE     1 BC1  1 ASN A 464                                                     
SITE     1 BC2  6 SER B 347  ASN B 350  LEU B 353  HOH B2322                    
SITE     2 BC2  6 HOH B2323  HOH B2450                                          
CRYST1   78.926  111.781  227.071  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      0.012670  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004404        0.00000                         
TER    4196      ALA A 542                                                      
TER    8367      THR B 543                                                      
MASTER      738    0   12   54   32    0   21    6 9507    2  168   86          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer