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LongText Report for: 5fpp-pdb

Name Class
5fpp-pdb
HEADER    HYDROLASE                               02-DEC-15   5FPP              
TITLE     STRUCTURE OF A PRE-REACTION TERNARY COMPLEX BETWEEN SARIN-            
TITLE    2 ACETYLCHOLINESTERASE AND HI-6                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 32-574;                     
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: SARIN PHOSPHONYLATION PRODUCT COVALENTLY ATTACHED TO  
COMPND   9  SER203                                                              
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: HEK293F                                 
KEYWDS    HYDROLASE, SARIN, HI-6, QM, DENSITY FUNCTIONAL THEORY CALCULATIONS,   
KEYWDS   2 MICHAELIS COMPLEX.                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ALLGARDSSON,L.BERG,C.AKFUR,A.HORNBERG,F.WOREK,A.LINUSSON,F.EKSTROM  
REVDAT   1   11-MAY-16 5FPP    0                                                
JRNL        AUTH   A.ALLGARDSSON,L.BERG,C.AKFUR,A.HORNBERG,F.WOREK,A.LINUSSON,  
JRNL        AUTH 2 F.J.EKSTROM                                                  
JRNL        TITL   STRUCTURE OF A PREREACTION COMPLEX BETWEEN THE NERVE AGENT   
JRNL        TITL 2 SARIN, ITS BIOLOGICAL TARGET ACETYLCHOLINESTERASE, AND THE   
JRNL        TITL 3 ANTIDOTE HI-6.                                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   27140636                                                     
JRNL        DOI    10.1073/PNAS.1523362113                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.400                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.950                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.04                          
REMARK   3   NUMBER OF REFLECTIONS             : 77689                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1763                          
REMARK   3   R VALUE            (WORKING SET) : 0.1756                          
REMARK   3   FREE R VALUE                     : 0.2133                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1541                            
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 28.9520 -  5.3275    0.96     7079   142  0.1621 0.1814        
REMARK   3     2  5.3275 -  4.2328    0.97     6996   141  0.1311 0.1653        
REMARK   3     3  4.2328 -  3.6990    0.98     6926   134  0.1477 0.1829        
REMARK   3     4  3.6990 -  3.3613    0.99     6969   139  0.1741 0.2145        
REMARK   3     5  3.3613 -  3.1207    0.99     6943   132  0.1958 0.2425        
REMARK   3     6  3.1207 -  2.9369    0.99     6929   154  0.2129 0.2510        
REMARK   3     7  2.9369 -  2.7899    0.99     6900   140  0.2182 0.2879        
REMARK   3     8  2.7899 -  2.6686    0.99     6923   141  0.2199 0.2718        
REMARK   3     9  2.6686 -  2.5659    0.99     6878   151  0.2243 0.2777        
REMARK   3    10  2.5659 -  2.4774    0.98     6812   144  0.2392 0.2723        
REMARK   3    11  2.4774 -  2.4000    0.97     6793   123  0.2732 0.3321        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.32             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.00            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.86                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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           8867                                  
REMARK   3   ANGLE     :  1.103          12100                                  
REMARK   3   CHIRALITY :  0.076           1286                                  
REMARK   3   PLANARITY :  0.005           1597                                  
REMARK   3   DIHEDRAL  : 15.961           3222                                  
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):  30.8717  11.2359  29.1061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2639 T22:   0.2173                                     
REMARK   3      T33:   0.2230 T12:   0.0042                                     
REMARK   3      T13:  -0.0257 T23:   0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3884 L22:   1.4015                                     
REMARK   3      L33:   3.0163 L12:   0.0965                                     
REMARK   3      L13:  -0.4026 L23:  -0.2151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0621 S12:  -0.1013 S13:   0.0581                       
REMARK   3      S21:   0.2088 S22:   0.0545 S23:   0.0101                       
REMARK   3      S31:   0.0917 S32:  -0.0321 S33:   0.0138                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 229:331)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3703   9.4725  10.3067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3307 T22:   0.2486                                     
REMARK   3      T33:   0.2372 T12:   0.0582                                     
REMARK   3      T13:   0.0274 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6741 L22:   1.2384                                     
REMARK   3      L33:   2.2876 L12:   1.4805                                     
REMARK   3      L13:   0.4398 L23:  -0.0064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1926 S12:   0.3830 S13:  -0.2237                       
REMARK   3      S21:  -0.1204 S22:   0.0683 S23:  -0.2183                       
REMARK   3      S31:   0.3278 S32:   0.3210 S33:   0.1134                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 332:486)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4035  17.1642   6.4542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1963 T22:   0.2917                                     
REMARK   3      T33:   0.2674 T12:  -0.0209                                     
REMARK   3      T13:  -0.0427 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0908 L22:   1.1775                                     
REMARK   3      L33:   4.0783 L12:   0.0951                                     
REMARK   3      L13:  -0.2018 L23:  -0.7397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0293 S12:   0.1164 S13:   0.0214                       
REMARK   3      S21:  -0.0413 S22:   0.0363 S23:   0.1892                       
REMARK   3      S31:  -0.0771 S32:  -0.4659 S33:  -0.0675                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 487:513)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9739   0.9793  13.7388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4297 T22:   0.6000                                     
REMARK   3      T33:   0.5000 T12:  -0.2721                                     
REMARK   3      T13:   0.0010 T23:   0.0819                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8619 L22:   8.0186                                     
REMARK   3      L33:   3.1970 L12:  -0.6572                                     
REMARK   3      L13:   1.8778 L23:  -1.3387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0649 S12:  -0.0944 S13:  -0.6848                       
REMARK   3      S21:   0.2626 S22:   0.1273 S23:   0.9049                       
REMARK   3      S31:   0.5871 S32:  -1.2217 S33:   0.0908                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 514:548)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3567   6.5767  -2.0484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3757 T22:   0.3232                                     
REMARK   3      T33:   0.2754 T12:  -0.0629                                     
REMARK   3      T13:  -0.0999 T23:   0.0693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5322 L22:   2.6792                                     
REMARK   3      L33:   7.1168 L12:  -2.2915                                     
REMARK   3      L13:  -0.7665 L23:   2.3523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1535 S12:   0.5940 S13:  -0.2056                       
REMARK   3      S21:  -0.3554 S22:  -0.2797 S23:   0.2213                       
REMARK   3      S31:  -0.1152 S32:  -0.0433 S33:   0.1152                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 5:45)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3828   6.3470 -61.6128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3611 T22:   0.3881                                     
REMARK   3      T33:   0.3375 T12:   0.0233                                     
REMARK   3      T13:  -0.0984 T23:  -0.1383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6968 L22:   2.0292                                     
REMARK   3      L33:   6.2394 L12:  -1.1688                                     
REMARK   3      L13:  -1.9621 L23:   0.6789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0667 S12:   0.5519 S13:   0.0424                       
REMARK   3      S21:  -0.2481 S22:  -0.1570 S23:   0.3111                       
REMARK   3      S31:  -0.1522 S32:  -0.7618 S33:   0.0528                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 46:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3161   1.5916 -51.7302              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3324 T22:   0.3331                                     
REMARK   3      T33:   0.2779 T12:  -0.0153                                     
REMARK   3      T13:  -0.0652 T23:  -0.0890                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3612 L22:   1.5944                                     
REMARK   3      L33:   3.6153 L12:  -0.1184                                     
REMARK   3      L13:   0.1712 L23:   0.5456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1164 S12:   0.1260 S13:  -0.1948                       
REMARK   3      S21:  -0.0951 S22:  -0.1281 S23:   0.1894                       
REMARK   3      S31:   0.4578 S32:  -0.2331 S33:  -0.0001                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 159:191)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0964   8.9240 -55.7360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3733 T22:   0.4063                                     
REMARK   3      T33:   0.2529 T12:  -0.0033                                     
REMARK   3      T13:  -0.0374 T23:  -0.0758                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7418 L22:   8.4533                                     
REMARK   3      L33:   3.9842 L12:  -6.3231                                     
REMARK   3      L13:   3.6663 L23:  -3.9254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2139 S12:   0.1549 S13:   0.0171                       
REMARK   3      S21:  -0.2873 S22:  -0.1010 S23:  -0.1936                       
REMARK   3      S31:  -0.2358 S32:   0.4092 S33:  -0.0929                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 192:298)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1055   1.4204 -45.1536              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3342 T22:   0.3623                                     
REMARK   3      T33:   0.2493 T12:   0.0475                                     
REMARK   3      T13:  -0.0605 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3638 L22:   3.2079                                     
REMARK   3      L33:   3.2961 L12:  -1.3846                                     
REMARK   3      L13:  -0.1103 L23:   1.3069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0947 S12:   0.0389 S13:  -0.1469                       
REMARK   3      S21:   0.1139 S22:   0.0847 S23:  -0.2489                       
REMARK   3      S31:   0.4399 S32:   0.5313 S33:  -0.1661                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 299:331)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5921  14.8574 -39.8306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2899 T22:   0.4019                                     
REMARK   3      T33:   0.3718 T12:  -0.0223                                     
REMARK   3      T13:  -0.0950 T23:  -0.0479                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1128 L22:   1.5616                                     
REMARK   3      L33:   5.0297 L12:  -1.5874                                     
REMARK   3      L13:  -1.7758 L23:   2.1952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2599 S12:   0.0838 S13:   0.7178                       
REMARK   3      S21:   0.0037 S22:   0.0653 S23:  -0.5209                       
REMARK   3      S31:  -0.5001 S32:   0.6874 S33:  -0.3079                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 332:382)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8477  -6.1588 -22.0526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6922 T22:   0.2904                                     
REMARK   3      T33:   0.3230 T12:   0.0109                                     
REMARK   3      T13:  -0.0924 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4156 L22:   5.2243                                     
REMARK   3      L33:   2.6897 L12:   2.0091                                     
REMARK   3      L13:   0.3087 L23:  -1.0110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3441 S12:  -0.0180 S13:  -0.7174                       
REMARK   3      S21:   0.2180 S22:  -0.0276 S23:  -0.0813                       
REMARK   3      S31:   0.9475 S32:   0.1173 S33:  -0.3314                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 383:486)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5652   6.0966 -29.4041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3401 T22:   0.3072                                     
REMARK   3      T33:   0.2848 T12:  -0.0705                                     
REMARK   3      T13:   0.0136 T23:  -0.1044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4513 L22:   2.1835                                     
REMARK   3      L33:   3.9890 L12:  -0.4092                                     
REMARK   3      L13:   1.3427 L23:  -0.7797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2227 S12:  -0.2085 S13:  -0.2112                       
REMARK   3      S21:   0.2218 S22:  -0.0906 S23:   0.3080                       
REMARK   3      S31:   0.2664 S32:  -0.3866 S33:  -0.1486                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 487:513)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2799  22.6124 -28.7967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4537 T22:   0.3507                                     
REMARK   3      T33:   0.3680 T12:   0.0462                                     
REMARK   3      T13:   0.0210 T23:  -0.1231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6116 L22:   8.9770                                     
REMARK   3      L33:   2.6601 L12:   2.2670                                     
REMARK   3      L13:   2.0295 L23:  -2.7004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0803 S12:  -0.5201 S13:   0.9030                       
REMARK   3      S21:   0.1608 S22:   0.1169 S23:   0.9942                       
REMARK   3      S31:  -0.3886 S32:  -0.4547 S33:  -0.0100                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 514:544)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6094  11.2404 -21.7206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4141 T22:   0.3668                                     
REMARK   3      T33:   0.1817 T12:  -0.0586                                     
REMARK   3      T13:   0.0006 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1329 L22:   1.9414                                     
REMARK   3      L33:   4.7414 L12:  -1.1544                                     
REMARK   3      L13:   5.0580 L23:  -0.4308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0204 S12:   0.1725 S13:  -0.3969                       
REMARK   3      S21:   0.2661 S22:   0.0161 S23:  -0.0415                       
REMARK   3      S31:   0.1128 S32:   0.5171 S33:   0.0176                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SOME REGIONS OF THE CATALYTIC SITE IS     
REMARK   3  DISORDERED. THE REFINEMENT INCLUDED AN INTEGRATED METHODOLOGY       
REMARK   3  CYCLING BETWEEN A CONVENTIONAL CRYSTALLOGRAPHIC REFINEMENT AND A    
REMARK   3  QUANTUM CHEMICAL CLUSTER APPROACH USING IMPLICIT DISPERSION-        
REMARK   3  CORRECTED DENSITY FUNCTIONAL THEORY (DFT) CALCULATIONS              
REMARK   4                                                                      
REMARK   4 5FPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65683.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.039                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MARMOSAIC 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   : 77695                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.7                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.2                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.70                               
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   (%): 70.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       39.41250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.77800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.77600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.77800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.41250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.77600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLU B     4                                                      
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     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     THR A 543    OG1  CG2                                            
REMARK 470     THR A 545    OG1  CG2                                            
REMARK 470     GLU A 546    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 548    CG   CD                                             
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   O3   HI6 B  1545     O    HOH B  2194              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -4.15     78.19                                   
REMARK 500    PRO A 104      151.66    -49.20                                   
REMARK 500    ALA A 167       68.51   -156.43                                   
REMARK 500    SGB A 203     -121.87     62.31                                   
REMARK 500    ASP A 306      -86.18   -132.56                                   
REMARK 500    VAL A 407      -61.47   -128.05                                   
REMARK 500    HIS A 447      122.45    -39.38                                   
REMARK 500    THR A 543      136.86   -174.70                                   
REMARK 500    GLU A 546     -139.52   -153.33                                   
REMARK 500    ALA A 547     -134.79    155.16                                   
REMARK 500    CYS B  96       10.09   -145.47                                   
REMARK 500    PHE B 158       -4.41   -140.49                                   
REMARK 500    ALA B 167       70.83   -151.51                                   
REMARK 500    SGB B 203     -122.73     55.36                                   
REMARK 500    ASP B 306      -84.37   -122.53                                   
REMARK 500    VAL B 407      -59.76   -122.97                                   
REMARK 500    HIS B 447      119.71    -38.18                                   
REMARK 500    ARG B 493       -6.89   -145.45                                   
REMARK 500    SER B 495     -150.52    -75.62                                   
REMARK 500    LYS B 496      120.40     61.66                                   
REMARK 500    SER B 497      156.24    -45.55                                   
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     HI6 B 1545                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE3 A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE3 B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 601  BOUND TO ASN A 350                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FOQ   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE IN COMPLEX WITH C7653                          
REMARK 900 RELATED ID: 5FPQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HOMO SAPIENS ACETYLCHOLINESTERASE                      
REMARK 900  PHOSPHONYLATED BY SARIN.                                            
DBREF  5FPP A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  5FPP B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 5FPP ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 5FPP 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 SGB 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 SGB 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 5FPP SGB A  203  SER  SARIN-SERINE                                       
MODRES 5FPP SGB B  203  SER  SARIN-SERINE                                       
HET    SGB  A 203      13                                                       
HET    SGB  B 203      13                                                       
HET    NAG  A 601      14                                                       
HET    CO3  A1549       4                                                       
HET    P6G  A1550      19                                                       
HET    AE3  A1551       9                                                       
HET    HI6  A1552      42                                                       
HET    HI6  B1545      36                                                       
HET    AE3  B1546       9                                                       
HET    CO3  B1547       4                                                       
HETNAM     SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     CO3 CARBONATE ION                                                    
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     AE3 2-(2-ETHOXYETHOXY)ETHANOL                                        
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
FORMUL   1  SGB    2(C7 H16 N O5 P)                                             
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  CO3    2(C O3 2-)                                                   
FORMUL   5  P6G    C12 H26 O7                                                   
FORMUL   6  AE3    2(C6 H14 O3)                                                 
FORMUL   7  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL  11  HOH   *457(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 SGB 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  TRP A  286  1                                  10    
HELIX   14  14 HIS A  287  LEU A  289  5                                   3    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  343  1                                   9    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  ALA A  542  1                                   9    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 SGB B  203  SER B  215  1                                  13    
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 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  VAL B  343  1                                   9    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  PHE B  455  1                                   6    
HELIX   49  49 GLY B  456  ASP B  460  5                                   5    
HELIX   50  50 ASP B  460  ASN B  464  5                                   5    
HELIX   51  51 THR B  466  GLY B  487  1                                  22    
HELIX   52  52 ARG B  525  ARG B  534  1                                  10    
HELIX   53  53 ARG B  534  THR B  543  1                                  10    
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  2.02  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.03  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.03  
LINK         C   GLU A 202                 N   SGB A 203     1555   1555  1.34  
LINK         C   SGB A 203                 N   ALA A 204     1555   1555  1.34  
LINK         ND2 ASN A 350                 C1  NAG A 601     1555   1555  1.47  
LINK         C   GLU B 202                 N   SGB B 203     1555   1555  1.34  
LINK         C   SGB B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0        -3.56                     
CISPEP   2 THR A  545    GLU A  546          0        -1.21                     
CISPEP   3 TYR B  105    PRO B  106          0         6.86                     
CISPEP   4 SER B  497    PRO B  498          0         2.14                     
SITE     1 AC1  1 TRP A 286                                                     
SITE     1 AC2 10 HIS A 381  GLN A 527  PHE A 535  HOH A2214                    
SITE     2 AC2 10 HOH A2263  ALA B 377  LEU B 380  HIS B 381                    
SITE     3 AC2 10 GLN B 527  PHE B 535                                          
SITE     1 AC3  4 HIS A 393  ASP A 404  ARG A 525  THR A 528                    
SITE     1 AC4 10 ASP A  74  TYR A 124  SGB A 203  TRP A 286                    
SITE     2 AC4 10 ARG A 296  PHE A 297  SER A 298  TYR A 337                    
SITE     3 AC4 10 PHE A 338  TYR A 341                                          
SITE     1 AC5  9 TRP B  86  TYR B 124  GLU B 202  SGB B 203                    
SITE     2 AC5  9 PHE B 295  TYR B 337  PHE B 338  TYR B 341                    
SITE     3 AC5  9 HOH B2194                                                     
SITE     1 AC6  1 GLN A 527                                                     
SITE     1 AC7  2 TRP B 286  HOH B2123                                          
SITE     1 AC8  5 SER A 347  ASN A 350  HOH A2200  HOH A2202                    
SITE     2 AC8  5 HOH A2207                                                     
CRYST1   78.825  111.552  227.556  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      0.012686  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008964  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004395        0.00000                         
TER    4278      PRO A 548                                                      
TER    8469      ALA B 544                                                      
MASTER      559    0   10   53   32    0   15    6 9061    2  180   86          
END                                                                             

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