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LongText Report for: 5fpq-pdb

Name Class
5fpq-pdb
HEADER    HYDROLASE                               02-DEC-15   5FPQ              
TITLE     STRUCTURE OF HOMO SAPIENS ACETYLCHOLINESTERASE                        
TITLE    2 PHOSPHONYLATED BY SARIN.                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 33-574;                     
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
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, SIGNALING PROTEIN, ACETYLCHOLINESTERASE, SARIN, HI-6, QM,  
KEYWDS   2 DENSITY FUNCTIONAL THEORY CALCULATIONS, 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 5FPQ    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) : 45.410                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.36                          
REMARK   3   NUMBER OF REFLECTIONS             : 81198                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1784                          
REMARK   3   R VALUE            (WORKING SET) : 0.1767                          
REMARK   3   FREE R VALUE                     : 0.2103                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4144                            
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 45.4177 -  7.4468    0.98     2786   154  0.1788 0.1843        
REMARK   3     2  7.4468 -  5.9149    1.00     2676   143  0.1737 0.2029        
REMARK   3     3  5.9149 -  5.1684    0.99     2641   131  0.1557 0.2036        
REMARK   3     4  5.1684 -  4.6964    0.99     2617   147  0.1344 0.1657        
REMARK   3     5  4.6964 -  4.3601    1.00     2594   135  0.1273 0.1452        
REMARK   3     6  4.3601 -  4.1032    1.00     2637   130  0.1363 0.1462        
REMARK   3     7  4.1032 -  3.8978    1.00     2556   150  0.1444 0.1816        
REMARK   3     8  3.8978 -  3.7282    1.00     2580   145  0.1573 0.1795        
REMARK   3     9  3.7282 -  3.5847    0.99     2585   132  0.1735 0.2095        
REMARK   3    10  3.5847 -  3.4611    0.99     2560   146  0.1935 0.2379        
REMARK   3    11  3.4611 -  3.3529    0.99     2562   143  0.1982 0.2162        
REMARK   3    12  3.3529 -  3.2571    0.99     2549   143  0.1992 0.2289        
REMARK   3    13  3.2571 -  3.1714    1.00     2561   129  0.2072 0.2334        
REMARK   3    14  3.1714 -  3.0940    0.99     2556   133  0.2071 0.2543        
REMARK   3    15  3.0940 -  3.0237    1.00     2567   119  0.2084 0.2666        
REMARK   3    16  3.0237 -  2.9594    0.99     2565   144  0.1987 0.2412        
REMARK   3    17  2.9594 -  2.9002    1.00     2544   135  0.2058 0.2730        
REMARK   3    18  2.9002 -  2.8454    0.99     2529   148  0.2106 0.2403        
REMARK   3    19  2.8454 -  2.7946    0.99     2546   135  0.2008 0.2423        
REMARK   3    20  2.7946 -  2.7473    0.99     2485   146  0.1947 0.2216        
REMARK   3    21  2.7473 -  2.7030    0.99     2560   137  0.1909 0.2445        
REMARK   3    22  2.7030 -  2.6614    0.99     2562   140  0.1862 0.2159        
REMARK   3    23  2.6614 -  2.6222    0.99     2490   133  0.1861 0.2370        
REMARK   3    24  2.6222 -  2.5853    0.99     2579   138  0.1916 0.2047        
REMARK   3    25  2.5853 -  2.5504    0.99     2523   120  0.1908 0.2626        
REMARK   3    26  2.5504 -  2.5173    0.99     2504   161  0.2001 0.2592        
REMARK   3    27  2.5173 -  2.4858    0.99     2533   127  0.1909 0.2465        
REMARK   3    28  2.4858 -  2.4558    0.99     2504   136  0.2077 0.2526        
REMARK   3    29  2.4558 -  2.4273    0.99     2548   132  0.2081 0.2579        
REMARK   3    30  2.4273 -  2.4000    0.99     2555   132  0.2179 0.2771        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
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)     : 0.25             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.30            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.71                          
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           8687                                  
REMARK   3   ANGLE     :  1.081          11874                                  
REMARK   3   CHIRALITY :  0.079           1256                                  
REMARK   3   PLANARITY :  0.005           1578                                  
REMARK   3   DIHEDRAL  : 14.655           3143                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID    4  THROUGH  142 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  62.9177  32.1947  39.1464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1594 T22:   0.2468                                     
REMARK   3      T33:   0.1903 T12:  -0.0087                                     
REMARK   3      T13:  -0.0496 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4276 L22:   0.7869                                     
REMARK   3      L33:   2.3159 L12:   0.0907                                     
REMARK   3      L13:   0.5150 L23:  -0.0428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:  -0.1097 S13:  -0.0389                       
REMARK   3      S21:   0.0675 S22:   0.0131 S23:  -0.0556                       
REMARK   3      S31:  -0.1586 S32:   0.1993 S33:  -0.0038                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  143  THROUGH  190 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0673  35.8377  37.0123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1948 T22:   0.2712                                     
REMARK   3      T33:   0.1733 T12:   0.0369                                     
REMARK   3      T13:  -0.0182 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4735 L22:   2.4525                                     
REMARK   3      L33:   1.4212 L12:   1.1463                                     
REMARK   3      L13:   0.5004 L23:   0.1491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0573 S12:  -0.1476 S13:   0.0178                       
REMARK   3      S21:   0.0901 S22:   0.0295 S23:   0.1616                       
REMARK   3      S31:  -0.3305 S32:  -0.2472 S33:   0.0032                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  191  THROUGH  255 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9071  33.6105  27.1921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1833 T22:   0.2665                                     
REMARK   3      T33:   0.1925 T12:   0.0515                                     
REMARK   3      T13:  -0.0312 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3232 L22:   0.7857                                     
REMARK   3      L33:   1.5654 L12:   0.3381                                     
REMARK   3      L13:   0.1483 L23:  -0.5353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0932 S12:   0.1613 S13:   0.0258                       
REMARK   3      S21:   0.0655 S22:   0.1439 S23:   0.0739                       
REMARK   3      S31:  -0.2348 S32:  -0.2431 S33:  -0.0259                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  256  THROUGH  331 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  42.7174  27.0438  28.6871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1916 T22:   0.3805                                     
REMARK   3      T33:   0.2404 T12:   0.0279                                     
REMARK   3      T13:  -0.0331 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2290 L22:   0.5492                                     
REMARK   3      L33:   1.6769 L12:   0.7828                                     
REMARK   3      L13:  -0.3695 L23:  -0.6775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0867 S12:  -0.0182 S13:   0.0129                       
REMARK   3      S21:  -0.0871 S22:   0.0808 S23:   0.0295                       
REMARK   3      S31:   0.0175 S32:  -0.4922 S33:   0.0859                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  332  THROUGH  466 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6208  22.5201  11.1382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2132 T22:   0.2961                                     
REMARK   3      T33:   0.2481 T12:   0.0227                                     
REMARK   3      T13:  -0.0208 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4963 L22:   0.0726                                     
REMARK   3      L33:   1.4960 L12:   0.2025                                     
REMARK   3      L13:   0.6730 L23:   0.2528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0888 S12:  -0.0221 S13:  -0.1497                       
REMARK   3      S21:  -0.0741 S22:  -0.0458 S23:  -0.0589                       
REMARK   3      S31:   0.1033 S32:   0.1642 S33:  -0.0201                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  467  THROUGH  513 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7767  42.2931  13.6956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3072 T22:   0.3572                                     
REMARK   3      T33:   0.2557 T12:  -0.1894                                     
REMARK   3      T13:  -0.0467 T23:   0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5383 L22:   0.7785                                     
REMARK   3      L33:   0.9383 L12:  -0.4632                                     
REMARK   3      L13:   1.0612 L23:  -0.2941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1697 S12:   0.4215 S13:   0.2059                       
REMARK   3      S21:  -0.1949 S22:  -0.0051 S23:  -0.0913                       
REMARK   3      S31:  -0.3745 S32:   0.3598 S33:   0.0348                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID  514  THROUGH  542 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4319  32.4997   5.0517              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2714 T22:   0.3233                                     
REMARK   3      T33:   0.2027 T12:  -0.0299                                     
REMARK   3      T13:  -0.0398 T23:   0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6742 L22:   0.7774                                     
REMARK   3      L33:   1.3115 L12:   0.4072                                     
REMARK   3      L13:   0.9004 L23:   0.2791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1811 S12:  -0.0186 S13:  -0.1643                       
REMARK   3      S21:  -0.0421 S22:  -0.1855 S23:  -0.0527                       
REMARK   3      S31:  -0.1788 S32:   0.1649 S33:   0.0684                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID    4  THROUGH   32 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 102.2755  35.3433  57.6287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3751 T22:   0.2602                                     
REMARK   3      T33:   0.1958 T12:  -0.0913                                     
REMARK   3      T13:   0.0321 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8447 L22:   4.6571                                     
REMARK   3      L33:   0.2132 L12:  -0.2202                                     
REMARK   3      L13:  -0.3156 L23:  -0.1174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0642 S12:  -0.3892 S13:  -0.0599                       
REMARK   3      S21:   0.4001 S22:  -0.0539 S23:   0.0728                       
REMARK   3      S31:   0.1244 S32:  -0.1321 S33:   0.1286                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   33  THROUGH   58 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 112.0381  20.8749  44.0790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2930 T22:   0.2358                                     
REMARK   3      T33:   0.2031 T12:  -0.0280                                     
REMARK   3      T13:  -0.0126 T23:   0.0401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7453 L22:   0.0446                                     
REMARK   3      L33:   0.9885 L12:  -0.1043                                     
REMARK   3      L13:  -0.8429 L23:   0.1559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2026 S12:  -0.2898 S13:  -0.3495                       
REMARK   3      S21:   0.2537 S22:  -0.0052 S23:   0.0888                       
REMARK   3      S31:   0.3401 S32:   0.3050 S33:   0.1250                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   59  THROUGH   86 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 119.1159  40.9072  40.9541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2745 T22:   0.3186                                     
REMARK   3      T33:   0.2521 T12:  -0.1208                                     
REMARK   3      T13:  -0.0466 T23:   0.0375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0200 L22:   0.9259                                     
REMARK   3      L33:   0.6468 L12:   0.1299                                     
REMARK   3      L13:  -0.3508 L23:  -0.4434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0408 S12:  -0.2012 S13:   0.0694                       
REMARK   3      S21:   0.1691 S22:  -0.1372 S23:  -0.0647                       
REMARK   3      S31:  -0.1905 S32:   0.3095 S33:   0.0541                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID   87  THROUGH  170 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 107.7817  34.8396  40.8791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1833 T22:   0.1976                                     
REMARK   3      T33:   0.1860 T12:  -0.0794                                     
REMARK   3      T13:   0.0161 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4669 L22:   1.4824                                     
REMARK   3      L33:   1.2341 L12:  -0.5767                                     
REMARK   3      L13:  -0.3649 L23:   0.4698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0277 S12:  -0.1518 S13:  -0.0885                       
REMARK   3      S21:   0.2868 S22:  -0.0716 S23:   0.0599                       
REMARK   3      S31:  -0.0148 S32:   0.0580 S33:   0.0982                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  171  THROUGH  300 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 111.7373  29.6781  29.1656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1350 T22:   0.2246                                     
REMARK   3      T33:   0.2373 T12:  -0.0660                                     
REMARK   3      T13:  -0.0073 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7522 L22:   1.0383                                     
REMARK   3      L33:   1.2084 L12:  -0.3082                                     
REMARK   3      L13:  -0.1669 L23:  -0.1438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1375 S12:   0.1698 S13:  -0.0090                       
REMARK   3      S21:  -0.0164 S22:  -0.1572 S23:   0.0318                       
REMARK   3      S31:   0.0383 S32:   0.0968 S33:   0.0160                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  301  THROUGH  341 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 103.0289  37.0343  22.1610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1816 T22:   0.2987                                     
REMARK   3      T33:   0.2374 T12:  -0.0455                                     
REMARK   3      T13:  -0.0049 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7787 L22:   0.6041                                     
REMARK   3      L33:   0.9233 L12:  -0.5510                                     
REMARK   3      L13:  -0.1050 L23:  -0.2303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1470 S12:   0.1682 S13:  -0.0537                       
REMARK   3      S21:   0.0499 S22:  -0.1292 S23:   0.1194                       
REMARK   3      S31:   0.0670 S32:   0.0282 S33:  -0.0295                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  342  THROUGH  406 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 117.3368  53.0670  11.7117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2448 T22:   0.2933                                     
REMARK   3      T33:   0.2326 T12:  -0.0579                                     
REMARK   3      T13:  -0.0230 T23:   0.0675                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8298 L22:   0.5894                                     
REMARK   3      L33:   1.4332 L12:   0.0134                                     
REMARK   3      L13:   0.6803 L23:  -0.3674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:  -0.0790 S13:  -0.0262                       
REMARK   3      S21:  -0.0133 S22:  -0.1704 S23:  -0.2292                       
REMARK   3      S31:  -0.1521 S32:   0.3548 S33:   0.1097                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  407  THROUGH  466 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 104.4376  50.9172  30.8354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2306 T22:   0.1917                                     
REMARK   3      T33:   0.2180 T12:  -0.0529                                     
REMARK   3      T13:  -0.0214 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9111 L22:   0.4327                                     
REMARK   3      L33:   0.8573 L12:  -0.2574                                     
REMARK   3      L13:  -0.3250 L23:   0.0366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0811 S12:   0.0314 S13:   0.2179                       
REMARK   3      S21:   0.1587 S22:  -0.1105 S23:   0.0368                       
REMARK   3      S31:  -0.1381 S32:   0.0002 S33:   0.0147                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  467  THROUGH  513 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  91.7471  52.0273  32.7954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1801 T22:   0.2287                                     
REMARK   3      T33:   0.2828 T12:   0.0370                                     
REMARK   3      T13:   0.0181 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2272 L22:   0.8746                                     
REMARK   3      L33:   2.2707 L12:   0.1994                                     
REMARK   3      L13:   0.3867 L23:   0.0539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:  -0.0160 S13:   0.1811                       
REMARK   3      S21:   0.0475 S22:  -0.0234 S23:   0.1732                       
REMARK   3      S31:  -0.2453 S32:  -0.3891 S33:   0.0088                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID  514  THROUGH  542 )              
REMARK   3    ORIGIN FOR THE GROUP (A): 100.9717  49.3503  14.2716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1849 T22:   0.1689                                     
REMARK   3      T33:   0.1728 T12:   0.0545                                     
REMARK   3      T13:  -0.0181 T23:   0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7930 L22:   0.2752                                     
REMARK   3      L33:   1.8051 L12:   0.3654                                     
REMARK   3      L13:  -0.2341 L23:  -0.3901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2108 S12:   0.0836 S13:  -0.0662                       
REMARK   3      S21:  -0.1316 S22:   0.0135 S23:   0.3926                       
REMARK   3      S31:  -0.2084 S32:   0.0801 S33:   0.0423                       
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 5FPQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65684.                                       
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        : 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) : 0.919                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81717                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.9                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5                                  
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.20                              
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.90                               
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 4EY4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.75000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      215.50000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      215.50000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      107.75000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000       52.43450            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000      -90.81922            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
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 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000      104.86900            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     ALA A   497                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     ALA B   497                                                      
REMARK 465     THR B   543                                                      
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   OH5  1PE A  1543     O    HOH A  2041              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    PRO A  25       30.38    -65.51                                   
REMARK 500    PHE A  47       -4.70     78.14                                   
REMARK 500    ALA A 167       76.39   -150.44                                   
REMARK 500    SER A 196       65.23   -117.31                                   
REMARK 500    ASP A 306      -86.77    -91.90                                   
REMARK 500    HIS A 387       54.93   -142.66                                   
REMARK 500    VAL A 407      -63.22   -131.45                                   
REMARK 500    ASN A 464       50.67   -116.43                                   
REMARK 500    ASP A 514     -160.88   -164.84                                   
REMARK 500    PHE B  47       -6.98     77.24                                   
REMARK 500    ALA B  62       50.01   -113.45                                   
REMARK 500    ALA B 167       72.03   -150.85                                   
REMARK 500    ASP B 306      -91.19    -95.25                                   
REMARK 500    VAL B 407      -60.60   -131.20                                   
REMARK 500    ASP B 514     -153.05   -156.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  264     ASN A  265                  136.71                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND ARE                    
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE): THESE HAVE BEEN REPOSITIONED              
REMARK 525 BY APPLYING THE SYMMETRY TRANSFORMATION INDICATED.                   
REMARK 525                                                                      
REMARK 525  M RES CSSEQI     ORIGINAL COORDINATES   SYMMETRY TRANS.    DIST.    
REMARK 525                    X       Y       Z                                 
REMARK 525    HOH D 113   127.565  21.434  39.207    001      455      3.41     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A1543                 
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: 5FPP   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A PRE-REACTION TERNAY COMPLEX BETWEEN                  
REMARK 900  SARIN-ACETYLCHOLINESTERASE AND HI-6                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 OTHER_DETAILS: SARIN PHOSPHONYLATION PRODUCT COVALENTLY ATTACHED TO  
REMARK 999  SER203D                                                             
DBREF  5FPQ A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  5FPQ B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
MODRES 5FPQ SGB A  203  SER  MODIFIED SERINE                                    
MODRES 5FPQ SGB B  203  SER  MODIFIED SERINE                                    
HET    SGB  A 203      13                                                       
HET    SGB  B 203      13                                                       
HET    1PE  A1543      38                                                       
HETNAM     SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-                      
HETNAM   2 SGB  SERINE                                                          
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   3  SGB    2(C7 H16 N O5 P)                                             
FORMUL   4  1PE    C10 H22 O6                                                   
FORMUL   5  HOH   *113(H2 O)                                                    
HELIX    1   1 ASP A    5  GLU A    7  5                                   3    
HELIX    2   2 MET 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  ARG A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  VAL A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 ALA A  204  LEU A  214  1                                  11    
HELIX   10  10 SER A  215  GLY A  220  1                                   6    
HELIX   11  11 GLY 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 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 PHE A  535  SER A  541  1                                   7    
HELIX   27  27 ASP B    5  GLU B    7  5                                   3    
HELIX   28  28 MET B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  ARG B  143  1                                   9    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  VAL B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 ALA B  204  LEU B  214  1                                  11    
HELIX   36  36 SER B  215  GLY B  220  1                                   6    
HELIX   37  37 MET B  241  VAL B  255  1                                  15    
HELIX   38  38 ASN B  265  THR B  275  1                                  11    
HELIX   39  39 PRO B  277  ASN B  283  1                                   7    
HELIX   40  40 HIS B  284  LEU B  289  5                                   6    
HELIX   41  41 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  VAL B  340  1                                   6    
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 THR B  466  GLY B  487  1                                  22    
HELIX   51  51 ARG B  525  ARG B  534  1                                  10    
HELIX   52  52 ARG B  534  ALA B  542  1                                   9    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  LEU A  22  0                                        
SHEET    2  AB11 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
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  GLY A 201  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  VAL 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  VAL B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  LEU B  22  0                                        
SHEET    2  BB11 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
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  GLY B 201  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  VAL B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SHEET    1  BD 2 VAL B 239  GLY B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.07  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.05  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.06  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.08  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         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         C   GLU B 202                 N   SGB B 203     1555   1555  1.35  
LINK         C   SGB B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0         2.77                     
CISPEP   2 TYR B  105    PRO B  106          0         1.48                     
SITE     1 AC1  6 MET A 241  ASP A 304  GLY A 305  ASP A 306                    
SITE     2 AC1  6 HOH A2041  ASN B 283                                          
CRYST1  104.869  104.869  323.250  90.00  90.00 120.00 P 31 2 1     12          
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      0.009536  0.005505  0.000000        0.00000                         
SCALE2      0.000000  0.011011  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003094        0.00000                         
TER    4205      ALA A 542                                                      
TER    8402      ALA B 542                                                      
MASTER      613    0    3   52   34    0    2    6 8551    2   61   84          
END                                                                             

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