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LongText Report for: 7r3c-pdb

Name Class
7r3c-pdb
HEADER    HYDROLASE                               07-FEB-22   7R3C              
TITLE     VX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)   
TITLE    2 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: VX PHOSPHONYLATION PRODUCT COVALENTLY ATTACHED TO     
COMPND   8 SER203                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    HYDROLASE, TERNARY COMPLEX, REACTIVATOR                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM                
REVDAT   1   27-APR-22 7R3C    0                                                
JRNL        AUTH   C.LINDGREN,N.FORSGREN,N.HOSTER,C.AKFUR,E.ARTURSSON,          
JRNL        AUTH 2 L.EDVINSSON,R.SVENSSON,F.WOREK,F.EKSTROM,A.LINUSSON          
JRNL        TITL   BROAD-SPECTRUM ANTIDOTE DISCOVERY BY UNTANGLING THE          
JRNL        TITL 2 REACTIVATION MECHANISM OF NERVE AGENT INHIBITED              
JRNL        TITL 3 ACETYLCHOLINESTERASE.                                        
JRNL        REF    CHEMISTRY                                  2022              
JRNL        REFN                   ISSN 0947-6539                               
JRNL        PMID   35420233                                                     
JRNL        DOI    10.1002/CHEM.202200678                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.336                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 77850                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.987                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1547                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.0277 -  5.3275    0.95     7058   144  0.1577 0.1684        
REMARK   3     2  5.3275 -  4.2328    0.96     6957   137  0.1317 0.1413        
REMARK   3     3  4.2328 -  3.6990    0.97     6938   135  0.1469 0.1767        
REMARK   3     4  3.6990 -  3.3613    0.98     6929   138  0.1724 0.2074        
REMARK   3     5  3.3613 -  3.1207    0.98     6896   136  0.1986 0.2307        
REMARK   3     6  3.1207 -  2.9369    0.98     6930   154  0.1989 0.2200        
REMARK   3     7  2.9369 -  2.7900    0.98     6910   140  0.1935 0.2688        
REMARK   3     8  2.7900 -  2.6686    0.99     6929   142  0.1920 0.2191        
REMARK   3     9  2.6686 -  2.5659    0.99     6928   157  0.1941 0.2219        
REMARK   3    10  2.5659 -  2.4774    0.99     6891   136  0.2024 0.2514        
REMARK   3    11  2.4774 -  2.4000    0.99     6937   128  0.2238 0.2815        
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)     : 0.213            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.250           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.86                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.61                          
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      :  0.007           8817                                  
REMARK   3   ANGLE     :  0.917          12017                                  
REMARK   3   CHIRALITY :  0.055           1279                                  
REMARK   3   PLANARITY :  0.006           1568                                  
REMARK   3   DIHEDRAL  : 10.288           7074                                  
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 1 THROUGH 158 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  31.0259  15.2563  31.3828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3157 T22:   0.2686                                     
REMARK   3      T33:   0.2397 T12:   0.0085                                     
REMARK   3      T13:  -0.0236 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9330 L22:   1.3090                                     
REMARK   3      L33:   3.4154 L12:   0.0356                                     
REMARK   3      L13:  -0.3932 L23:  -0.5436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1207 S12:  -0.2054 S13:   0.1269                       
REMARK   3      S21:   0.2810 S22:   0.0357 S23:  -0.0345                       
REMARK   3      S31:  -0.1148 S32:   0.0203 S33:   0.0638                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0531   3.9821  25.5722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4129 T22:   0.2803                                     
REMARK   3      T33:   0.3582 T12:   0.1151                                     
REMARK   3      T13:  -0.0260 T23:   0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0932 L22:   1.7520                                     
REMARK   3      L33:   5.1019 L12:   0.7499                                     
REMARK   3      L13:  -1.0287 L23:  -1.1328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1722 S12:  -0.2350 S13:  -0.2678                       
REMARK   3      S21:   0.0743 S22:  -0.0534 S23:  -0.3473                       
REMARK   3      S31:   0.6425 S32:   0.3670 S33:   0.2376                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0964  10.3808  14.1209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3263 T22:   0.2659                                     
REMARK   3      T33:   0.2515 T12:   0.0807                                     
REMARK   3      T13:   0.0046 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0616 L22:   1.4542                                     
REMARK   3      L33:   2.9663 L12:   0.7132                                     
REMARK   3      L13:  -0.2218 L23:  -0.7347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1038 S12:   0.1639 S13:  -0.0647                       
REMARK   3      S21:  -0.1367 S22:  -0.0180 S23:  -0.1910                       
REMARK   3      S31:   0.2172 S32:   0.2436 S33:   0.1596                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7775  -1.1469  11.4101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5841 T22:   0.3831                                     
REMARK   3      T33:   0.3762 T12:   0.0142                                     
REMARK   3      T13:   0.0740 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0963 L22:   2.8158                                     
REMARK   3      L33:   2.8461 L12:  -0.2611                                     
REMARK   3      L13:   0.0927 L23:   0.8536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1958 S12:   0.2186 S13:  -1.0249                       
REMARK   3      S21:   0.0387 S22:   0.1014 S23:  -0.0207                       
REMARK   3      S31:   0.8361 S32:   0.1260 S33:   0.0604                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6526  21.7759  -3.9043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2251 T22:   0.3683                                     
REMARK   3      T33:   0.2461 T12:  -0.0317                                     
REMARK   3      T13:  -0.0228 T23:   0.0820                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7083 L22:   5.3897                                     
REMARK   3      L33:   3.3402 L12:  -0.4386                                     
REMARK   3      L13:   0.8796 L23:  -1.8261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0157 S12:   0.2662 S13:   0.1522                       
REMARK   3      S21:  -0.1092 S22:  -0.0280 S23:  -0.0197                       
REMARK   3      S31:  -0.1730 S32:  -0.0086 S33:   0.0464                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 486 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7279  15.6203  10.7959              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2512 T22:   0.3604                                     
REMARK   3      T33:   0.2998 T12:  -0.0613                                     
REMARK   3      T13:  -0.0227 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3344 L22:   1.1708                                     
REMARK   3      L33:   4.1293 L12:  -0.4795                                     
REMARK   3      L13:   0.1582 L23:  -0.4776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0589 S12:   0.0690 S13:  -0.0129                       
REMARK   3      S21:  -0.0776 S22:   0.0340 S23:   0.2119                       
REMARK   3      S31:   0.1011 S32:  -0.4977 S33:   0.0573                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3073   1.4143  13.6553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5481 T22:   0.5922                                     
REMARK   3      T33:   0.4494 T12:  -0.2445                                     
REMARK   3      T13:   0.0353 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7250 L22:   2.4060                                     
REMARK   3      L33:   5.2230 L12:  -0.5293                                     
REMARK   3      L13:   0.2938 L23:  -2.9202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1599 S12:  -0.0202 S13:  -0.6460                       
REMARK   3      S21:   0.3036 S22:   0.1430 S23:   0.7104                       
REMARK   3      S31:   0.9144 S32:  -1.4885 S33:   0.0604                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9279   6.3272  -1.1315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4881 T22:   0.5331                                     
REMARK   3      T33:   0.3125 T12:   0.0014                                     
REMARK   3      T13:  -0.1185 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8828 L22:   3.0396                                     
REMARK   3      L33:   8.8070 L12:  -0.8393                                     
REMARK   3      L13:  -3.6822 L23:   2.5352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0931 S12:  -0.0271 S13:  -0.1668                       
REMARK   3      S21:  -0.3735 S22:  -0.1119 S23:   0.0853                       
REMARK   3      S31:   0.3266 S32:   0.1587 S33:   0.0495                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7069   6.0231 -61.3326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4468 T22:   0.4994                                     
REMARK   3      T33:   0.3562 T12:   0.0497                                     
REMARK   3      T13:  -0.0995 T23:  -0.1557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6392 L22:   2.3385                                     
REMARK   3      L33:   4.6927 L12:  -1.1718                                     
REMARK   3      L13:  -1.5410 L23:   0.3494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:   0.6116 S13:   0.1085                       
REMARK   3      S21:  -0.2702 S22:  -0.2030 S23:   0.3303                       
REMARK   3      S31:  -0.2551 S32:  -0.8045 S33:   0.1677                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3628  -4.2845 -52.8326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4494 T22:   0.4477                                     
REMARK   3      T33:   0.3405 T12:  -0.0334                                     
REMARK   3      T13:  -0.0685 T23:  -0.1182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4948 L22:   1.7181                                     
REMARK   3      L33:   6.6983 L12:  -0.5262                                     
REMARK   3      L13:   0.2128 L23:  -0.5137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1461 S12:   0.1155 S13:  -0.1683                       
REMARK   3      S21:  -0.1095 S22:  -0.0963 S23:   0.2023                       
REMARK   3      S31:   0.7719 S32:  -0.2168 S33:  -0.0478                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 297 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2429   3.4797 -48.6220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3579 T22:   0.3758                                     
REMARK   3      T33:   0.2320 T12:   0.0097                                     
REMARK   3      T13:  -0.0254 T23:  -0.0752                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9189 L22:   1.9874                                     
REMARK   3      L33:   3.0838 L12:  -0.4864                                     
REMARK   3      L13:   0.1042 L23:   0.8123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1032 S12:   0.1468 S13:  -0.1109                       
REMARK   3      S21:  -0.0276 S22:  -0.0675 S23:   0.0085                       
REMARK   3      S31:   0.2055 S32:   0.1655 S33:  -0.0309                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 298 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4844  14.1259 -40.0685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3951 T22:   0.4597                                     
REMARK   3      T33:   0.3920 T12:  -0.0722                                     
REMARK   3      T13:  -0.0173 T23:  -0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5790 L22:   1.6023                                     
REMARK   3      L33:   4.6315 L12:  -1.5963                                     
REMARK   3      L13:  -1.1965 L23:   1.6834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2653 S12:   0.3228 S13:   0.5518                       
REMARK   3      S21:  -0.0453 S22:  -0.0372 S23:  -0.3703                       
REMARK   3      S31:  -0.3045 S32:   0.6247 S33:  -0.2560                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3542  -6.0850 -21.9095              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8074 T22:   0.3445                                     
REMARK   3      T33:   0.3626 T12:   0.0129                                     
REMARK   3      T13:  -0.0732 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8805 L22:   2.3417                                     
REMARK   3      L33:   4.7488 L12:   0.6825                                     
REMARK   3      L13:   0.7522 L23:   0.0925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3001 S12:  -0.0961 S13:  -0.5113                       
REMARK   3      S21:   0.5450 S22:   0.0167 S23:   0.0099                       
REMARK   3      S31:   0.9625 S32:   0.0569 S33:  -0.2140                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9570   4.9182 -23.6440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4585 T22:   0.3752                                     
REMARK   3      T33:   0.2356 T12:  -0.0792                                     
REMARK   3      T13:   0.0031 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0466 L22:   1.7654                                     
REMARK   3      L33:   3.5015 L12:  -0.1844                                     
REMARK   3      L13:   0.1814 L23:  -0.3789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1844 S12:  -0.2635 S13:  -0.0885                       
REMARK   3      S21:   0.5123 S22:  -0.1778 S23:   0.0494                       
REMARK   3      S31:   0.3540 S32:   0.1153 S33:   0.0106                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 486 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5174   6.8773 -35.1408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3293 T22:   0.5875                                     
REMARK   3      T33:   0.3959 T12:  -0.0490                                     
REMARK   3      T13:   0.0424 T23:  -0.1538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4533 L22:   3.7647                                     
REMARK   3      L33:   4.2998 L12:   0.0810                                     
REMARK   3      L13:   0.1142 L23:  -0.6093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0209 S12:  -0.1058 S13:  -0.0520                       
REMARK   3      S21:   0.1472 S22:  -0.0948 S23:   0.5124                       
REMARK   3      S31:   0.2604 S32:  -0.9633 S33:   0.0246                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8470  22.4693 -28.6452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4884 T22:   0.4280                                     
REMARK   3      T33:   0.4005 T12:   0.0323                                     
REMARK   3      T13:  -0.0133 T23:  -0.1453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3238 L22:   4.5139                                     
REMARK   3      L33:   5.3457 L12:  -0.0681                                     
REMARK   3      L13:   0.7439 L23:  -2.8288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0456 S12:  -0.4369 S13:   0.6740                       
REMARK   3      S21:   0.1284 S22:   0.1043 S23:   0.4940                       
REMARK   3      S31:  -0.6349 S32:  -0.3220 S33:   0.0456                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8388  11.7232 -21.5371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5499 T22:   0.4442                                     
REMARK   3      T33:   0.2131 T12:  -0.0921                                     
REMARK   3      T13:   0.0571 T23:  -0.0478                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5083 L22:   1.5425                                     
REMARK   3      L33:   5.9225 L12:   0.1505                                     
REMARK   3      L13:   5.9877 L23:  -0.3125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0371 S12:   0.3558 S13:  -0.0226                       
REMARK   3      S21:   0.0777 S22:  -0.1263 S23:  -0.0433                       
REMARK   3      S31:   0.0021 S32:   0.5776 S33:   0.1270                       
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 7R3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292120845.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78034                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.1000                            
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) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 1J06                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-30 % (W/V) PEG750MME 0.1 M HEPES PH   
REMARK 280  7.0-7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K            
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       39.57700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.42600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.04700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.42600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.57700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.04700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     THR B   543                                                      
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     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 496    CG   CD   CE   NZ                                   
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   ND2  ASN A   350     O5   NAG A   602              2.13            
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       -2.94     75.24                                   
REMARK 500    PHE A 158       -1.09   -141.40                                   
REMARK 500    ALA A 167       76.95   -153.57                                   
REMARK 500    SVX A 203     -119.15     59.48                                   
REMARK 500    ASP A 306      -83.45   -126.35                                   
REMARK 500    VAL A 407      -62.02   -129.02                                   
REMARK 500    PHE B  47       -0.43     70.51                                   
REMARK 500    PRO B  55      153.14    -47.42                                   
REMARK 500    CYS B  96       10.65   -142.21                                   
REMARK 500    SVX B 203     -116.78     62.68                                   
REMARK 500    ASP B 306      -80.21   -124.12                                   
REMARK 500    ASP B 323       40.30    -84.18                                   
REMARK 500    VAL B 407      -62.72   -125.04                                   
REMARK 500    ARG B 525       56.29     36.60                                   
REMARK 500    LEU B 539      -73.16    -72.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7QYN   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)  
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM            
REMARK 900 RELATED ID: 7R0A   RELATED DB: PDB                                   
REMARK 900 SARIN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-              
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)       
REMARK 900 PYRIDINIUM                                                           
REMARK 900 RELATED ID: 7R02   RELATED DB: PDB                                   
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH N-(3-(DIETHYLAMINO)PROPYL)-4-   
REMARK 900 METHYL-3-NITROBENZAMIDE                                              
REMARK 900 RELATED ID: 7R2F   RELATED DB: PDB                                   
REMARK 900 TABUN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-              
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)       
REMARK 900 PYRIDINIUM                                                           
REMARK 900 RELATED ID: 7R4E   RELATED DB: PDB                                   
REMARK 900 RVX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO) 
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM            
DBREF  7R3C A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  7R3C B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQRES   1 A  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  543  SER VAL THR LEU PHE GLY GLU SVX ALA GLY ALA ALA SER          
SEQRES  17 A  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 B  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  543  SER VAL THR LEU PHE GLY GLU SVX ALA GLY ALA ALA SER          
SEQRES  17 B  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
MODRES 7R3C SVX A  203  SER  MODIFIED RESIDUE                                   
MODRES 7R3C SVX B  203  SER  MODIFIED RESIDUE                                   
HET    SVX  A 203      12                                                       
HET    SVX  B 203      12                                                       
HET    I1X  A 601      27                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    PG0  A 604       8                                                       
HET    PG0  A 605       8                                                       
HET    PG0  A 606       8                                                       
HET    PG0  A 607       8                                                       
HET    TOE  A 608      11                                                       
HET    P15  A 609      20                                                       
HET    I1X  B 601      27                                                       
HET    PG0  B 602       8                                                       
HET    PG0  B 603       8                                                       
HET    PG0  B 604       8                                                       
HET    TOE  B 605      11                                                       
HET    TOE  B 606      11                                                       
HETNAM     SVX O-[(R)-ETHOXY(METHYL)PHOSPHORYL]-L-SERINE                        
HETNAM     I1X 4-METHYL-3-NITRO-~{N}-[(2~{E},4~{E})-5-[2-                       
HETNAM   2 I1X  [(OXIDANYLAMINO)METHYL]PYRIDIN-1-YL]PENTA-2,4-                  
HETNAM   3 I1X  DIENYL]BENZAMIDE                                                
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     PG0 2-(2-METHOXYETHOXY)ETHANOL                                       
HETNAM     TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL                          
HETNAM     P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL                            
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     PG0 PEG 6000                                                         
FORMUL   1  SVX    2(C6 H14 N O5 P)                                             
FORMUL   3  I1X    2(C19 H23 N4 O4 1+)                                          
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   6  PG0    7(C5 H12 O3)                                                 
FORMUL  10  TOE    3(C7 H16 O4)                                                 
FORMUL  11  P15    C13 H28 O7                                                   
FORMUL  18  HOH   *295(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLN A    7  5                                   3    
HELIX    2 AA2 VAL A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  GLY A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  ILE A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SVX A  203  SER A  215  1                                  13    
HELIX   10 AB1 SER A  215  SER A  220  1                                   6    
HELIX   11 AB2 SER A  240  GLY A  256  1                                  17    
HELIX   12 AB3 ASP A  266  THR A  275  1                                  10    
HELIX   13 AB4 PRO A  277  GLU A  285  1                                   9    
HELIX   14 AB5 TRP A  286  LEU A  289  5                                   4    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASN A  464  5                                   9    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 ARG A  534  SER A  541  1                                   8    
HELIX   27 AC9 ASP B    5  GLN B    7  5                                   3    
HELIX   28 AD1 VAL B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  GLY B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  ILE B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SVX B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  SER B  220  1                                   6    
HELIX   37 AE1 SER B  240  GLY B  256  1                                  17    
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10    
HELIX   39 AE3 PRO B  277  ASP B  283  1                                   7    
HELIX   40 AE4 HIS B  284  VAL B  288  5                                   5    
HELIX   41 AE5 THR B  311  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  340  1                                   6    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  THR B  383  1                                  13    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASN B  464  5                                   9    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 ARG B  534  SER B  541  1                                   8    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  GLN A  16           
SHEET    1 AA211 ILE A  20  ALA A  24  0                                        
SHEET    2 AA211 GLY A  27  PRO A  36 -1  O  ALA A  31   N  ILE A  20           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  VAL A 101   N  PHE A  32           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 145           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  ASP A 193   N  THR A 112           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  VAL A 226   N  LEU A 199           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  ILE A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  GLN B  16           
SHEET    1 AA511 ILE B  20  ALA B  24  0                                        
SHEET    2 AA511 GLY B  27  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  THR B 198   N  ILE B 116           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  ILE B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.07  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.06  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.06  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.07  
LINK         C   GLU A 202                 N   SVX A 203     1555   1555  1.33  
LINK         C   SVX A 203                 N   ALA A 204     1555   1555  1.33  
LINK         ND2 ASN A 350                 C1  NAG A 602     1555   1555  1.43  
LINK         ND2 ASN A 464                 C1  NAG A 603     1555   1555  1.45  
LINK         C   GLU B 202                 N   SVX B 203     1555   1555  1.34  
LINK         C   SVX B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0        -2.16                     
CISPEP   2 TYR B  105    PRO B  106          0         2.22                     
CISPEP   3 SER B  497    PRO B  498          0        15.64                     
CRYST1   79.154  112.094  226.852  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      0.012634  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004408        0.00000                         
TER    4207      ALA A 542                                                      
TER    8375      ALA B 542                                                      
MASTER      550    0   17   52   32    0    0    6 8812    2  233   84          
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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