Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 7r4e-pdb

Name Class
7r4e-pdb
HEADER    HYDROLASE                               08-FEB-22   7R4E              
TITLE     RVX-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: RVX PHOSPHYLATION 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: 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 7R4E    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.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.335                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40697                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.949                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 793                             
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 29.1069 -  5.4415    1.00     6939   135  0.1589 0.1899        
REMARK   3     2  5.4415 -  4.3236    1.00     6702   132  0.1346 0.1468        
REMARK   3     3  4.3236 -  3.7784    1.00     6595   125  0.1470 0.1991        
REMARK   3     4  3.7784 -  3.4335    0.99     6578   142  0.1748 0.2267        
REMARK   3     5  3.4335 -  3.1878    1.00     6571   115  0.2031 0.2653        
REMARK   3     6  3.1878 -  3.0000    0.99     6519   144  0.2230 0.2949        
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)     : 0.315            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.787           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.27                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.45                          
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      :  0.009           8837                                  
REMARK   3   ANGLE     :  1.044          12057                                  
REMARK   3   CHIRALITY :  0.057           1289                                  
REMARK   3   PLANARITY :  0.007           1576                                  
REMARK   3   DIHEDRAL  : 12.553           7088                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 36 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6333  13.6036  44.2823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5795 T22:   0.5448                                     
REMARK   3      T33:   0.3358 T12:   0.0053                                     
REMARK   3      T13:   0.0444 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0336 L22:   1.7318                                     
REMARK   3      L33:   5.7225 L12:   0.4778                                     
REMARK   3      L13:  -1.0739 L23:  -0.2573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5637 S12:  -0.6587 S13:   0.3418                       
REMARK   3      S21:   0.6552 S22:   0.3736 S23:   0.0607                       
REMARK   3      S31:  -0.1751 S32:  -0.3990 S33:  -0.0270                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1609  15.3259  27.9661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3216 T22:   0.3459                                     
REMARK   3      T33:   0.2144 T12:   0.0012                                     
REMARK   3      T13:  -0.0258 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5245 L22:   2.0639                                     
REMARK   3      L33:   5.3475 L12:   0.2262                                     
REMARK   3      L13:  -0.4336 L23:  -0.5621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1560 S12:  -0.2158 S13:   0.2342                       
REMARK   3      S21:   0.1686 S22:   0.1112 S23:  -0.0257                       
REMARK   3      S31:  -0.0035 S32:   0.1141 S33:   0.0179                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 240 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1299   3.0860  21.1794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4120 T22:   0.2245                                     
REMARK   3      T33:   0.2919 T12:   0.0536                                     
REMARK   3      T13:  -0.0164 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1644 L22:   1.6534                                     
REMARK   3      L33:   5.3510 L12:   0.9523                                     
REMARK   3      L13:  -0.2028 L23:  -0.5406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1123 S12:  -0.1055 S13:  -0.4225                       
REMARK   3      S21:   0.0642 S22:   0.0918 S23:  -0.1457                       
REMARK   3      S31:   0.5679 S32:  -0.0095 S33:   0.0548                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 297 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.9405  16.2017  10.5695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4079 T22:   0.6275                                     
REMARK   3      T33:   0.3579 T12:   0.0395                                     
REMARK   3      T13:   0.0151 T23:   0.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3202 L22:   1.7201                                     
REMARK   3      L33:   4.7017 L12:   1.9107                                     
REMARK   3      L13:   0.6048 L23:   0.4325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4060 S12:   0.8688 S13:   0.2890                       
REMARK   3      S21:  -0.3052 S22:   0.1645 S23:  -0.2866                       
REMARK   3      S31:  -0.2766 S32:   0.7643 S33:   0.1465                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9286  -0.9766  11.1923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6244 T22:   0.3356                                     
REMARK   3      T33:   0.4567 T12:  -0.0304                                     
REMARK   3      T13:   0.0470 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4991 L22:   0.4548                                     
REMARK   3      L33:   4.4486 L12:  -0.5240                                     
REMARK   3      L13:   0.6026 L23:   0.2433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0355 S12:   0.2985 S13:  -1.1284                       
REMARK   3      S21:  -0.2907 S22:   0.0342 S23:   0.2070                       
REMARK   3      S31:   0.8754 S32:   0.4628 S33:   0.0361                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4321  21.7321  -3.9839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3338 T22:   0.4806                                     
REMARK   3      T33:   0.2759 T12:  -0.0321                                     
REMARK   3      T13:  -0.0613 T23:   0.0886                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1388 L22:   8.5341                                     
REMARK   3      L33:   4.0064 L12:  -1.6876                                     
REMARK   3      L13:  -1.9180 L23:   2.8043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1656 S12:   0.1268 S13:   0.1810                       
REMARK   3      S21:  -0.6090 S22:   0.0729 S23:  -0.1768                       
REMARK   3      S31:  -0.3103 S32:   0.1172 S33:  -0.2143                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2934  13.8841   2.4931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2644 T22:   0.4960                                     
REMARK   3      T33:   0.3056 T12:  -0.0731                                     
REMARK   3      T13:  -0.0595 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2899 L22:   2.4025                                     
REMARK   3      L33:   4.0313 L12:  -0.1601                                     
REMARK   3      L13:   0.1012 L23:  -0.4248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0959 S12:   0.2278 S13:  -0.0502                       
REMARK   3      S21:  -0.2202 S22:   0.0417 S23:   0.2190                       
REMARK   3      S31:   0.2546 S32:  -0.2737 S33:  -0.1393                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 441 THROUGH 486 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3682  16.9504  20.5949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3214 T22:   0.6619                                     
REMARK   3      T33:   0.3636 T12:   0.0235                                     
REMARK   3      T13:  -0.0022 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3749 L22:   3.0549                                     
REMARK   3      L33:   4.4670 L12:  -0.0226                                     
REMARK   3      L13:   0.4943 L23:  -1.0961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0554 S12:  -0.1879 S13:   0.0163                       
REMARK   3      S21:   0.0527 S22:   0.1148 S23:   0.4508                       
REMARK   3      S31:  -0.0632 S32:  -0.9949 S33:  -0.1561                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1624   1.1601  13.5060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4090 T22:   0.7450                                     
REMARK   3      T33:   0.5314 T12:  -0.2473                                     
REMARK   3      T13:  -0.0360 T23:   0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0790 L22:   8.0260                                     
REMARK   3      L33:   4.4010 L12:  -1.1009                                     
REMARK   3      L13:   2.8013 L23:  -0.7381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0093 S12:   0.1112 S13:  -0.7158                       
REMARK   3      S21:  -0.1142 S22:   0.1621 S23:   0.9039                       
REMARK   3      S31:   0.5129 S32:  -1.6026 S33:   0.0769                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 543 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2528   6.1997  -1.5407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5557 T22:   0.7386                                     
REMARK   3      T33:   0.3403 T12:   0.0208                                     
REMARK   3      T13:  -0.1834 T23:   0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9232 L22:   3.1101                                     
REMARK   3      L33:   9.3988 L12:  -0.3465                                     
REMARK   3      L13:  -2.5473 L23:   3.1724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1152 S12:   0.1845 S13:  -0.1391                       
REMARK   3      S21:  -0.4575 S22:  -0.1758 S23:   0.1680                       
REMARK   3      S31:   0.2149 S32:  -0.3925 S33:   0.0540                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8430   5.9741 -61.9762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4752 T22:   0.7260                                     
REMARK   3      T33:   0.3749 T12:   0.0156                                     
REMARK   3      T13:  -0.0949 T23:  -0.1625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4271 L22:   1.3373                                     
REMARK   3      L33:   4.1920 L12:  -1.1420                                     
REMARK   3      L13:  -1.5312 L23:   0.0106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1868 S12:   0.8588 S13:  -0.1638                       
REMARK   3      S21:  -0.1264 S22:  -0.1952 S23:   0.3608                       
REMARK   3      S31:  -0.2184 S32:  -0.7860 S33:  -0.0332                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6896   1.2215 -51.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4093 T22:   0.5798                                     
REMARK   3      T33:   0.3067 T12:  -0.0461                                     
REMARK   3      T13:  -0.0600 T23:  -0.1013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4567 L22:   2.4088                                     
REMARK   3      L33:   4.2041 L12:  -0.1077                                     
REMARK   3      L13:   0.2742 L23:   0.6872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0624 S12:   0.2430 S13:  -0.2072                       
REMARK   3      S21:   0.0740 S22:  -0.2167 S23:   0.2603                       
REMARK   3      S31:   0.4380 S32:  -0.3266 S33:   0.1005                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5008   2.9453 -47.9872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4097 T22:   0.6087                                     
REMARK   3      T33:   0.2924 T12:   0.0078                                     
REMARK   3      T13:  -0.0566 T23:  -0.0763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7328 L22:   4.1060                                     
REMARK   3      L33:   3.1490 L12:  -1.9022                                     
REMARK   3      L13:   0.1670 L23:   0.5347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1432 S12:   0.0705 S13:  -0.0985                       
REMARK   3      S21:   0.0503 S22:   0.0320 S23:  -0.3130                       
REMARK   3      S31:   0.2923 S32:   0.5142 S33:  -0.1522                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 301 THROUGH 341 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2459  10.6260 -37.0414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4082 T22:   0.6519                                     
REMARK   3      T33:   0.3784 T12:  -0.0621                                     
REMARK   3      T13:  -0.1146 T23:  -0.0773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0017 L22:   1.8784                                     
REMARK   3      L33:   2.8597 L12:  -0.7374                                     
REMARK   3      L13:  -0.0523 L23:   0.0122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3145 S12:   0.1068 S13:   0.1521                       
REMARK   3      S21:   0.0797 S22:  -0.1787 S23:  -0.1788                       
REMARK   3      S31:  -0.1072 S32:   0.4800 S33:  -0.1208                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3653  -5.2915 -18.3442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8279 T22:   0.4553                                     
REMARK   3      T33:   0.3395 T12:  -0.0352                                     
REMARK   3      T13:  -0.1274 T23:   0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2569 L22:   4.5581                                     
REMARK   3      L33:   2.8353 L12:   2.4268                                     
REMARK   3      L13:   1.8854 L23:   0.2583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4151 S12:  -0.6674 S13:  -0.4022                       
REMARK   3      S21:   0.3252 S22:  -0.1231 S23:  -0.0903                       
REMARK   3      S31:   0.6491 S32:  -0.2106 S33:  -0.3301                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 486 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1931   8.3939 -33.4674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4176 T22:   0.5315                                     
REMARK   3      T33:   0.3028 T12:   0.0099                                     
REMARK   3      T13:   0.0092 T23:  -0.1409                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7454 L22:   3.6695                                     
REMARK   3      L33:   4.2914 L12:   0.8748                                     
REMARK   3      L13:  -0.2101 L23:  -0.4860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1587 S12:  -0.1109 S13:   0.0402                       
REMARK   3      S21:   0.0393 S22:  -0.1008 S23:   0.4064                       
REMARK   3      S31:   0.2722 S32:  -0.6730 S33:  -0.0652                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7830  22.3711 -28.9014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4549 T22:   0.3749                                     
REMARK   3      T33:   0.3331 T12:   0.0231                                     
REMARK   3      T13:   0.0214 T23:  -0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0362 L22:   7.2481                                     
REMARK   3      L33:   9.0981 L12:  -0.0331                                     
REMARK   3      L13:   2.4339 L23:  -2.1781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5115 S12:  -0.2789 S13:   0.5395                       
REMARK   3      S21:  -0.0253 S22:  -0.0758 S23:   0.5575                       
REMARK   3      S31:  -0.1607 S32:  -0.4506 S33:  -0.4401                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8481  11.5854 -21.7175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6252 T22:   0.7450                                     
REMARK   3      T33:   0.2499 T12:  -0.0207                                     
REMARK   3      T13:   0.0278 T23:  -0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1644 L22:   1.5566                                     
REMARK   3      L33:   3.3503 L12:  -0.3300                                     
REMARK   3      L13:   4.1463 L23:  -0.4912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1599 S12:   0.1254 S13:  -0.0872                       
REMARK   3      S21:   0.2309 S22:  -0.0820 S23:  -0.0896                       
REMARK   3      S31:   0.3297 S32:   0.3702 S33:   0.2736                       
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 7R4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292120855.                                   
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) : 1.000                              
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   : 40881                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.107                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.100                              
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   (%): 70.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16                     
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       39.47800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.77450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.49850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.77450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.47800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.49850            
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   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     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     ASP A 323    CG   OD1  OD2                                       
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     GLU B 268    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: 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    ARG A   3       31.10    -98.98                                   
REMARK 500    PHE A  47      -11.83     78.18                                   
REMARK 500    PHE A  80      116.74   -161.01                                   
REMARK 500    ASP A  95       93.54    -64.69                                   
REMARK 500    CYS A  96        3.05   -152.89                                   
REMARK 500    TYR A 133       31.83    -96.78                                   
REMARK 500    RVX A 203     -120.83     50.42                                   
REMARK 500    CYS A 257       76.37   -118.12                                   
REMARK 500    ASP A 306      -80.51   -123.58                                   
REMARK 500    PHE A 321       28.15   -140.75                                   
REMARK 500    ASP A 323       42.48    -76.26                                   
REMARK 500    VAL A 407      -65.75   -138.04                                   
REMARK 500    ASP A 488      113.00   -170.43                                   
REMARK 500    ARG A 493       49.02    -88.17                                   
REMARK 500    ASP A 494       93.13   -170.97                                   
REMARK 500    GLN A 508       56.10     33.49                                   
REMARK 500    ALA A 542       50.77    -98.23                                   
REMARK 500    PRO B  41       48.87    -86.34                                   
REMARK 500    ALA B 109      -70.23    -63.47                                   
REMARK 500    PHE B 123       12.18     56.85                                   
REMARK 500    ALA B 127      143.53   -175.47                                   
REMARK 500    ALA B 167       64.87   -156.81                                   
REMARK 500    RVX B 203     -122.78     59.47                                   
REMARK 500    HIS B 223      -30.81   -132.44                                   
REMARK 500    THR B 275       37.11    -92.87                                   
REMARK 500    THR B 275       37.11    -94.89                                   
REMARK 500    TRP B 286        2.17    -63.42                                   
REMARK 500    PRO B 301      158.98    -49.90                                   
REMARK 500    ASP B 306      -87.13   -103.28                                   
REMARK 500    TYR B 341       32.62    -96.96                                   
REMARK 500    SER B 347      139.83    173.95                                   
REMARK 500    VAL B 367       75.23   -119.07                                   
REMARK 500    VAL B 407      -63.91   -130.23                                   
REMARK 500    HIS B 447      104.41    -58.18                                   
REMARK 500    PRO B 498       90.97    -53.16                                   
REMARK 500    SER B 541       49.45    -84.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     I1X A  601                                                       
REMARK 610     I1X B  601                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7QYN   RELATED DB: PDB                                   
REMARK 900 7QYN CONTAINS THE NON-INHIBITED PROTEIN IN COMPLEX WITH THE SAME     
REMARK 900 REACTIVATOR                                                          
REMARK 900 RELATED ID: 7R0A   RELATED DB: PDB                                   
REMARK 900 7R0A CONTAINS THE SAME PROTEIN, ALBEIT SARIN-INHIBITED, IN COMPLEX   
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)       
REMARK 900 PENTYL)PYRIDINIUM                                                    
REMARK 900 RELATED ID: 7R2F   RELATED DB: PDB                                   
REMARK 900 7R2F CONTAINS THE SAME PROTEIN, ALBEIT TABUN-INHIBITED, IN COMPLEX   
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)       
REMARK 900 PENTYL)PYRIDINIUM                                                    
REMARK 900 RELATED ID: 7R3C   RELATED DB: PDB                                   
REMARK 900 7R3C CONTAINS THE SAME PROTEIN, ALBEIT VX-INHIBITED, IN COMPLEX      
REMARK 900 WITH 2-((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)       
REMARK 900 PENTYL)PYRIDINIUM                                                    
REMARK 900 RELATED ID: 7R02   RELATED DB: PDB                                   
REMARK 900 7R02 CONTAINS THE NON-INHIBITED PROTEIN IN COMPLEX WITH N-(3-        
REMARK 900 (DIETHYLAMINO)PROPYL)-4-METHYL-3-NITROBENZAMIDE                      
DBREF  7R4E A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  7R4E 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 RVX 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 RVX 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 7R4E RVX A  203  SER  MODIFIED RESIDUE                                   
MODRES 7R4E RVX B  203  SER  MODIFIED RESIDUE                                   
HET    RVX  A 203      14                                                       
HET    RVX  B 203      14                                                       
HET    I1X  A 601      16                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    PG0  A 604       8                                                       
HET    PG0  A 605       8                                                       
HET    TOE  A 606      11                                                       
HET    TOE  A 607      11                                                       
HET    P15  A 608      20                                                       
HET    I1X  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    PG0  B 604       8                                                       
HET    PG0  B 605       8                                                       
HET    PG0  B 606       8                                                       
HET    TOE  B 607      11                                                       
HETNAM     RVX O-[METHYL(2-METHYLPROPOXY)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  RVX    2(C8 H18 N O5 P)                                             
FORMUL   3  I1X    2(C19 H23 N4 O4 1+)                                          
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   6  PG0    5(C5 H12 O3)                                                 
FORMUL   8  TOE    3(C7 H16 O4)                                                 
FORMUL  10  P15    C13 H28 O7                                                   
FORMUL  18  HOH   *121(H2 O)                                                    
HELIX    1 AA1 VAL A   42  ARG A   46  5                                   5    
HELIX    2 AA2 PHE A   80  MET A   85  1                                   6    
HELIX    3 AA3 LEU A  130  ASP A  134  5                                   5    
HELIX    4 AA4 GLY A  135  GLY A  143  1                                   9    
HELIX    5 AA5 VAL A  153  LEU A  159  1                                   7    
HELIX    6 AA6 ASN A  170  ILE A  187  1                                  18    
HELIX    7 AA7 ALA A  188  PHE A  190  5                                   3    
HELIX    8 AA8 RVX A  203  SER A  215  1                                  13    
HELIX    9 AA9 LEU A  216  LEU A  221  5                                   6    
HELIX   10 AB1 ALA A  241  VAL A  255  1                                  15    
HELIX   11 AB2 ASP A  266  THR A  275  1                                  10    
HELIX   12 AB3 PRO A  277  TRP A  286  1                                  10    
HELIX   13 AB4 HIS A  287  LEU A  289  5                                   3    
HELIX   14 AB5 THR A  311  GLY A  319  1                                   9    
HELIX   15 AB6 GLY A  335  VAL A  340  1                                   6    
HELIX   16 AB7 SER A  355  VAL A  367  1                                  13    
HELIX   17 AB8 SER A  371  THR A  383  1                                  13    
HELIX   18 AB9 ASP A  390  VAL A  407  1                                  18    
HELIX   19 AC1 VAL A  407  GLN A  421  1                                  15    
HELIX   20 AC2 PRO A  440  GLY A  444  5                                   5    
HELIX   21 AC3 GLU A  450  GLY A  456  1                                   7    
HELIX   22 AC4 LEU A  457  ASN A  464  5                                   8    
HELIX   23 AC5 THR A  466  GLY A  487  1                                  22    
HELIX   24 AC6 ARG A  525  ARG A  534  1                                  10    
HELIX   25 AC7 ARG A  534  ALA A  542  1                                   9    
HELIX   26 AC8 ASP B    5  GLN B    7  5                                   3    
HELIX   27 AC9 VAL B   42  ARG B   46  5                                   5    
HELIX   28 AD1 PHE B   80  MET B   85  1                                   6    
HELIX   29 AD2 LEU B  130  ASP B  134  5                                   5    
HELIX   30 AD3 GLY B  135  GLY B  143  1                                   9    
HELIX   31 AD4 GLY B  154  LEU B  159  1                                   6    
HELIX   32 AD5 ASN B  170  ILE B  187  1                                  18    
HELIX   33 AD6 ALA B  188  PHE B  190  5                                   3    
HELIX   34 AD7 RVX B  203  LEU B  214  1                                  12    
HELIX   35 AD8 SER B  215  PHE B  222  5                                   8    
HELIX   36 AD9 ALA B  241  LEU B  254  1                                  14    
HELIX   37 AE1 ASP B  266  THR B  275  1                                  10    
HELIX   38 AE2 PRO B  277  ASP B  283  1                                   7    
HELIX   39 AE3 HIS B  284  VAL B  288  5                                   5    
HELIX   40 AE4 THR B  311  GLY B  319  1                                   9    
HELIX   41 AE5 SER B  336  GLY B  342  5                                   7    
HELIX   42 AE6 SER B  355  VAL B  367  1                                  13    
HELIX   43 AE7 SER B  371  THR B  383  1                                  13    
HELIX   44 AE8 ASP B  390  VAL B  407  1                                  18    
HELIX   45 AE9 VAL B  407  GLN B  421  1                                  15    
HELIX   46 AF1 PRO B  440  GLY B  444  5                                   5    
HELIX   47 AF2 GLU B  450  PHE B  455  1                                   6    
HELIX   48 AF3 GLY B  456  ASN B  464  5                                   9    
HELIX   49 AF4 THR B  466  GLY B  487  1                                  22    
HELIX   50 AF5 ARG B  525  SER B  541  1                                  17    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
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  TRP A 117   O  VAL A 147           
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  GLN A 228   N  GLY A 201           
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 VAL A 520  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A 239  SER A 240  0                                        
SHEET    2 AA3 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
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  GLY B  27   N  ALA B  24           
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  LEU B 115   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  PHE B 430   N  VAL B 330           
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           
SHEET    1 AA7 2 VAL B 239  SER B 240  0                                        
SHEET    2 AA7 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  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  2.08  
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  2.08  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.08  
LINK         C   GLU A 202                 N   RVX A 203     1555   1555  1.33  
LINK         C   RVX A 203                 N   ALA A 204     1555   1555  1.33  
LINK         ND2 ASN A 350                 C1  NAG A 602     1555   1555  1.46  
LINK         ND2 ASN A 464                 C1  NAG A 603     1555   1555  1.47  
LINK         C   GLU B 202                 N   RVX B 203     1555   1555  1.33  
LINK         C   RVX B 203                 N   ALA B 204     1555   1555  1.33  
LINK         ND2 ASN B 350                 C1  NAG B 602     1555   1555  1.47  
LINK         ND2 ASN B 464                 C1  NAG B 603     1555   1555  1.45  
CISPEP   1 TYR A  105    PRO A  106          0        -7.30                     
CISPEP   2 TYR B  105    PRO B  106          0         9.31                     
CISPEP   3 CYS B  257    PRO B  258          0         7.09                     
CRYST1   78.956  110.997  227.549  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      0.012665  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004395        0.00000                         
TER    4218      THR A 543                                                      
TER    8405      ALA B 542                                                      
MASTER      579    0   17   50   34    0    0    6 8645    2  227   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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer