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LongText Report for: 6wv1-pdb

Name Class
6wv1-pdb
HEADER    HYDROLASE                               05-MAY-20   6WV1              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE    2 WITH GB AND HI-6                                                     
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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    NERVE AGENT, ACETYLCHOLINESTERASE, TABUN, GA, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.MCGUIRE,S.M.BESTER,S.D.PEGAN,J.J.HEIGHT                           
REVDAT   1   17-FEB-21 6WV1    0                                                
JRNL        AUTH   J.R.MCGUIRE,S.M.BESTER,M.A.GUELTA,J.CHEUNG,C.LANGLEY,        
JRNL        AUTH 2 M.D.WINEMILLER,S.Y.BAE,V.FUNK,J.M.MYSLINSKI,S.D.PEGAN,       
JRNL        AUTH 3 J.J.HEIGHT                                                   
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO THE INHIBITION OF   
JRNL        TITL 2 HUMAN ACETYLCHOLINESTERASE BY G-SERIES NERVE AGENTS AND      
JRNL        TITL 3 SUBSEQUENT REACTIVATION BY HI-6.                             
JRNL        REF    CHEM.RES.TOXICOL.                          2021              
JRNL        REFN                   ISSN 0893-228X                               
JRNL        PMID   33538594                                                     
JRNL        DOI    10.1021/ACS.CHEMRESTOX.0C00406                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1-3660                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 83046                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4141                            
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 37.0150 -  7.3519    0.95     2737   153  0.1794 0.1899        
REMARK   3     2  7.3519 -  5.8429    0.98     2695   144  0.1815 0.2106        
REMARK   3     3  5.8429 -  5.1065    0.99     2672   170  0.1652 0.2067        
REMARK   3     4  5.1065 -  4.6405    1.00     2688   130  0.1397 0.1383        
REMARK   3     5  4.6405 -  4.3085    0.99     2657   135  0.1296 0.1552        
REMARK   3     6  4.3085 -  4.0548    0.99     2650   154  0.1404 0.1822        
REMARK   3     7  4.0548 -  3.8519    0.99     2643   132  0.1413 0.1770        
REMARK   3     8  3.8519 -  3.6844    0.99     2681   124  0.1482 0.1607        
REMARK   3     9  3.6844 -  3.5427    1.00     2633   121  0.1574 0.1890        
REMARK   3    10  3.5427 -  3.4205    0.99     2656   137  0.1642 0.2120        
REMARK   3    11  3.4205 -  3.3136    1.00     2638   150  0.1675 0.1960        
REMARK   3    12  3.3136 -  3.2190    1.00     2587   157  0.1734 0.2093        
REMARK   3    13  3.2190 -  3.1343    1.00     2624   145  0.1805 0.2267        
REMARK   3    14  3.1343 -  3.0578    1.00     2590   137  0.1701 0.1894        
REMARK   3    15  3.0578 -  2.9884    1.00     2633   136  0.1653 0.2042        
REMARK   3    16  2.9884 -  2.9248    1.00     2667   139  0.1672 0.2078        
REMARK   3    17  2.9248 -  2.8663    1.00     2640   105  0.1748 0.1951        
REMARK   3    18  2.8663 -  2.8122    1.00     2626   118  0.1824 0.2175        
REMARK   3    19  2.8122 -  2.7620    1.00     2582   163  0.1799 0.2492        
REMARK   3    20  2.7620 -  2.7152    1.00     2668   154  0.1826 0.2255        
REMARK   3    21  2.7152 -  2.6714    1.00     2545   117  0.1913 0.2228        
REMARK   3    22  2.6714 -  2.6304    1.00     2643   158  0.1917 0.2322        
REMARK   3    23  2.6304 -  2.5917    1.00     2608   126  0.1900 0.2625        
REMARK   3    24  2.5917 -  2.5552    1.00     2567   156  0.1928 0.2440        
REMARK   3    25  2.5552 -  2.5207    1.00     2633   143  0.2029 0.2537        
REMARK   3    26  2.5207 -  2.4879    1.00     2560   126  0.1996 0.2670        
REMARK   3    27  2.4879 -  2.4568    1.00     2689   101  0.2083 0.2768        
REMARK   3    28  2.4568 -  2.4272    1.00     2586   158  0.2156 0.2415        
REMARK   3    29  2.4272 -  2.3990    1.00     2634   120  0.2180 0.2685        
REMARK   3    30  2.3990 -  2.3721    0.96     2473   132  0.2272 0.2843        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.03                          
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      :  0.005           8851                                  
REMARK   3   ANGLE     :  0.766          12115                                  
REMARK   3   CHIRALITY :  0.048           1298                                  
REMARK   3   PLANARITY :  0.006           1592                                  
REMARK   3   DIHEDRAL  :  4.252           7003                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 288 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 126.2345  23.2066  28.3107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2463 T22:   0.5812                                     
REMARK   3      T33:   0.4313 T12:   0.0598                                     
REMARK   3      T13:  -0.0169 T23:   0.0574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1615 L22:   3.1338                                     
REMARK   3      L33:   3.3719 L12:   2.4002                                     
REMARK   3      L13:   0.8426 L23:  -0.4794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0772 S12:   0.0960 S13:   0.0276                       
REMARK   3      S21:  -0.3577 S22:  -0.3486 S23:  -0.0988                       
REMARK   3      S31:   0.0942 S32:   0.7833 S33:   0.2243                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 289 THROUGH 341 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 106.4092  36.6867  21.9355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3162 T22:   0.5189                                     
REMARK   3      T33:   0.3032 T12:  -0.0264                                     
REMARK   3      T13:  -0.0415 T23:  -0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5157 L22:   2.5785                                     
REMARK   3      L33:   2.3492 L12:  -1.4193                                     
REMARK   3      L13:  -0.6781 L23:  -0.1649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2075 S12:   0.2983 S13:  -0.0527                       
REMARK   3      S21:  -0.0230 S22:  -0.2697 S23:  -0.1600                       
REMARK   3      S31:  -0.0461 S32:   0.1120 S33:   0.0481                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 116.6924  52.5243  11.7972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4082 T22:   0.4876                                     
REMARK   3      T33:   0.3554 T12:  -0.1282                                     
REMARK   3      T13:  -0.0166 T23:   0.1267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2638 L22:   1.5917                                     
REMARK   3      L33:   3.5841 L12:   0.2400                                     
REMARK   3      L13:   0.6959 L23:  -0.2157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0400 S12:  -0.0704 S13:   0.0489                       
REMARK   3      S21:   0.0127 S22:  -0.1660 S23:  -0.3820                       
REMARK   3      S31:  -0.6328 S32:   0.6354 S33:   0.0984                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 466 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 103.8312  50.4828  30.7716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3944 T22:   0.3285                                     
REMARK   3      T33:   0.3266 T12:  -0.0702                                     
REMARK   3      T13:  -0.0129 T23:   0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7640 L22:   0.9984                                     
REMARK   3      L33:   3.5467 L12:  -0.3380                                     
REMARK   3      L13:  -1.3378 L23:  -0.2699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1375 S12:   0.0842 S13:   0.3436                       
REMARK   3      S21:   0.1616 S22:  -0.1034 S23:  -0.0341                       
REMARK   3      S31:  -0.7125 S32:   0.4125 S33:  -0.0339                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  91.7609  51.5437  33.0154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2655 T22:   0.3197                                     
REMARK   3      T33:   0.2892 T12:   0.0432                                     
REMARK   3      T13:   0.0121 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5178 L22:   2.3904                                     
REMARK   3      L33:   5.4224 L12:  -0.5583                                     
REMARK   3      L13:   0.3698 L23:  -0.0134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.0949 S13:   0.2702                       
REMARK   3      S21:   0.0989 S22:  -0.0473 S23:   0.1854                       
REMARK   3      S31:  -0.6115 S32:  -0.5977 S33:   0.0088                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 100.2896  48.9342  14.3672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3776 T22:   0.3634                                     
REMARK   3      T33:   0.3188 T12:   0.0256                                     
REMARK   3      T13:  -0.0270 T23:   0.0797                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5032 L22:   0.2233                                     
REMARK   3      L33:   3.9942 L12:   0.5770                                     
REMARK   3      L13:  -0.3694 L23:  -0.2093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1183 S12:   0.2642 S13:   0.2739                       
REMARK   3      S21:  -0.0806 S22:   0.0347 S23:   0.0718                       
REMARK   3      S31:  -0.3498 S32:  -0.1185 S33:   0.0557                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  65.9370  37.2131  45.6943              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3984 T22:   0.3792                                     
REMARK   3      T33:   0.2743 T12:  -0.0145                                     
REMARK   3      T13:  -0.0995 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1031 L22:   2.3928                                     
REMARK   3      L33:   4.0523 L12:   0.9763                                     
REMARK   3      L13:  -0.4612 L23:  -0.0208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1147 S12:  -0.2371 S13:   0.0169                       
REMARK   3      S21:   0.2767 S22:   0.0339 S23:  -0.3328                       
REMARK   3      S31:  -0.6900 S32:   0.2944 S33:  -0.1440                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 237 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5774  33.2408  34.2901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2140 T22:   0.3606                                     
REMARK   3      T33:   0.2417 T12:   0.0121                                     
REMARK   3      T13:  -0.0332 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0727 L22:   1.8495                                     
REMARK   3      L33:   3.3415 L12:   0.3357                                     
REMARK   3      L13:   0.9294 L23:  -0.0505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0839 S12:  -0.0915 S13:  -0.0288                       
REMARK   3      S21:   0.0503 S22:   0.0875 S23:  -0.0360                       
REMARK   3      S31:  -0.2665 S32:  -0.0066 S33:  -0.0251                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1594  17.3977  33.3145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2636 T22:   0.6110                                     
REMARK   3      T33:   0.3996 T12:  -0.0594                                     
REMARK   3      T13:  -0.0265 T23:   0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0514 L22:   2.4531                                     
REMARK   3      L33:   3.2421 L12:   0.1526                                     
REMARK   3      L13:   0.7843 L23:  -0.6996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0348 S12:  -0.0354 S13:  -0.3121                       
REMARK   3      S21:  -0.0934 S22:   0.0118 S23:   0.0863                       
REMARK   3      S31:   0.4664 S32:  -0.9343 S33:   0.0123                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 341 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0046  34.5595  19.3717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3474 T22:   0.5250                                     
REMARK   3      T33:   0.3730 T12:   0.0221                                     
REMARK   3      T13:  -0.1260 T23:   0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8239 L22:   1.0368                                     
REMARK   3      L33:   2.2064 L12:   1.3502                                     
REMARK   3      L13:   0.0020 L23:   0.0289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1268 S12:   0.0375 S13:   0.1673                       
REMARK   3      S21:  -0.0166 S22:   0.1611 S23:   0.1652                       
REMARK   3      S31:  -0.2087 S32:  -0.2982 S33:  -0.0683                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 366 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  52.7773  10.3314   8.7263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5584 T22:   0.4757                                     
REMARK   3      T33:   0.4481 T12:   0.1205                                     
REMARK   3      T13:  -0.0925 T23:  -0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1174 L22:   2.0831                                     
REMARK   3      L33:   3.2284 L12:   0.4380                                     
REMARK   3      L13:   1.8056 L23:   0.2564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2989 S12:  -0.3135 S13:  -0.6615                       
REMARK   3      S21:   0.3736 S22:   0.2110 S23:  -0.5445                       
REMARK   3      S31:   0.6342 S32:   0.4629 S33:  -0.3829                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 367 THROUGH 406 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.1017  18.0501   2.9588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3739 T22:   0.4529                                     
REMARK   3      T33:   0.3090 T12:   0.0581                                     
REMARK   3      T13:  -0.0722 T23:  -0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2435 L22:   1.8914                                     
REMARK   3      L33:   3.5891 L12:  -0.1942                                     
REMARK   3      L13:  -0.0134 L23:   1.1340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1500 S12:  -0.0124 S13:  -0.1344                       
REMARK   3      S21:   0.0010 S22:  -0.1106 S23:  -0.1248                       
REMARK   3      S31:   0.2414 S32:   0.2924 S33:  -0.1275                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 466 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  62.9713  30.7267  16.3689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3465 T22:   0.5943                                     
REMARK   3      T33:   0.3299 T12:  -0.0817                                     
REMARK   3      T13:  -0.0293 T23:  -0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8636 L22:   1.8609                                     
REMARK   3      L33:   1.6000 L12:   0.2374                                     
REMARK   3      L13:   0.0043 L23:   0.3552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0694 S12:   0.1055 S13:  -0.2385                       
REMARK   3      S21:  -0.1948 S22:   0.2149 S23:  -0.2267                       
REMARK   3      S31:  -0.0688 S32:   0.4329 S33:  -0.1035                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6921  41.9826  14.1274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4892 T22:   0.5953                                     
REMARK   3      T33:   0.4217 T12:  -0.2650                                     
REMARK   3      T13:  -0.0435 T23:   0.0686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0567 L22:   1.4741                                     
REMARK   3      L33:   2.4463 L12:  -0.8880                                     
REMARK   3      L13:   1.6361 L23:  -0.3998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1962 S12:   0.5763 S13:   0.4268                       
REMARK   3      S21:  -0.0922 S22:  -0.0074 S23:  -0.3123                       
REMARK   3      S31:  -0.5922 S32:   0.6481 S33:   0.0960                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9826  32.3478   5.0155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3702 T22:   0.5148                                     
REMARK   3      T33:   0.2302 T12:  -0.0696                                     
REMARK   3      T13:  -0.0371 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5787 L22:   2.3007                                     
REMARK   3      L33:   2.1607 L12:   0.8093                                     
REMARK   3      L13:   1.4875 L23:   0.7235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2091 S12:  -0.3152 S13:  -0.0872                       
REMARK   3      S21:  -0.1839 S22:  -0.2307 S23:  -0.0497                       
REMARK   3      S31:  -0.3605 S32:   0.3510 S33:   0.0152                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 104.9210  31.3406  53.8321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3582 T22:   0.3763                                     
REMARK   3      T33:   0.3109 T12:  -0.1338                                     
REMARK   3      T13:  -0.0224 T23:   0.0555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8306 L22:   3.3734                                     
REMARK   3      L33:   1.9740 L12:  -1.4530                                     
REMARK   3      L13:  -0.6876 L23:   0.7336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0830 S12:  -0.2968 S13:  -0.1042                       
REMARK   3      S21:   0.6712 S22:  -0.0297 S23:  -0.0455                       
REMARK   3      S31:   0.2054 S32:   0.0601 S33:   0.1068                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 110.9922  34.1095  44.0319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2779 T22:   0.3996                                     
REMARK   3      T33:   0.3057 T12:  -0.1337                                     
REMARK   3      T13:  -0.0354 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0995 L22:   1.6399                                     
REMARK   3      L33:   2.0062 L12:  -0.2532                                     
REMARK   3      L13:  -0.2124 L23:  -0.0915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0236 S12:  -0.1263 S13:   0.0321                       
REMARK   3      S21:   0.2968 S22:  -0.0837 S23:  -0.2378                       
REMARK   3      S31:  -0.1732 S32:   0.4849 S33:   0.0485                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 108.8270  33.4400  37.1745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2270 T22:   0.3365                                     
REMARK   3      T33:   0.3274 T12:  -0.1027                                     
REMARK   3      T13:  -0.0045 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8366 L22:   1.7887                                     
REMARK   3      L33:   2.3661 L12:  -1.7285                                     
REMARK   3      L13:  -0.8866 L23:   1.1700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0395 S12:  -0.0273 S13:   0.0032                       
REMARK   3      S21:   0.2297 S22:  -0.0335 S23:  -0.0566                       
REMARK   3      S31:   0.0968 S32:   0.1554 S33:  -0.0186                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 103.6035  30.1270  31.1112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2067 T22:   0.3224                                     
REMARK   3      T33:   0.3441 T12:  -0.0915                                     
REMARK   3      T13:  -0.0157 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5367 L22:   1.1184                                     
REMARK   3      L33:   2.2127 L12:  -0.6269                                     
REMARK   3      L13:   0.2398 L23:  -0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0944 S12:   0.1571 S13:  -0.1125                       
REMARK   3      S21:   0.0048 S22:  -0.1171 S23:   0.1569                       
REMARK   3      S31:   0.1075 S32:  -0.1055 S33:   0.0234                       
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 6WV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000249039.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83198                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.370                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.17.1-3660                                    
REMARK 200 STARTING MODEL: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, KNO3, PH 7.0, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.92000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      215.84000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      215.84000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      107.92000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000       52.09150            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000      -90.22512            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     2                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     THR B   543                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B   203     P1   UCJ B   604              1.12            
REMARK 500   OG   SER A   203     P1   UCJ A   607              1.30            
REMARK 500   ND2  ASN A   265     C1   NAG A   604              1.64            
REMARK 500   OG   SER B   203     O1   UCJ B   604              1.70            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU B 285   O   -  C   -  N   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    GLU B 285   O   -  C   -  N   ANGL. DEV. = -17.9 DEGREES          
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       -2.26     69.83                                   
REMARK 500    ALA A  62       68.13   -100.58                                   
REMARK 500    ALA A 167       73.70   -151.82                                   
REMARK 500    SER A 203     -126.84     58.04                                   
REMARK 500    ASP A 306      -81.75    -94.72                                   
REMARK 500    VAL A 407      -64.17   -124.20                                   
REMARK 500    ASN A 464       50.46    -97.28                                   
REMARK 500    ASP A 514     -167.17   -160.04                                   
REMARK 500    PHE B  47       -3.98     78.90                                   
REMARK 500    ALA B  62       50.46   -111.73                                   
REMARK 500    TYR B  77       79.65   -113.80                                   
REMARK 500    SER B 203     -129.44     55.58                                   
REMARK 500    ASP B 306      -86.66   -103.49                                   
REMARK 500    VAL B 407      -61.42   -128.49                                   
REMARK 500    ASP B 514     -159.45   -158.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU B 285         29.47                                           
REMARK 500    GLU B 285         29.23                                           
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     NAG A  604                                                       
REMARK 610     UCJ A  607                                                       
REMARK 610     UCJ B  604                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6WUV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6WUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6WUZ   RELATED DB: PDB                                   
DBREF  6WV1 A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  6WV1 B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUC  C   3      10                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    FUC  D   3      10                                                       
HET    NAG  A 604      14                                                       
HET    7PE  A 605      21                                                       
HET    NAG  A 606      14                                                       
HET    UCJ  A 607       7                                                       
HET    HI6  A 608      21                                                       
HET    UCJ  B 604       7                                                       
HET    HI6  B 605      42                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)              
HETNAM   2 7PE  ETHOXY)ETHANOL                                                  
HETNAM     UCJ PROPAN-2-YL HYDROGEN (S)-METHYLPHOSPHONATE                       
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
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     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
HETSYN     7PE POLYETHYLENE GLYCOL FRAGMENT                                     
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   6  7PE    C14 H30 O7                                                   
FORMUL   8  UCJ    2(C4 H11 O3 P)                                               
FORMUL   9  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL  12  HOH   *413(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET 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  ARG A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  LEU A  214  1                                  12    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 MET A  241  GLY A  256  1                                  16    
HELIX   12 AB3 ASN A  265  THR A  275  1                                  11    
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  ALA A  318  1                                   8    
HELIX   16 AB7 GLY A  335  GLY A  342  5                                   8    
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  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  PHE A  535  1                                  11    
HELIX   26 AC8 PHE A  535  ALA A  542  1                                   8    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET 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  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 MET B  241  VAL B  255  1                                  15    
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10    
HELIX   39 AE3 PRO B  277  GLU B  285  1                                   9    
HELIX   40 AE4 TRP B  286  LEU B  289  5                                   4    
HELIX   41 AE5 THR B  311  ALA B  318  1                                   8    
HELIX   42 AE6 GLY B  335  GLY B  342  5                                   8    
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  ASP B  460  5                                   5    
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 PHE B  535  ALA B  542  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  VAL A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  LEU A  22  0                                        
SHEET    2 AA211 VAL A  29  PRO A  36 -1  O  ALA A  31   N  ILE A  20           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
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  THR A 198   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  ARG A 224   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  TYR A 426   N  VAL A 328           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL 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 2 VAL A 239  GLY A 240  0                                        
SHEET    2 AA4 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA5 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA611 ILE B  20  THR B  24  0                                        
SHEET    2 AA611 GLY B  27  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30           
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA611 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA7 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA8 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA8 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  2.05  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.05  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.05  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.02  
LINK         ND2 ASN A 350                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN A 464                 C1  NAG A 606     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG D   1     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O6  NAG C   1                 C1  FUC C   3     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.46  
LINK         O6  NAG D   1                 C1  FUC D   3     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0         4.02                     
CISPEP   2 CYS A  257    PRO A  258          0        -4.16                     
CISPEP   3 TYR B  105    PRO B  106          0         0.46                     
CISPEP   4 PRO B  258    PRO B  259          0       -12.86                     
CRYST1  104.183  104.183  323.760  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009598  0.005542  0.000000        0.00000                         
SCALE2      0.000000  0.011083  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003089        0.00000                         
TER    4184      ALA A 542                                                      
TER    8366      ALA B 542                                                      
MASTER      640    0   13   52   36    0    0    6 8859    2  217   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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