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LongText Report for: 4BTL-pdb

Name Class
4BTL-pdb
HEADER    HYDROLASE                               18-JUN-13   4BTL              
TITLE     AROMATIC INTERACTIONS IN ACETYLCHOLINESTERASE-INHIBITOR COMPLEXES     
CAVEAT     4BTL    NAG A 1544 HAS WRONG CHIRALITY AT ATOM C1                    
CAVEAT   2 4BTL    NAG B 1548 HAS WRONG CHIRALITY AT ATOM C1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    ACETYLCHOLINESTERASE, HYDROLASE, INHIBITOR                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,W.QIAN,C.ENGDAHL,      
AUTHOR   2 L.BERG,F.EKSTROM,A.LINUSSON                                          
REVDAT   1   11-SEP-13 4BTL    0                                                
JRNL        AUTH   C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,       
JRNL        AUTH 2 C.ENGDAHL,W.QIAN,F.J.EKSTROM,A.LINUSSON                      
JRNL        TITL   DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY   
JRNL        TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS.                     
JRNL        REF    J.MED.CHEM.                                2013              
JRNL        REFN                   ESSN 1520-4804                               
JRNL        PMID   23984975                                                     
JRNL        DOI    10.1021/JM400990P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.500                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.813                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.86                          
REMARK   3   NUMBER OF REFLECTIONS             : 68722                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1916                          
REMARK   3   R VALUE            (WORKING SET) : 0.1908                          
REMARK   3   FREE R VALUE                     : 0.2316                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1384                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.8148 -  5.3756    0.99     7093   140  0.1712 0.1988        
REMARK   3     2  5.3756 -  4.2712    0.99     6816   131  0.1440 0.1559        
REMARK   3     3  4.2712 -  3.7326    0.98     6724   133  0.1581 0.2162        
REMARK   3     4  3.7326 -  3.3919    0.99     6730   149  0.1992 0.2435        
REMARK   3     5  3.3919 -  3.1491    0.99     6735   115  0.2231 0.2804        
REMARK   3     6  3.1491 -  2.9637    0.99     6678   154  0.2235 0.2672        
REMARK   3     7  2.9637 -  2.8154    0.99     6640   136  0.2279 0.2714        
REMARK   3     8  2.8154 -  2.6929    0.99     6678   131  0.2601 0.3000        
REMARK   3     9  2.6929 -  2.5893    0.99     6636   149  0.2620 0.3242        
REMARK   3    10  2.5893 -  2.5000    0.99     6608   146  0.2818 0.3357        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.310                                         
REMARK   3   B_SOL              : 40.932                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.37             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.77            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.4814                                               
REMARK   3    B22 (A**2) : 14.3665                                              
REMARK   3    B33 (A**2) : -17.8480                                             
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           8896                                  
REMARK   3   ANGLE     :  1.094          12115                                  
REMARK   3   CHIRALITY :  0.077           1287                                  
REMARK   3   PLANARITY :  0.005           1576                                  
REMARK   3   DIHEDRAL  : 16.667           3284                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6863  12.8063  41.3651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3575 T22:   0.4322                                     
REMARK   3      T33:   0.2012 T12:  -0.0103                                     
REMARK   3      T13:  -0.0276 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3564 L22:   2.0142                                     
REMARK   3      L33:   4.4758 L12:  -1.0457                                     
REMARK   3      L13:   0.0256 L23:  -0.5539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1963 S12:  -0.1974 S13:   0.1523                       
REMARK   3      S21:   0.4640 S22:   0.1863 S23:   0.0426                       
REMARK   3      S31:   0.0118 S32:  -0.3499 S33:  -0.0156                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 46:111)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2376  17.4367  29.1879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3160 T22:   0.5378                                     
REMARK   3      T33:   0.0865 T12:  -0.0161                                     
REMARK   3      T13:  -0.0427 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6208 L22:   0.8516                                     
REMARK   3      L33:   1.8128 L12:  -0.1488                                     
REMARK   3      L13:  -0.0442 L23:  -0.2425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1776 S12:  -0.6056 S13:   0.2855                       
REMARK   3      S21:   0.2392 S22:   0.1372 S23:  -0.2683                       
REMARK   3      S31:  -0.0088 S32:   0.0108 S33:   0.0387                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 112:190)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6803   9.1452  25.3053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2952 T22:   0.3500                                     
REMARK   3      T33:   0.1915 T12:   0.0105                                     
REMARK   3      T13:  -0.0729 T23:   0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1202 L22:   1.5108                                     
REMARK   3      L33:   4.5819 L12:  -0.0705                                     
REMARK   3      L13:  -0.9803 L23:  -0.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0502 S12:  -0.1429 S13:  -0.1237                       
REMARK   3      S21:   0.2306 S22:   0.0164 S23:  -0.1082                       
REMARK   3      S31:   0.2384 S32:   0.0222 S33:   0.0388                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 191:240)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5687   2.3017  18.2060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2836 T22:   0.2572                                     
REMARK   3      T33:   0.1420 T12:  -0.0193                                     
REMARK   3      T13:  -0.0318 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9208 L22:   1.4543                                     
REMARK   3      L33:   6.1995 L12:   0.1204                                     
REMARK   3      L13:  -1.9955 L23:  -0.6911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0358 S12:  -0.2937 S13:  -0.1578                       
REMARK   3      S21:   0.1265 S22:   0.0662 S23:   0.0147                       
REMARK   3      S31:   0.4601 S32:  -0.4187 S33:  -0.0129                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 241:275)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  53.6590  13.0302  11.9151              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2807 T22:   0.7831                                     
REMARK   3      T33:   0.2718 T12:   0.0627                                     
REMARK   3      T13:   0.0270 T23:   0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1921 L22:   1.3581                                     
REMARK   3      L33:   6.0583 L12:   1.1728                                     
REMARK   3      L13:   5.0293 L23:   1.5596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1829 S12:   0.3811 S13:  -0.0458                       
REMARK   3      S21:  -0.2684 S22:  -0.1169 S23:  -0.3160                       
REMARK   3      S31:  -0.2438 S32:   1.0155 S33:   0.2767                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 276:318)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0237  11.1903   9.2738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2542 T22:   0.5354                                     
REMARK   3      T33:   0.2114 T12:   0.0905                                     
REMARK   3      T13:   0.0210 T23:   0.0393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8894 L22:   5.3397                                     
REMARK   3      L33:   3.4607 L12:   2.0110                                     
REMARK   3      L13:   1.0023 L23:   0.9542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:   0.2888 S13:  -0.0627                       
REMARK   3      S21:   0.2849 S22:   0.0011 S23:  -0.3040                       
REMARK   3      S31:   0.1971 S32:   0.3429 S33:  -0.0102                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 319:366)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8358  17.7976   2.7978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1415 T22:   0.3255                                     
REMARK   3      T33:   0.1702 T12:  -0.0412                                     
REMARK   3      T13:  -0.0020 T23:   0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7804 L22:   5.3657                                     
REMARK   3      L33:   4.0594 L12:   0.9321                                     
REMARK   3      L13:  -0.7861 L23:  -2.0643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0719 S12:   0.3593 S13:   0.0407                       
REMARK   3      S21:   0.0632 S22:  -0.0150 S23:   0.0207                       
REMARK   3      S31:  -0.0323 S32:  -0.2159 S33:   0.0966                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 367:406)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9058  17.7599  -8.4540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2910 T22:   0.5722                                     
REMARK   3      T33:   0.1769 T12:  -0.0384                                     
REMARK   3      T13:   0.0005 T23:   0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3497 L22:   4.4892                                     
REMARK   3      L33:   2.1751 L12:  -2.1991                                     
REMARK   3      L13:  -0.0237 L23:   0.2870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1964 S12:   0.5959 S13:   0.1494                       
REMARK   3      S21:  -0.3755 S22:  -0.1841 S23:   0.1124                       
REMARK   3      S31:   0.1995 S32:   0.0823 S33:  -0.0483                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 407:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2744  13.6266  16.1449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2162 T22:   0.5877                                     
REMARK   3      T33:   0.1996 T12:  -0.0312                                     
REMARK   3      T13:  -0.0143 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6117 L22:   3.8991                                     
REMARK   3      L33:   2.9673 L12:   0.2352                                     
REMARK   3      L13:   0.2520 L23:   0.9212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0319 S12:   0.0960 S13:   0.0387                       
REMARK   3      S21:   0.0343 S22:   0.0502 S23:   0.3303                       
REMARK   3      S31:   0.0822 S32:  -0.7082 S33:  -0.0200                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9515   1.0249  13.4346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3491 T22:   0.8708                                     
REMARK   3      T33:   0.4386 T12:  -0.2109                                     
REMARK   3      T13:   0.0054 T23:   0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8904 L22:   8.5862                                     
REMARK   3      L33:   2.2005 L12:  -1.2593                                     
REMARK   3      L13:  -1.3768 L23:  -1.0978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1928 S12:   0.1179 S13:  -0.8077                       
REMARK   3      S21:   0.1903 S22:  -0.0112 S23:   1.1903                       
REMARK   3      S31:   0.5189 S32:  -1.3949 S33:   0.2081                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6121   6.0928  -1.3185              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3530 T22:   0.9403                                     
REMARK   3      T33:   0.1373 T12:  -0.0390                                     
REMARK   3      T13:  -0.2290 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6128 L22:   1.9024                                     
REMARK   3      L33:   5.7747 L12:  -0.4651                                     
REMARK   3      L13:  -1.5947 L23:   0.9710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0643 S12:  -0.0693 S13:  -0.0767                       
REMARK   3      S21:  -0.5329 S22:  -0.0958 S23:   0.3582                       
REMARK   3      S31:   0.5451 S32:   0.1252 S33:  -0.0078                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7200   6.2561 -61.8018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3883 T22:   0.6680                                     
REMARK   3      T33:   0.2274 T12:   0.0320                                     
REMARK   3      T13:  -0.0840 T23:  -0.1321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5209 L22:   1.9497                                     
REMARK   3      L33:   4.6081 L12:  -0.2451                                     
REMARK   3      L13:   0.6691 L23:  -0.2434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2128 S12:   0.6037 S13:   0.1243                       
REMARK   3      S21:  -0.3903 S22:  -0.1992 S23:   0.2829                       
REMARK   3      S31:  -0.2285 S32:  -0.8365 S33:  -0.0160                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:86)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3722  -4.1337 -53.1468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5816 T22:   0.6655                                     
REMARK   3      T33:   0.2496 T12:  -0.0786                                     
REMARK   3      T13:  -0.0998 T23:  -0.1322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5961 L22:   1.4661                                     
REMARK   3      L33:   2.1416 L12:  -0.4311                                     
REMARK   3      L13:   0.5452 L23:   0.2354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3075 S12:   0.3687 S13:  -0.1366                       
REMARK   3      S21:  -0.1650 S22:  -0.2686 S23:   0.1251                       
REMARK   3      S31:   0.8846 S32:  -0.0882 S33:  -0.1083                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 87:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.1067   4.1348 -51.0720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3406 T22:   0.5852                                     
REMARK   3      T33:   0.1375 T12:   0.0171                                     
REMARK   3      T13:  -0.0656 T23:  -0.0776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4967 L22:   1.3072                                     
REMARK   3      L33:   2.7230 L12:   0.2003                                     
REMARK   3      L13:   0.0504 L23:   0.6660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0471 S12:   0.3549 S13:  -0.1714                       
REMARK   3      S21:  -0.2539 S22:  -0.1392 S23:   0.1503                       
REMARK   3      S31:   0.1874 S32:  -0.1915 S33:   0.0321                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 171:300)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5512   3.0263 -47.4148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3068 T22:   0.5758                                     
REMARK   3      T33:   0.1774 T12:   0.0369                                     
REMARK   3      T13:  -0.0514 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0428 L22:   1.6383                                     
REMARK   3      L33:   3.0652 L12:  -0.3647                                     
REMARK   3      L13:  -0.0236 L23:   0.8992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0819 S12:   0.0437 S13:  -0.0903                       
REMARK   3      S21:  -0.0315 S22:   0.0839 S23:  -0.1370                       
REMARK   3      S31:   0.2902 S32:   0.3901 S33:  -0.1604                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 301:341)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0447  10.6142 -36.8734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2215 T22:   0.4106                                     
REMARK   3      T33:   0.1435 T12:  -0.0578                                     
REMARK   3      T13:  -0.0746 T23:  -0.0560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3490 L22:   2.2175                                     
REMARK   3      L33:   4.9620 L12:  -1.5951                                     
REMARK   3      L13:  -0.5991 L23:  -0.0777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1947 S12:   0.2382 S13:   0.2469                       
REMARK   3      S21:   0.0636 S22:  -0.0659 S23:  -0.2586                       
REMARK   3      S31:  -0.0837 S32:   0.4682 S33:  -0.1375                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 342:406)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2142  -5.3040 -18.5396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6423 T22:   0.4029                                     
REMARK   3      T33:   0.2484 T12:   0.0074                                     
REMARK   3      T13:  -0.1154 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9030 L22:   1.9413                                     
REMARK   3      L33:   5.6079 L12:   1.2148                                     
REMARK   3      L13:   0.6400 L23:   0.2721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2206 S12:  -0.8224 S13:  -0.2722                       
REMARK   3      S21:   0.4139 S22:  -0.0307 S23:  -0.0285                       
REMARK   3      S31:   0.9059 S32:   0.0979 S33:  -0.1577                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 407:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4239   8.3091 -33.3972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2872 T22:   0.5820                                     
REMARK   3      T33:   0.2036 T12:   0.0060                                     
REMARK   3      T13:   0.0012 T23:  -0.0764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1420 L22:   4.2293                                     
REMARK   3      L33:   3.5151 L12:   0.7659                                     
REMARK   3      L13:  -0.2668 L23:   0.3582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0390 S12:  -0.0222 S13:  -0.0369                       
REMARK   3      S21:   0.1103 S22:  -0.0387 S23:   0.2565                       
REMARK   3      S31:   0.1963 S32:  -0.3665 S33:  -0.0072                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9888  22.2256 -28.8968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4229 T22:   0.7462                                     
REMARK   3      T33:   0.3008 T12:   0.0891                                     
REMARK   3      T13:   0.0761 T23:  -0.0491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4287 L22:   7.9371                                     
REMARK   3      L33:   2.6602 L12:   1.4033                                     
REMARK   3      L13:   1.5610 L23:  -2.7497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:  -0.5027 S13:   0.6404                       
REMARK   3      S21:   0.4943 S22:   0.3791 S23:   0.9116                       
REMARK   3      S31:  -0.4337 S32:  -1.0682 S33:  -0.3772                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:543)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2780  11.2396 -21.7828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4628 T22:   0.7597                                     
REMARK   3      T33:  -0.0153 T12:  -0.0568                                     
REMARK   3      T13:  -0.0042 T23:  -0.0572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7041 L22:   1.8700                                     
REMARK   3      L33:   5.2563 L12:   0.1026                                     
REMARK   3      L13:   2.9799 L23:  -0.1108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2122 S12:  -0.1128 S13:  -0.1586                       
REMARK   3      S21:   0.2656 S22:  -0.2214 S23:   0.1544                       
REMARK   3      S31:   0.1765 S32:   0.6188 S33:   0.0823                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 258-264 WERE EXCLUDED FROM THE   
REMARK   3  MODEL DUE TO LACK OF ELECTRON DENSITY.                              
REMARK   4                                                                      
REMARK   4 4BTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57320.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-13                          
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               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9805                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69367                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.05                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 %(W/V) PEG750MME, 0.1 M            
REMARK 280  HEPES PH 7.0-7.1                                                    
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       39.33550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.55600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.41200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.55600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.33550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.41200            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     GLU B 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: 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   O    HOH A  2149     O    HOH A  2152              2.00            
REMARK 500   O    HOH B  2121     O    HOH B  2125              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -4.33     68.63                                   
REMARK 500    CYS A  96        8.22   -156.00                                   
REMARK 500    PHE A 123       14.79     58.31                                   
REMARK 500    ALA A 167       75.75   -157.73                                   
REMARK 500    SER A 203     -122.00     56.33                                   
REMARK 500    ASP A 306      -83.13   -128.58                                   
REMARK 500    SER A 371      173.67    -58.16                                   
REMARK 500    HIS A 387       59.00   -140.17                                   
REMARK 500    VAL A 407      -66.06   -129.60                                   
REMARK 500    LEU A 518      118.32    -39.48                                   
REMARK 500    ARG A 525       51.76     38.91                                   
REMARK 500    PRO B  41       47.66    -75.79                                   
REMARK 500    PRO B  55      153.04    -46.43                                   
REMARK 500    ALA B  62       54.78   -116.11                                   
REMARK 500    PHE B 123       19.92     59.61                                   
REMARK 500    ALA B 167       65.47   -167.18                                   
REMARK 500    SER B 203     -121.02     59.20                                   
REMARK 500    ASP B 306      -83.42   -123.38                                   
REMARK 500    ASP B 323       30.36    -98.42                                   
REMARK 500    VAL B 407      -67.05   -120.10                                   
REMARK 500    LYS B 496      166.70     64.05                                   
REMARK 500    SER B 497      102.50     62.85                                   
REMARK 500    ASN B 514     -166.97   -164.30                                   
REMARK 500    ALA B 542       57.39   -105.94                                   
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     PE3 A 1545                                                       
REMARK 610     PE3 A 1546                                                       
REMARK 610     PE3 A 1550                                                       
REMARK 610     PE3 A 1552                                                       
REMARK 610     PE3 A 1553                                                       
REMARK 610     PE3 B 1545                                                       
REMARK 610     PE3 B 1547                                                       
REMARK 610     PE3 B 1550                                                       
REMARK 610     PE3 B 1551                                                       
REMARK 610     PE3 B 1553                                                       
REMARK 610     PE3 B 1555                                                       
REMARK 610     5GZ A 1549                                                       
REMARK 610     5GZ B 1552                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ B1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1555                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1553                 
DBREF  4BTL A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4BTL 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 SER 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 SER 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                      
HET    5GZ  A1543      28                                                       
HET    NAG  A1544      14                                                       
HET    PE3  A1545       5                                                       
HET    PE3  A1546       7                                                       
HET    NAG  A1547      14                                                       
HET    EDO  A1548       4                                                       
HET    5GZ  A1549      22                                                       
HET    PE3  A1550       4                                                       
HET    EDO  A1551       4                                                       
HET    5GZ  B1544      28                                                       
HET    PE3  B1545       7                                                       
HET    NAG  B1546      14                                                       
HET    PE3  B1547      10                                                       
HET    NAG  B1548      14                                                       
HET    EDO  B1549       4                                                       
HET    PE3  B1550       4                                                       
HET    PE3  B1551       7                                                       
HET    5GZ  B1552      23                                                       
HET    PE3  B1553       7                                                       
HET    EDO  B1554       4                                                       
HET    PE3  B1555      22                                                       
HET    PE3  A1552       7                                                       
HET    PE3  A1553      10                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-                             
HETNAM   2 PE3  TRIDECAOXAHENTETRACONTANE-1,41-DIOL                             
HETNAM     5GZ 4-(2-CHLORO-6-NITROPHENOXY)-N-[2-                                
HETNAM   2 5GZ  (DIETHYLAMINO)ETHYL]BENZENESULFONAMIDE                          
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PE3 POLYETHYLENE GLYCOL                                              
FORMUL   3  EDO    4(C2 H6 O2)                                                  
FORMUL   6  5GZ    4(C18 H22 CL N3 O5 S)                                        
FORMUL   8  PE3    11(C28 H58 O15)                                              
FORMUL   8  NAG    4(C8 H15 N O6)                                               
FORMUL   9  HOH   *318(H2 O)                                                    
HELIX    1   1 VAL A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  GLY A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  ILE A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 SER A  203  SER A  215  1                                  13    
HELIX    9   9 LEU A  216  PHE A  222  5                                   7    
HELIX   10  10 SER A  240  VAL A  255  1                                  16    
HELIX   11  11 ASN A  265  THR A  275  1                                  11    
HELIX   12  12 PRO A  277  HIS A  284  1                                   8    
HELIX   13  13 GLU A  285  LEU A  289  5                                   5    
HELIX   14  14 THR A  311  GLY A  319  1                                   9    
HELIX   15  15 GLY A  335  VAL A  340  1                                   6    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  GLN A  421  1                                  15    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 ASP A  460  ASN A  464  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 PHE A  535  SER A  541  1                                   7    
HELIX   27  27 ASP B    5  GLN B    7  5                                   3    
HELIX   28  28 VAL B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  GLY B  143  1                                   9    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  ILE B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 SER B  203  SER B  215  1                                  13    
HELIX   36  36 SER B  215  SER B  220  1                                   6    
HELIX   37  37 ALA B  241  GLY B  256  1                                  16    
HELIX   38  38 GLY B  264  THR B  275  1                                  12    
HELIX   39  39 PRO B  277  TRP B  286  1                                  10    
HELIX   40  40 HIS B  287  LEU B  289  5                                   3    
HELIX   41  41 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  VAL B  340  1                                   6    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  PHE B  455  1                                   6    
HELIX   49  49 GLY B  456  ASP B  460  5                                   5    
HELIX   50  50 ASP B  460  ASN B  464  5                                   5    
HELIX   51  51 THR B  466  GLY B  487  1                                  22    
HELIX   52  52 ARG B  525  ARG B  534  1                                  10    
HELIX   53  53 PHE B  535  SER B  541  1                                   7    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.05  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
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  2.05  
LINK         ND2 ASN A 350                 C1  NAG A1544     1555   1555  1.45  
LINK         ND2 ASN A 464                 C1  NAG A1547     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B1548     1555   1555  1.45  
LINK         ND2 ASN B 464                 C1  NAG B1546     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0        -4.18                     
CISPEP   2 TYR B  105    PRO B  106          0         5.53                     
SITE     1 AC1 19 ASP A  74  TRP A  86  GLY A 120  GLY A 121                    
SITE     2 AC1 19 GLY A 122  TYR A 124  GLU A 202  TRP A 286                    
SITE     3 AC1 19 SER A 293  ILE A 294  PHE A 295  TYR A 337                    
SITE     4 AC1 19 PHE A 338  TYR A 341  HIS A 447  PE3 A1546                    
SITE     5 AC1 19 5GZ A1549  HOH A2060  HOH A2110                               
SITE     1 AC2  2 GLY A 345  ASN A 350                                          
SITE     1 AC3  1 HIS A 381                                                     
SITE     1 AC4  3 TYR A  72  5GZ A1543  5GZ A1549                               
SITE     1 AC5  1 ASN A 464                                                     
SITE     1 AC6  2 GLU A  81  MET A  85                                          
SITE     1 AC7  8 TRP A 286  HIS A 287  LEU A 289  GLN A 291                    
SITE     2 AC7  8 SER A 293  5GZ A1543  PE3 A1546  HOH A2110                    
SITE     1 AC8  1 ASP A   5                                                     
SITE     1 AC9 19 ASP B  74  TRP B  86  GLY B 120  GLY B 121                    
SITE     2 AC9 19 GLY B 122  TYR B 124  GLU B 202  TRP B 286                    
SITE     3 AC9 19 SER B 293  ILE B 294  PHE B 295  PHE B 297                    
SITE     4 AC9 19 TYR B 337  PHE B 338  TYR B 341  HIS B 447                    
SITE     5 AC9 19 5GZ B1552  HOH B2059  HOH B2101                               
SITE     1 BC1  4 TRP B 286  TYR B 341  5GZ B1552  HOH B2148                    
SITE     1 BC2  2 SER B 462  ASN B 464                                          
SITE     1 BC3  4 GLN A 527  HIS B 381  TYR B 382  PE3 B1555                    
SITE     1 BC4  4 GLY B 345  SER B 347  ASN B 350  LEU B 353                    
SITE     1 BC5  5 THR B 112  GLU B 142  GLY B 143  ALA B 144                    
SITE     2 BC5  5 ARG B 485                                                     
SITE     1 BC6  3 ARG B 224  GLN B 325  THR B 486                               
SITE     1 BC7  4 ASP B 333  ASP B 396  LEU B 441  TRP B 442                    
SITE     1 BC8  7 TRP B 286  HIS B 287  LEU B 289  GLU B 292                    
SITE     2 BC8  7 SER B 293  5GZ B1544  PE3 B1545                               
SITE     1 BC9  2 ASP B 304  SER B 309                                          
SITE     1 CC1  1 ARG B 417                                                     
SITE     1 CC2  9 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 CC2  9 ALA B 377  LEU B 380  HIS B 381  PHE B 531                    
SITE     3 CC2  9 PE3 B1547                                                     
SITE     1 CC3  2 ASP A 304  GLY A 305                                          
SITE     1 CC4  1 ASP A 333                                                     
CRYST1   78.671  110.824  227.112  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      0.012711  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004403        0.00000                         
TER    4210      ALA A 542                                                      
TER    8382      THR B 543                                                      
MASTER      697    0   23   53   34    0   35    6 8961    2  279   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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