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LongText Report for: 6cqx-pdb

Name Class
6cqx-pdb
HEADER    HYDROLASE                               16-MAR-18   6CQX              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED 
TITLE    2 BY VX(+)                                                             
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    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.BESTER,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT                            
REVDAT   1   05-DEC-18 6CQX    0                                                
JRNL        AUTH   S.M.BESTER,M.A.GUELTA,J.CHEUNG,M.D.WINEMILLER,S.Y.BAE,       
JRNL        AUTH 2 J.MYSLINSKI,S.D.PEGAN,J.J.HEIGHT                             
JRNL        TITL   STRUCTURAL INSIGHTS OF STEREOSPECIFIC INHIBITION OF HUMAN    
JRNL        TITL 2 ACETYLCHOLINESTERASE BY VX AND SUBSEQUENT REACTIVATION BY    
JRNL        TITL 3 HI-6.                                                        
JRNL        REF    CHEM. RES. TOXICOL.                        2018              
JRNL        REFN                   ISSN 1520-5010                               
JRNL        PMID   30462502                                                     
JRNL        DOI    10.1021/ACS.CHEMRESTOX.8B00294                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 81623                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4059                            
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 41.2404 -  7.3611    0.96     2807   153  0.1651 0.1937        
REMARK   3     2  7.3611 -  5.8480    1.00     2770   146  0.1623 0.1853        
REMARK   3     3  5.8480 -  5.1103    1.00     2783   128  0.1471 0.1558        
REMARK   3     4  5.1103 -  4.6438    1.00     2726   147  0.1208 0.1633        
REMARK   3     5  4.6438 -  4.3113    1.00     2686   152  0.1142 0.1303        
REMARK   3     6  4.3113 -  4.0574    1.00     2703   145  0.1229 0.1461        
REMARK   3     7  4.0574 -  3.8543    1.00     2700   154  0.1246 0.1514        
REMARK   3     8  3.8543 -  3.6867    1.00     2710   120  0.1353 0.1705        
REMARK   3     9  3.6867 -  3.5448    1.00     2682   156  0.1447 0.1593        
REMARK   3    10  3.5448 -  3.4226    1.00     2691   134  0.1559 0.1971        
REMARK   3    11  3.4226 -  3.3156    1.00     2673   119  0.1519 0.2113        
REMARK   3    12  3.3156 -  3.2209    1.00     2670   160  0.1589 0.2085        
REMARK   3    13  3.2209 -  3.1361    1.00     2644   132  0.1721 0.1832        
REMARK   3    14  3.1361 -  3.0596    1.00     2698   131  0.1679 0.1962        
REMARK   3    15  3.0596 -  2.9901    1.00     2604   162  0.1597 0.1996        
REMARK   3    16  2.9901 -  2.9265    1.00     2689   110  0.1711 0.2380        
REMARK   3    17  2.9265 -  2.8679    1.00     2708   129  0.1752 0.2089        
REMARK   3    18  2.8679 -  2.8138    1.00     2646   149  0.1776 0.2375        
REMARK   3    19  2.8138 -  2.7636    1.00     2625   136  0.1776 0.2208        
REMARK   3    20  2.7636 -  2.7167    1.00     2666   147  0.1832 0.2169        
REMARK   3    21  2.7167 -  2.6729    1.00     2679   105  0.1776 0.2587        
REMARK   3    22  2.6729 -  2.6318    1.00     2609   160  0.1888 0.2437        
REMARK   3    23  2.6318 -  2.5931    1.00     2663   136  0.1875 0.2221        
REMARK   3    24  2.5931 -  2.5566    1.00     2614   155  0.1856 0.2253        
REMARK   3    25  2.5566 -  2.5220    1.00     2641   149  0.1932 0.2453        
REMARK   3    26  2.5220 -  2.4893    1.00     2646   145  0.2004 0.2349        
REMARK   3    27  2.4893 -  2.4582    1.00     2635   142  0.2063 0.2478        
REMARK   3    28  2.4582 -  2.4286    1.00     2654   129  0.2154 0.2259        
REMARK   3    29  2.4286 -  2.4003    0.95     2542   128  0.2307 0.2649        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           8781                                  
REMARK   3   ANGLE     :  0.990          12020                                  
REMARK   3   CHIRALITY :  0.057           1301                                  
REMARK   3   PLANARITY :  0.007           1576                                  
REMARK   3   DIHEDRAL  :  5.555           6976                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 3:257)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -57.2108  32.8370 -18.0806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2683 T22:   0.1846                                     
REMARK   3      T33:   0.1798 T12:  -0.0011                                     
REMARK   3      T13:   0.0274 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0703 L22:   1.6226                                     
REMARK   3      L33:   2.8808 L12:  -0.5665                                     
REMARK   3      L13:  -0.4439 L23:   0.8959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:  -0.1102 S13:   0.0220                       
REMARK   3      S21:   0.1610 S22:  -0.0243 S23:   0.0166                       
REMARK   3      S31:   0.1590 S32:  -0.2456 S33:   0.0353                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 258:315)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -39.3249  23.9844 -21.8544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3970 T22:   0.3303                                     
REMARK   3      T33:   0.3020 T12:   0.1371                                     
REMARK   3      T13:   0.0420 T23:  -0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0519 L22:   4.3977                                     
REMARK   3      L33:   3.7149 L12:   1.1255                                     
REMARK   3      L13:   2.3323 L23:   2.0251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1581 S12:   0.2635 S13:  -0.0672                       
REMARK   3      S21:   0.0948 S22:   0.2399 S23:  -0.3839                       
REMARK   3      S31:   0.4680 S32:   0.5799 S33:  -0.0737                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 316:542)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -54.3431  35.6317 -42.7376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2931 T22:   0.2729                                     
REMARK   3      T33:   0.1954 T12:   0.0446                                     
REMARK   3      T13:  -0.0082 T23:  -0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1556 L22:   1.1750                                     
REMARK   3      L33:   2.8368 L12:  -0.2718                                     
REMARK   3      L13:  -1.3541 L23:   0.6246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:   0.1685 S13:   0.0503                       
REMARK   3      S21:  -0.1802 S22:  -0.0318 S23:  -0.0602                       
REMARK   3      S31:  -0.1737 S32:  -0.1847 S33:  -0.0160                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 4:254)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -29.8711 -13.6224 -13.9388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1417 T22:   0.2821                                     
REMARK   3      T33:   0.2147 T12:   0.0594                                     
REMARK   3      T13:  -0.0103 T23:  -0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9317 L22:   1.8261                                     
REMARK   3      L33:   1.9697 L12:   0.1218                                     
REMARK   3      L13:   0.1533 L23:   0.0626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0579 S12:  -0.1912 S13:   0.0220                       
REMARK   3      S21:   0.0388 S22:  -0.0538 S23:  -0.0373                       
REMARK   3      S31:  -0.1098 S32:  -0.0361 S33:  -0.0104                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 255:322)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9037  -3.4255 -29.9567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4355 T22:   0.3089                                     
REMARK   3      T33:   0.2126 T12:   0.0646                                     
REMARK   3      T13:  -0.0128 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8416 L22:   7.7543                                     
REMARK   3      L33:   2.2463 L12:  -1.8132                                     
REMARK   3      L13:  -0.7892 L23:   3.1634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0340 S12:   0.1859 S13:   0.0607                       
REMARK   3      S21:  -0.8443 S22:  -0.1401 S23:   0.1492                       
REMARK   3      S31:  -0.3860 S32:   0.0287 S33:   0.1185                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 323:542)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7606 -25.1480 -30.9171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2397 T22:   0.2728                                     
REMARK   3      T33:   0.2379 T12:   0.0183                                     
REMARK   3      T13:  -0.0314 T23:  -0.0549                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0020 L22:   1.0685                                     
REMARK   3      L33:   4.1261 L12:  -0.5606                                     
REMARK   3      L13:   1.1691 L23:  -0.7235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:   0.0152 S13:  -0.0201                       
REMARK   3      S21:  -0.1530 S22:  -0.0326 S23:   0.1490                       
REMARK   3      S31:   0.0433 S32:  -0.4391 S33:   0.0197                       
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 6CQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233253.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
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   : 81653                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 TO 21% PEG 3350, 0.17 - 0.21M         
REMARK 280  POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 295K, TEMPERATURE 295.0K                                
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      107.96767            
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      215.93533            
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      215.93533            
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      107.96767            
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: 5420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -107.96767            
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     PRO A   492                                                      
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     PRO B   492                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     ALA B   497                                                      
REMARK 465     THR B   543                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   203     P1    VX A   601              1.32            
REMARK 500   ND2  ASN A   350     O5   NAG A   603              1.77            
REMARK 500   O3   FUC A   607     O4   NAG A   609              2.04            
REMARK 500   OG   SER A   203     O1    VX A   601              2.06            
REMARK 500   CG   ASN A   265     C1   NAG A   608              2.17            
REMARK 500   OG   SER A   203     O2    VX A   601              2.19            
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 166   N   -  CA  -  C   ANGL. DEV. =  16.4 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       -4.37     79.25                                   
REMARK 500    ALA A  62       68.52   -100.08                                   
REMARK 500    ALA A 167       71.84   -151.51                                   
REMARK 500    SER A 203     -118.60     53.64                                   
REMARK 500    PHE A 295      -63.22   -105.43                                   
REMARK 500    ASP A 306      -84.96   -103.22                                   
REMARK 500    VAL A 407      -62.87   -126.52                                   
REMARK 500    PHE B  47       -6.94     79.53                                   
REMARK 500    ALA B  62       50.85   -111.03                                   
REMARK 500    PHE B 158       10.41   -141.58                                   
REMARK 500    SER B 203     -120.29     56.13                                   
REMARK 500    ARG B 296       37.40    -90.38                                   
REMARK 500    ASP B 306      -85.21   -103.15                                   
REMARK 500    TYR B 341       32.84    -90.07                                   
REMARK 500    VAL B 367       77.74   -118.59                                   
REMARK 500    VAL B 407      -60.30   -127.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1127        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B1190        DISTANCE =  5.99 ANGSTROMS                       
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      VX A  601                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A    
REMARK 800  607 through NAG A 609 bound to ASN A 265                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  602 through FUC A 604 bound to ASN A 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound   
REMARK 800  to ASN A 464                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B    
REMARK 800  602 through NAG B 604 bound to ASN B 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VX B 601 and SER B     
REMARK 800  203                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6CQY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQW   RELATED DB: PDB                                   
DBREF  6CQX A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  6CQX 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     VX  A 601       6                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    FUC  A 604      10                                                       
HET    NAG  A 605      14                                                       
HET    7PE  A 606      21                                                       
HET    FUC  A 607      10                                                       
HET    NAG  A 608      14                                                       
HET    NAG  A 609      14                                                       
HET     VX  B 601       6                                                       
HET    FUC  B 602      10                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HETNAM      VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)              
HETNAM   2 7PE  ETHOXY)ETHANOL                                                  
HETSYN     7PE POLYETHYLENE GLYCOL FRAGMENT                                     
FORMUL   3   VX    2(C3 H9 O3 P)                                                
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL   4  FUC    3(C6 H12 O5)                                                 
FORMUL   6  7PE    C14 H30 O7                                                   
FORMUL  10  HOH   *917(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 GLY A  240  VAL A  255  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  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 PHE A  535  SER A  541  1                                   7    
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  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  340  1                                   6    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  TYR B  382  1                                  12    
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 ARG B  534  SER B  541  1                                   8    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  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  LEU A 115   O  VAL A 145           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  SER A 196   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  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 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  VAL B 226   N  LEU B 199           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA6 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  1.93  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  1.96  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05  
LINK         ND2 ASN A 265                 C1  NAG A 608     1555   1555  1.45  
LINK         ND2 ASN A 350                 C1  NAG A 603     1555   1555  1.47  
LINK         ND2 ASN A 464                 C1  NAG A 605     1555   1555  1.55  
LINK         OG  SER B 203                 P1   VX B 601     1555   1555  1.41  
LINK         ND2 ASN B 350                 C1  NAG B 603     1555   1555  1.28  
LINK         ND2 ASN B 350                 O5  NAG B 603     1555   1555  1.32  
LINK         C1  NAG A 602                 O4  NAG A 603     1555   1555  1.44  
LINK         O6  NAG A 603                 C1  FUC A 604     1555   1555  1.44  
LINK         C1  FUC A 607                 O6  NAG A 608     1555   1555  1.44  
LINK         O4  NAG A 608                 C1  NAG A 609     1555   1555  1.44  
LINK         C1  FUC B 602                 O6  NAG B 603     1555   1555  1.44  
LINK         O4  NAG B 603                 C1  NAG B 604     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0         2.33                     
CISPEP   2 CYS A  257    PRO A  258          0       -19.08                     
CISPEP   3 TYR B  105    PRO B  106          0        -3.85                     
SITE     1 AC1  8 GLY A 121  GLY A 122  SER A 203  ALA A 204                    
SITE     2 AC1  8 TRP A 236  PHE A 295  PHE A 297  HIS A 447                    
SITE     1 AC2  5 ASP A 304  GLY A 305  ASP A 306  SER A 309                    
SITE     2 AC2  5 ASN B 283                                                     
SITE     1 AC3  4 ASN A 265  HOH A 701  HOH A 761  HOH B 977                    
SITE     1 AC4  5 GLY A 345  SER A 347  ASN A 350  HOH A 764                    
SITE     2 AC4  5 HOH A 921                                                     
SITE     1 AC5  3 SER A 462  ASN A 464  HOH A 709                               
SITE     1 AC6  7 PRO B 344  GLY B 345  SER B 347  ASN B 350                    
SITE     2 AC6  7 HOH B 856  HOH B 909  HOH B1074                               
SITE     1 AC7 14 GLY B 121  GLY B 122  GLU B 202  ALA B 204                    
SITE     2 AC7 14 GLY B 205  ALA B 206  ALA B 207  GLN B 228                    
SITE     3 AC7 14 SER B 229  GLY B 230  TRP B 236  PHE B 297                    
SITE     4 AC7 14 PHE B 338  HIS B 447                                          
CRYST1  104.934  104.934  323.903  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      0.009530  0.005502  0.000000        0.00000                         
SCALE2      0.000000  0.011004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003087        0.00000                         
TER    4145      ALA A 542                                                      
TER    8325      ALA B 542                                                      
MASTER      484    0   13   52   32    0   14    6 9324    2  178   84          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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