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LongText Report for: 6r8r-pdb

Name Class
6r8r-pdb
HEADER    HYDROLASE                               02-APR-19   6R8R              
TITLE     STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH ISOQUINOLINE 45  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HNOTUM;                                                     
COMPND   5 EC: 3.1.1.98;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NOTUM, OK/SW-CL.30;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-                           
KEYWDS    WNT SIGNALLING, NOTUM INHIBITOR, CRYSTALLOGRAPHIC FRAGMENT SCREEN,    
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.VECCHIA,Y.ZHAO,R.R.RUZA,E.Y.JONES                                   
REVDAT   1   08-MAY-19 6R8R    0                                                
JRNL        AUTH   B.N.ATKINSON,D.STEADMAN,Y.ZHAO,J.SIPTHORP,L.VECCHIA,         
JRNL        AUTH 2 R.R.RUZA,F.JEGNATHAN,G.LINES,S.FREW,A.MONAGHAN,S.KJAER,      
JRNL        AUTH 3 M.BICTASH,Y.JONES,P.V.FISH                                   
JRNL        TITL   DISCOVERY OF 2-PHENOXYACETAMIDES AS INHIBITORS OF THE        
JRNL        TITL 2 WNT-DEPALMITOLEATING ENZYME NOTUM FROM AN X-RAY FRAGMENT     
JRNL        TITL 3 SCREEN                                                       
JRNL        REF    MEDCHEMCOMM                                2019              
JRNL        REFN                   ESSN 2040-2511                               
JRNL        DOI    10.1039/C9MD00096H                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.15RC3_3435                                  
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 89931                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4507                            
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 24.2041 -  3.9407    1.00     3098   128  0.1714 0.1626        
REMARK   3     2  3.9407 -  3.1300    1.00     2928   158  0.1526 0.1562        
REMARK   3     3  3.1300 -  2.7350    1.00     2921   159  0.1522 0.1724        
REMARK   3     4  2.7350 -  2.4852    1.00     2914   124  0.1499 0.1863        
REMARK   3     5  2.4852 -  2.3072    1.00     2877   131  0.1365 0.1951        
REMARK   3     6  2.3072 -  2.1713    1.00     2880   141  0.1275 0.1619        
REMARK   3     7  2.1713 -  2.0626    1.00     2869   148  0.1168 0.1586        
REMARK   3     8  2.0626 -  1.9728    1.00     2856   149  0.1143 0.1597        
REMARK   3     9  1.9728 -  1.8969    1.00     2843   151  0.1209 0.1809        
REMARK   3    10  1.8969 -  1.8315    1.00     2840   152  0.1148 0.1500        
REMARK   3    11  1.8315 -  1.7742    1.00     2845   146  0.1138 0.1875        
REMARK   3    12  1.7742 -  1.7235    1.00     2836   157  0.1131 0.1763        
REMARK   3    13  1.7235 -  1.6782    1.00     2819   161  0.1117 0.1542        
REMARK   3    14  1.6782 -  1.6372    1.00     2839   140  0.1067 0.1504        
REMARK   3    15  1.6372 -  1.6000    1.00     2852   158  0.1124 0.1380        
REMARK   3    16  1.6000 -  1.5660    1.00     2830   127  0.1179 0.1734        
REMARK   3    17  1.5660 -  1.5347    1.00     2853   138  0.1282 0.2020        
REMARK   3    18  1.5347 -  1.5057    1.00     2804   157  0.1396 0.1923        
REMARK   3    19  1.5057 -  1.4788    1.00     2813   173  0.1378 0.2023        
REMARK   3    20  1.4788 -  1.4538    1.00     2804   164  0.1529 0.1944        
REMARK   3    21  1.4538 -  1.4303    1.00     2805   155  0.1652 0.2172        
REMARK   3    22  1.4303 -  1.4083    1.00     2814   143  0.1802 0.2315        
REMARK   3    23  1.4083 -  1.3876    1.00     2846   147  0.2081 0.2620        
REMARK   3    24  1.3876 -  1.3681    1.00     2813   152  0.2150 0.2523        
REMARK   3    25  1.3681 -  1.3496    1.00     2795   160  0.2305 0.2823        
REMARK   3    26  1.3496 -  1.3320    1.00     2807   163  0.2297 0.2810        
REMARK   3    27  1.3320 -  1.3154    1.00     2807   151  0.2314 0.2824        
REMARK   3    28  1.3154 -  1.2995    1.00     2780   167  0.2429 0.2952        
REMARK   3    29  1.2995 -  1.2844    1.00     2783   147  0.2512 0.2801        
REMARK   3    30  1.2844 -  1.2700    1.00     2853   160  0.2779 0.3334        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.25                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6R8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101554.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91587                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90021                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4UZ1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULPHATE, 0.1 M CITRIC    
REMARK 280  ACID, PH 4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K         
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       30.17000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.06500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.86000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.06500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.17000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.86000            
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: MONOMERIC                         
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 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     GLU A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     GLY A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLN A    83                                                      
REMARK 465     GLN A    84                                                      
REMARK 465     LEU A    85                                                      
REMARK 465     SER A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     LYS A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     LYS A   426                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     HIS A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     HIS A   460                                                      
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    TRP A 128     -145.19     59.27                                   
REMARK 500    ALA A 191       57.91   -143.49                                   
REMARK 500    SER A 232     -127.45     65.30                                   
REMARK 500    SER A 232     -126.24     63.40                                   
REMARK 500    GLN A 311     -175.80     63.77                                   
REMARK 500    GLU A 390      153.45     74.65                                   
REMARK 500    ILE A 391      -38.94   -149.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JV8 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound   
REMARK 800  to ASN A 96                                                         
DBREF  6R8R A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 6R8R GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 6R8R GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6R8R HIS A  460  UNP  Q6P988              EXPRESSION TAG                 
SEQRES   1 A  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG          
SEQRES   2 A  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP          
SEQRES   3 A  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY          
SEQRES   4 A  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR          
SEQRES   5 A  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR          
SEQRES   6 A  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR          
SEQRES   7 A  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU          
SEQRES   8 A  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO          
SEQRES   9 A  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS          
SEQRES  10 A  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE          
SEQRES  11 A  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU          
SEQRES  12 A  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA          
SEQRES  13 A  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA          
SEQRES  14 A  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL          
SEQRES  15 A  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS          
SEQRES  16 A  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS          
SEQRES  17 A  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP          
SEQRES  18 A  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN          
SEQRES  19 A  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL          
SEQRES  20 A  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP          
SEQRES  21 A  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS          
SEQRES  22 A  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR          
SEQRES  23 A  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS          
SEQRES  24 A  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS          
SEQRES  25 A  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL          
SEQRES  26 A  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP          
SEQRES  27 A  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO          
SEQRES  28 A  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO          
SEQRES  29 A  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS          
SEQRES  30 A  383  HIS HIS HIS HIS HIS HIS                                      
HET    NAG  A 501      14                                                       
HET    JV8  A 502      22                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HET    SO4  A 508       5                                                       
HET    SO4  A 509       5                                                       
HET    SO4  A 510       5                                                       
HET    DMS  A 511       4                                                       
HET    DMS  A 512       4                                                       
HET    DMS  A 513       4                                                       
HET    DMS  A 514       4                                                       
HET    DMS  A 515       4                                                       
HET    EDO  A 516       4                                                       
HET    EDO  A 517       4                                                       
HET    EDO  A 518       4                                                       
HET    EDO  A 519       4                                                       
HET    EDO  A 520       4                                                       
HET    EDO  A 521       4                                                       
HET    EDO  A 522       4                                                       
HET    EDO  A 523       4                                                       
HET    EDO  A 524       4                                                       
HET    EDO  A 525       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     JV8 ~{N}-ISOQUINOLIN-6-YL-2-(2-METHYLPHENOXY)ETHANAMIDE              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  JV8    C18 H16 N2 O2                                                
FORMUL   4  SO4    8(O4 S 2-)                                                   
FORMUL  12  DMS    5(C2 H6 O S)                                                 
FORMUL  17  EDO    10(C2 H6 O2)                                                 
FORMUL  27  HOH   *183(H2 O)                                                    
HELIX    1 AA1 ASN A  132  MET A  143  1                                  12    
HELIX    2 AA2 ARG A  144  MET A  147  5                                   4    
HELIX    3 AA3 THR A  159  SER A  163  5                                   5    
HELIX    4 AA4 MET A  203  GLY A  217  1                                  15    
HELIX    5 AA5 ARG A  218  ALA A  223  5                                   6    
HELIX    6 AA6 SER A  232  LEU A  252  1                                  21    
HELIX    7 AA7 ALA A  286  ASN A  299  1                                  14    
HELIX    8 AA8 PRO A  303  GLN A  311  1                                   9    
HELIX    9 AA9 GLU A  314  PHE A  319  5                                   6    
HELIX   10 AB1 PHE A  320  TYR A  325  1                                   6    
HELIX   11 AB2 PRO A  326  LEU A  328  5                                   3    
HELIX   12 AB3 GLU A  341  ASP A  347  1                                   7    
HELIX   13 AB4 GLN A  357  LYS A  376  1                                  20    
HELIX   14 AB5 LEU A  407  LEU A  418  1                                  12    
SHEET    1 AA110 THR A 155  THR A 157  0                                        
SHEET    2 AA110 ASP A  88  LEU A  93 -1  N  LEU A  89   O  ARG A 156           
SHEET    3 AA110 GLY A 108  LYS A 112 -1  O  TYR A 109   N  HIS A  92           
SHEET    4 AA110 ASN A 176  ILE A 180 -1  O  PHE A 179   N  TYR A 110           
SHEET    5 AA110 ARG A 119  LEU A 124  1  N  PHE A 123   O  ILE A 180           
SHEET    6 AA110 VAL A 225  SER A 231  1  O  LEU A 227   N  TRP A 120           
SHEET    7 AA110 GLN A 258  ASP A 264  1  O  ARG A 260   N  LEU A 228           
SHEET    8 AA110 VAL A 332  VAL A 335  1  O  VAL A 335   N  ALA A 263           
SHEET    9 AA110 SER A 381  ALA A 383  1  O  PHE A 382   N  VAL A 334           
SHEET   10 AA110 HIS A 435  VAL A 437  1  O  LEU A 436   N  ALA A 383           
SHEET    1 AA2 2 PHE A 339  ASP A 340  0                                        
SHEET    2 AA2 2 LEU A 387  SER A 388  1  O  SER A 388   N  PHE A 339           
SHEET    1 AA3 2 GLN A 401  VAL A 402  0                                        
SHEET    2 AA3 2 THR A 405  SER A 406 -1  O  THR A 405   N  VAL A 402           
SSBOND   1 CYS A  101    CYS A  183                          1555   1555  2.07  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.04  
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.04  
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.23  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.02  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.01  
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.04  
LINK         ND2 ASN A  96                 C1  NAG A 501     1555   1555  1.43  
SITE     1 AC1  7 TRP A 128  TYR A 129  PHE A 268  ILE A 291                    
SITE     2 AC1  7 THR A 345  SO4 A 507  HOH A 619                               
SITE     1 AC2  5 ARG A 305  ARG A 308  GLN A 357  GLU A 358                    
SITE     2 AC2  5 ARG A 361                                                     
SITE     1 AC3  4 HIS A 373  LYS A 376  HOH A 604  HOH A 701                    
SITE     1 AC4  8 THR A 142  MET A 143  ARG A 144  ARG A 145                    
SITE     2 AC4  8 ARG A 409  HIS A 412  ARG A 416  HOH A 668                    
SITE     1 AC5  4 TYR A 274  ARG A 275  LEU A 360  HOH A 730                    
SITE     1 AC6  7 GLY A 127  TRP A 128  SER A 232  ALA A 233                    
SITE     2 AC6  7 HIS A 389  JV8 A 502  HOH A 603                               
SITE     1 AC7  9 ARG A 133  LYS A 197  ASN A 198  GLU A 199                    
SITE     2 AC7  9 ARG A 275  TYR A 297  HOH A 717  HOH A 719                    
SITE     3 AC7  9 HOH A 728                                                     
SITE     1 AC8  5 ARG A 244  GLU A 247  VAL A 302  ARG A 307                    
SITE     2 AC8  5 HOH A 671                                                     
SITE     1 AC9  3 ARG A  90  HIS A  92  ARG A 218                               
SITE     1 AD1  4 TYR A 171  TRP A 172  TRP A 173  ASN A 174                    
SITE     1 AD2  7 TYR A 325  LEU A 328  ARG A 329  SER A 330                    
SITE     2 AD2  7 PRO A 331  VAL A 332  HOH A 602                               
SITE     1 AD3  6 TYR A 110  GLU A 125  TRP A 152  ARG A 156                    
SITE     2 AD3  6 PHE A 179  PRO A 181                                          
SITE     1 AD4  3 ARG A 394  SER A 395  HIS A 396                               
SITE     1 AD5  6 PRO A 255  ARG A 372  LYS A 403  VAL A 437                    
SITE     2 AD5  6 HOH A 631  HOH A 718                                          
SITE     1 AD6  6 TRP A 128  TYR A 129  ARG A 139  MET A 143                    
SITE     2 AD6  6 EDO A 524  HOH A 609                                          
SITE     1 AD7  5 ARG A 156  THR A 157  GLY A 158  THR A 159                    
SITE     2 AD7  5 PHE A 179                                                     
SITE     1 AD8  7 TYR A 254  LYS A 376  ASP A 377  VAL A 378                    
SITE     2 AD8  7 PRO A 379  HIS A 435  HOH A 688                               
SITE     1 AD9  8 LEU A 269  ASP A 270  ASN A 271  GLN A 273                    
SITE     2 AD9  8 PRO A 287  THR A 288  VAL A 346  ASP A 347                    
SITE     1 AE1  5 ASP A 103  LYS A 194  GLU A 199  TYR A 200                    
SITE     2 AE1  5 EDO A 525                                                     
SITE     1 AE2  6 TYR A 322  TYR A 325  PRO A 326  THR A 374                    
SITE     2 AE2  6 HOH A 678  HOH A 699                                          
SITE     1 AE3  4 GLN A 401  LYS A 403  GLY A 404  ASN A 446                    
SITE     1 AE4  6 SER A 192  ASN A 198  ARG A 296  TYR A 297                    
SITE     2 AE4  6 ASN A 299  HOH A 601                                          
SITE     1 AE5  7 SER A 138  ARG A 139  THR A 142  MET A 143                    
SITE     2 AE5  7 PRO A 170  TRP A 173  EDO A 516                               
SITE     1 AE6  5 ASP A 103  LYS A 194  THR A 277  ASP A 278                    
SITE     2 AE6  5 EDO A 520                                                     
SITE     1 AE7  8 ASN A  96  SER A  98  VAL A  99  PRO A 153                    
SITE     2 AE7  8 ARG A 154  THR A 155  ARG A 213  HOH A 690                    
CRYST1   60.340   71.720   78.130  90.00  90.00  90.00 P 21 21 21    4          
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      0.016573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013943  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012799        0.00000                         
TER    2969      THR A 453                                                      
MASTER      370    0   25   14   14    0   45    6 3212    1  153   30          
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:
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