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LongText Report for: 6yv2-pdb

Name Class
6yv2-pdb
HEADER    HYDROLASE                               27-APR-20   6YV2              
TITLE     STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH A PYRROLIDINE-3- 
TITLE    2 CARBOXYLIC ACID FRAGMENT 598                                         
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-;                          
SOURCE  10 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022                              
KEYWDS    WNT, WNT SIGNALLING, FRIZZLED, FZD, FRAGMENT SCREEN, NOTUM, HYDROLASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.R.RUZA,J.HILLIER,E.Y.JONES                                          
REVDAT   1   13-MAY-20 6YV2    0                                                
JRNL        AUTH   W.MAHY,M.PATEL,D.STEADMAN,H.WOODWARD,B.N.ATKINSON,           
JRNL        AUTH 2 F.SVENSSON,N.J.WILLIS,A.FLINT,D.PAPATHEODOROU,Y.ZHAO,        
JRNL        AUTH 3 L.VECCHIA,R.R.RUZA,S.FREW,A.MONAGHAN,A.COSTA,M.BICTASH,      
JRNL        AUTH 4 M.WALTER,E.Y.JONES,P.V.FISH                                  
JRNL        TITL   SCREENING OF A CUSTOM-DESIGNED ACID FRAGMENT LIBRARY         
JRNL        TITL 2 IDENTIFIES 1-PHENYLPYRROLES AND 1- PHENYLPYRROLIDINES AS     
JRNL        TITL 3 INHIBITORS OF NOTUM CARBOXYLESTERASE ACTIVITY.               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_3699                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19997                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.580                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1116                            
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 36.5100 -  4.2000    1.00     2596   145  0.1845 0.1990        
REMARK   3     2  4.2000 -  3.3300    0.99     2430   148  0.1953 0.1969        
REMARK   3     3  3.3300 -  2.9100    1.00     2411   177  0.2149 0.2354        
REMARK   3     4  2.9100 -  2.6500    1.00     2427   165  0.2319 0.2510        
REMARK   3     5  2.6500 -  2.4600    1.00     2412   136  0.2333 0.2941        
REMARK   3     6  2.4600 -  2.3100    1.00     2426   132  0.2409 0.2292        
REMARK   3     7  2.3100 -  2.2000    0.73     1757    82  0.3699 0.4385        
REMARK   3     8  2.2000 -  2.1000    1.00     2422   131  0.2639 0.2822        
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)     : 0.184            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.428           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.81                          
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      :  0.003           3034                                  
REMARK   3   ANGLE     :  0.646           4128                                  
REMARK   3   CHIRALITY :  0.053            437                                  
REMARK   3   PLANARITY :  0.004            539                                  
REMARK   3   DIHEDRAL  : 24.442           1116                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7788  -1.8868  -2.4909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2113 T22:   0.2466                                     
REMARK   3      T33:   0.5405 T12:  -0.0307                                     
REMARK   3      T13:  -0.0614 T23:   0.0530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2595 L22:   1.9544                                     
REMARK   3      L33:   1.1096 L12:  -0.0465                                     
REMARK   3      L13:  -0.2376 L23:  -0.1681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0003 S12:   0.0255 S13:   0.1237                       
REMARK   3      S21:   0.0667 S22:  -0.0260 S23:  -0.0772                       
REMARK   3      S31:  -0.1974 S32:   0.0341 S33:   0.0217                       
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 6YV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292108346.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-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                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : DIALS                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28311                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
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   (%): 37.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULPHATE, 0.1 M CITRIC    
REMARK 280  ACID, PH 4.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K       
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       29.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.51000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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     ASN A    86                                                      
REMARK 465     GLU A    87                                                      
REMARK 465     ASP A   420                                                      
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     THR A   453                                                      
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     -136.34     59.25                                   
REMARK 500    TYR A 129     -175.48   -175.53                                   
REMARK 500    ASN A 135      -31.54   -163.66                                   
REMARK 500    ALA A 191       42.80   -141.98                                   
REMARK 500    SER A 192     -148.33   -100.44                                   
REMARK 500    SER A 193      136.64   -174.28                                   
REMARK 500    SER A 232     -118.03     52.63                                   
REMARK 500    ASP A 281      149.68     72.38                                   
REMARK 500    GLN A 311     -171.99     64.25                                   
REMARK 500    GLU A 390      158.66     72.85                                   
REMARK 500    ILE A 391      -45.60   -145.71                                   
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 A 705        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A 706        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 707        DISTANCE =  7.13 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PUE 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 EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
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  6YV2 A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 6YV2 GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 6YV2 GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6YV2 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    PUE  A 502      14                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    EDO  A 506       4                                                       
HET    EDO  A 507       4                                                       
HET    EDO  A 508       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PUE (3~{R})-1-PHENYLPYRROLIDINE-3-CARBOXYLIC ACID                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  PUE    C11 H13 N O2                                                 
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7  EDO    3(C2 H6 O2)                                                  
FORMUL  10  HOH   *107(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  LEU A  375  1                                  19    
HELIX   14 AB5 LEU A  407  LEU A  418  1                                  12    
SHEET    1 AA110 THR A 155  ARG A 156  0                                        
SHEET    2 AA110 LEU A  89  LEU A  93 -1  N  LEU A  89   O  ARG A 156           
SHEET    3 AA110 GLY A 108  LYS A 112 -1  O  LEU A 111   N  ARG A  90           
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  VAL A 178           
SHEET    6 AA110 VAL A 225  SER A 231  1  O  ALA A 229   N  LEU A 124           
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  PHE A 333   N  GLY A 261           
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  2.03  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.03  
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.04  
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.03  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.02  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.03  
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.03  
LINK         ND2 ASN A  96                 C1  NAG A 501     1555   1555  1.44  
SITE     1 AC1  7 TRP A 128  TYR A 129  SER A 232  ALA A 233                    
SITE     2 AC1  7 PHE A 268  ALA A 342  HIS A 389                               
SITE     1 AC2  4 PRO A 255  ALA A 256  LYS A 403  HOH A 639                    
SITE     1 AC3  7 THR A 142  MET A 143  ARG A 144  ARG A 145                    
SITE     2 AC3  7 HIS A 412  ARG A 416  SO4 A 505                               
SITE     1 AC4  7 MET A 143  ARG A 144  ARG A 145  ASP A 151                    
SITE     2 AC4  7 ARG A 409  ARG A 416  SO4 A 504                               
SITE     1 AC5  5 LEU A 252  GLY A 253  PRO A 433  VAL A 434                    
SITE     2 AC5  5 HIS A 435                                                     
SITE     1 AC6  7 TYR A 325  LEU A 328  SER A 330  PRO A 331                    
SITE     2 AC6  7 VAL A 332  GLN A 354  HOH A 663                               
SITE     1 AC7  4 ARG A 244  GLU A 247  PRO A 303  GLU A 304                    
SITE     1 AC8  8 ASN A  96  SER A  98  VAL A  99  PRO A 153                    
SITE     2 AC8  8 ARG A 154  THR A 155  ARG A 213  HOH A 607                    
CRYST1   59.300   73.020   79.460  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      0.016863  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013695  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012585        0.00000                         
TER    2902      GLY A 452                                                      
MASTER      323    0    8   14   14    0   14    6 3023    1   70   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:
ESTHER Home Page and ACEDB Home Page
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