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LongText Report for: 6zvl-pdb

Name Class
6zvl-pdb
HEADER    SIGNALING PROTEIN                       24-JUL-20   6ZVL              
TITLE     ARUK3000263 COMPLEX WITH NOTUM                                        
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                                                      
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_TAXID: 9606                                        
KEYWDS    NOTUM, INHIBITOR, WNT, SIGNALING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,R.RUZA                                                         
REVDAT   1   11-NOV-20 6ZVL    0                                                
JRNL        AUTH   W.MAHY,N.J.WILLIS,Y.ZHAO,H.L.WOODWARD,F.SVENSSON,J.SIPTHORP, 
JRNL        AUTH 2 L.VECCHIA,R.R.RUZA,J.HILLIER,S.KJAER,S.FREW,A.MONAGHAN,      
JRNL        AUTH 3 M.BICTASH,P.C.SALINAS,P.WHITING,J.P.VINCENT,E.Y.JONES,       
JRNL        AUTH 4 P.V.FISH                                                     
JRNL        TITL   5-PHENYL-1,3,4-OXADIAZOL-2(3 H )-ONES ARE POTENT INHIBITORS  
JRNL        TITL 2 OF NOTUM CARBOXYLESTERASE ACTIVITY IDENTIFIED BY THE         
JRNL        TITL 3 OPTIMIZATION OF A CRYSTALLOGRAPHIC FRAGMENT SCREENING HIT.   
JRNL        REF    J.MED.CHEM.                                2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   33124429                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.0C01391                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 81770                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.820                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3945                            
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 52.8300 -  3.9500    1.00     3072   129  0.1894 0.2075        
REMARK   3     2  3.9500 -  3.1300    1.00     2902   159  0.1824 0.1920        
REMARK   3     3  3.1300 -  2.7400    1.00     2890   144  0.1816 0.1770        
REMARK   3     4  2.7400 -  2.4900    1.00     2862   137  0.1826 0.1981        
REMARK   3     5  2.4900 -  2.3100    1.00     2869   130  0.1735 0.1953        
REMARK   3     6  2.3100 -  2.1700    1.00     2813   158  0.1716 0.2090        
REMARK   3     7  2.1700 -  2.0600    1.00     2842   142  0.1693 0.1812        
REMARK   3     8  2.0600 -  1.9700    1.00     2856   137  0.1696 0.1944        
REMARK   3     9  1.9700 -  1.9000    1.00     2809   135  0.1772 0.2081        
REMARK   3    10  1.9000 -  1.8300    0.99     2825   128  0.1859 0.2212        
REMARK   3    11  1.8300 -  1.7800    0.99     2821   127  0.1911 0.2242        
REMARK   3    12  1.7800 -  1.7200    1.00     2754   174  0.1975 0.2381        
REMARK   3    13  1.7200 -  1.6800    0.99     2793   152  0.2046 0.2410        
REMARK   3    14  1.6800 -  1.6400    0.99     2786   126  0.2161 0.2174        
REMARK   3    15  1.6400 -  1.6000    0.99     2785   151  0.2218 0.2525        
REMARK   3    16  1.6000 -  1.5700    0.98     2749   130  0.2319 0.2162        
REMARK   3    17  1.5700 -  1.5400    0.99     2743   147  0.2300 0.2962        
REMARK   3    18  1.5400 -  1.5100    0.98     2796   124  0.2495 0.2817        
REMARK   3    19  1.5100 -  1.4800    0.98     2766   128  0.2662 0.3031        
REMARK   3    20  1.4800 -  1.4500    0.98     2714   151  0.2797 0.2995        
REMARK   3    21  1.4500 -  1.4300    0.98     2728   151  0.2902 0.3364        
REMARK   3    22  1.4300 -  1.4100    0.97     2727   142  0.3175 0.3567        
REMARK   3    23  1.4100 -  1.3900    0.97     2714   141  0.3383 0.3891        
REMARK   3    24  1.3900 -  1.3700    0.97     2698   125  0.3413 0.4065        
REMARK   3    25  1.3700 -  1.3500    0.96     2672   164  0.3606 0.3800        
REMARK   3    26  1.3500 -  1.3300    0.95     2668   145  0.3553 0.4200        
REMARK   3    27  1.3300 -  1.3200    0.96     2675   145  0.3836 0.4299        
REMARK   3    28  1.3200 -  1.3000    0.90     2496   123  0.3878 0.3917        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.090           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.86                          
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  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 86 THROUGH 232 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2018  81.7283  79.0635              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1296 T22:   0.0851                                     
REMARK   3      T33:   0.1402 T12:   0.0049                                     
REMARK   3      T13:  -0.0153 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1274 L22:   1.1616                                     
REMARK   3      L33:   3.0162 L12:  -0.1419                                     
REMARK   3      L13:  -0.4691 L23:  -0.5351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0108 S12:  -0.0029 S13:   0.1194                       
REMARK   3      S21:  -0.0253 S22:   0.0019 S23:   0.0257                       
REMARK   3      S31:  -0.1954 S32:  -0.0531 S33:  -0.0092                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 297 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5945  70.4609  79.1641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0811 T22:   0.1027                                     
REMARK   3      T33:   0.1082 T12:   0.0090                                     
REMARK   3      T13:   0.0086 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6893 L22:   2.1276                                     
REMARK   3      L33:   0.5568 L12:   0.1388                                     
REMARK   3      L13:  -0.0284 L23:   0.3953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.1018 S13:   0.0424                       
REMARK   3      S21:  -0.1140 S22:  -0.0289 S23:  -0.1934                       
REMARK   3      S31:  -0.0861 S32:   0.0351 S33:  -0.0690                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8693  69.7736  76.6535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.1491                                     
REMARK   3      T33:   0.1577 T12:  -0.0179                                     
REMARK   3      T13:   0.0257 T23:  -0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3254 L22:   4.1559                                     
REMARK   3      L33:   3.4330 L12:  -2.6853                                     
REMARK   3      L13:   1.6611 L23:  -2.6535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0546 S12:   0.1192 S13:   0.3012                       
REMARK   3      S21:   0.0371 S22:  -0.0875 S23:  -0.3640                       
REMARK   3      S31:  -0.1924 S32:   0.2288 S33:   0.1316                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 452 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.8518  57.5091  83.9456              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0917 T22:   0.0997                                     
REMARK   3      T33:   0.1100 T12:   0.0012                                     
REMARK   3      T13:   0.0026 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2367 L22:   1.4497                                     
REMARK   3      L33:   1.5824 L12:   0.1565                                     
REMARK   3      L13:  -0.2893 L23:   0.7789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0428 S12:   0.0346 S13:  -0.1053                       
REMARK   3      S21:   0.0381 S22:  -0.0060 S23:   0.0731                       
REMARK   3      S31:   0.0782 S32:  -0.0895 S33:   0.0559                       
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 6ZVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292110293.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9159                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83089                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 12.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32                     
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         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 6TR5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM     
REMARK 280  CITRATE, PH 4.2, EVAPORATION, TEMPERATURE 293K                      
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       29.90250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.01800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.89550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.01800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.90250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.89550            
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: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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     HIS A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     ASP A   278                                                      
REMARK 465     CYS A   279                                                      
REMARK 465     VAL A   280                                                      
REMARK 465     ASP A   281                                                      
REMARK 465     THR A   282                                                      
REMARK 465     ILE A   283                                                      
REMARK 465     THR A   284                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     GLN A   354                                                      
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: 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  HH12  ARG A   409     O1   SO4 A   502              1.20            
REMARK 500  HH22  ARG A   409     O4   SO4 A   502              1.56            
REMARK 500   OD1  ASN A   366     NH2  ARG A   369              1.88            
REMARK 500   NH1  ARG A   409     O1   SO4 A   502              2.02            
REMARK 500   NE2  GLN A   209     OE1  GLN A   248              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   H    ARG A   144     O3   SO4 A   502     2574     1.59            
REMARK 500   N    ARG A   144     O3   SO4 A   502     2574     2.14            
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    LYS A 197   CD  -  CE  -  NZ  ANGL. DEV. = -17.8 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    GLU A  87       66.65   -108.29                                   
REMARK 500    TRP A 128     -142.55     59.61                                   
REMARK 500    ALA A 191       57.52   -144.94                                   
REMARK 500    SER A 232     -122.52     59.08                                   
REMARK 500    SER A 232     -122.17     58.47                                   
REMARK 500    GLN A 311     -177.34     70.10                                   
REMARK 500    GLU A 390      158.61     63.06                                   
REMARK 500    ILE A 391      -34.97   -147.61                                   
REMARK 500    HIS A 444       12.01     92.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6ZUV   RELATED DB: PDB                                   
DBREF  6ZVL A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 6ZVL GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 6ZVL GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZVL 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      28                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    DMS  A 506      10                                                       
HET    DMS  A 507      10                                                       
HET    EDO  A 508      10                                                       
HET    QR2  A 509      17                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     QR2 5-[4-CHLORANYL-3-(TRIFLUOROMETHYL)PHENYL]-3~{H}-1,3,4-           
HETNAM   2 QR2  OXADIAZOL-2-ONE                                                 
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  DMS    2(C2 H6 O S)                                                 
FORMUL   9  EDO    C2 H6 O2                                                     
FORMUL  10  QR2    C9 H4 CL F3 N2 O2                                            
FORMUL  11  HOH   *120(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  GLY A  253  1                                  22    
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  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  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  SER A 381           
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  2.04  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.03  
SSBOND   3 CYS A  306    CYS A  318                          1555   1555  2.04  
SSBOND   4 CYS A  386    CYS A  449                          1555   1555  2.03  
SSBOND   5 CYS A  413    CYS A  432                          1555   1555  2.02  
SSBOND   6 CYS A  440    CYS A  445                          1555   1555  2.02  
LINK         ND2 ASN A  96                 C1  NAG A 501     1555   1555  1.43  
CRYST1   59.805   71.791   78.036  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      0.016721  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012815        0.00000                         
TER    5546      GLY A 452                                                      
MASTER      403    0    9   14   14    0    0    6 2973    1  108   30          
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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