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LongText Report for: 6zuv-pdb

Name Class
6zuv-pdb
HEADER    SIGNALING PROTEIN                       23-JUL-20   6ZUV              
TITLE     NOTUM FRAGMENT 286                                                    
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    WNT NOTUM INHIBITOR COMPLEX, SIGNALING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,E.Y.JONES                                                      
REVDAT   1   11-NOV-20 6ZUV    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.    1.54 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) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51471                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2522                            
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 53.3300 -  4.0400    1.00     2941   161  0.1888 0.2362        
REMARK   3     2  4.0400 -  3.2000    1.00     2828   138  0.1806 0.2388        
REMARK   3     3  3.2000 -  2.8000    1.00     2782   148  0.1963 0.2468        
REMARK   3     4  2.8000 -  2.5400    1.00     2779   130  0.1972 0.2566        
REMARK   3     5  2.5400 -  2.3600    1.00     2767   131  0.1967 0.2206        
REMARK   3     6  2.3600 -  2.2200    1.00     2715   168  0.1942 0.2383        
REMARK   3     7  2.2200 -  2.1100    1.00     2747   136  0.1873 0.2458        
REMARK   3     8  2.1100 -  2.0200    1.00     2712   133  0.2011 0.2617        
REMARK   3     9  2.0200 -  1.9400    0.99     2739   136  0.2119 0.2433        
REMARK   3    10  1.9400 -  1.8700    0.99     2691   152  0.2232 0.3090        
REMARK   3    11  1.8700 -  1.8200    0.99     2701   135  0.2503 0.2773        
REMARK   3    12  1.8200 -  1.7600    1.00     2708   147  0.2655 0.3067        
REMARK   3    13  1.7600 -  1.7200    0.99     2665   153  0.2975 0.3415        
REMARK   3    14  1.7200 -  1.6800    0.99     2689   141  0.3028 0.3198        
REMARK   3    15  1.6800 -  1.6400    0.98     2655   126  0.3217 0.3705        
REMARK   3    16  1.6400 -  1.6000    0.97     2626   136  0.3410 0.3850        
REMARK   3    17  1.6000 -  1.5700    0.97     2649   120  0.3622 0.3958        
REMARK   3    18  1.5700 -  1.5400    0.94     2555   131  0.3685 0.4009        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.53                          
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 88 THROUGH 224 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4384  10.4868  -0.4075              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1764 T22:   0.1242                                     
REMARK   3      T33:   0.1769 T12:  -0.0018                                     
REMARK   3      T13:  -0.0194 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0405 L22:   1.2916                                     
REMARK   3      L33:   2.3049 L12:   0.1100                                     
REMARK   3      L13:  -0.5302 L23:   0.4161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0090 S12:   0.0360 S13:   0.1367                       
REMARK   3      S21:   0.0440 S22:   0.0003 S23:   0.0022                       
REMARK   3      S31:  -0.2151 S32:   0.0156 S33:  -0.0003                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6587  -2.0457  -1.6275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1296 T22:   0.1359                                     
REMARK   3      T33:   0.1292 T12:   0.0013                                     
REMARK   3      T13:   0.0128 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6012 L22:   2.1258                                     
REMARK   3      L33:   0.2526 L12:  -0.2417                                     
REMARK   3      L13:  -0.0827 L23:  -0.1335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0489 S12:  -0.0228 S13:   0.0201                       
REMARK   3      S21:   0.1755 S22:   0.0185 S23:   0.1125                       
REMARK   3      S31:  -0.1303 S32:  -0.0903 S33:  -0.0104                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7338  -2.0743   4.7566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1345 T22:   0.1668                                     
REMARK   3      T33:   0.1867 T12:  -0.0070                                     
REMARK   3      T13:   0.0379 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6626 L22:   5.5618                                     
REMARK   3      L33:   2.9266 L12:   2.2534                                     
REMARK   3      L13:   1.3872 L23:   2.5336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1374 S12:  -0.2303 S13:   0.2665                       
REMARK   3      S21:   0.0869 S22:  -0.2490 S23:   0.3229                       
REMARK   3      S31:  -0.1248 S32:  -0.1953 S33:   0.0530                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 451 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3790 -14.3361  -5.6032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1484 T22:   0.1606                                     
REMARK   3      T33:   0.1937 T12:  -0.0027                                     
REMARK   3      T13:   0.0129 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9139 L22:   1.5686                                     
REMARK   3      L33:   1.7706 L12:  -0.1037                                     
REMARK   3      L13:  -0.4826 L23:  -0.8949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0644 S12:  -0.0134 S13:  -0.1190                       
REMARK   3      S21:  -0.0766 S22:  -0.0285 S23:  -0.1329                       
REMARK   3      S31:   0.1250 S32:   0.1248 S33:   0.1013                       
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 6ZUV 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_1292110251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-17                          
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) : 0.9282                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52038                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
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: MOLREP                                                
REMARK 200 STARTING MODEL: 6TR5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM     
REMARK 280  CITRATE, PH4.2, 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       30.33650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.50050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.14200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.50050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.33650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.14200            
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: 2040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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     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   427                                                      
REMARK 465     GLY A   452                                                      
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   NH1  ARG A   296     O    HOH A   601              2.16            
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   OE1  GLU A   167     OG1  THR A   282     2554     2.08            
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    ARG A 305   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG A 329   CD  -  NE  -  CZ  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG A 329   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 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    TRP A 128     -140.79     53.18                                   
REMARK 500    MET A 143       43.80   -141.64                                   
REMARK 500    MET A 147       -1.66   -143.42                                   
REMARK 500    SER A 148      147.46   -171.30                                   
REMARK 500    ALA A 191       57.31   -145.26                                   
REMARK 500    ALA A 191       56.58   -145.26                                   
REMARK 500    SER A 232     -126.80     61.43                                   
REMARK 500    CYS A 279       91.20    -64.76                                   
REMARK 500    GLN A 311     -178.90     72.10                                   
REMARK 500    VAL A 356     -179.72    -57.29                                   
REMARK 500    GLU A 390      163.38     64.39                                   
REMARK 500    ILE A 391      -33.74   -163.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 329         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6ZUV A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 6ZUV GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 6ZUV GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZUV 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    SO4  A 502       5                                                       
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    EDO  A 508       4                                                       
HET    EDO  A 509       4                                                       
HET    EDO  A 510      10                                                       
HET    B1J  A 511      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     B1J [1-(4-CHLOROPHENYL)-1,2,3-TRIAZOL-4-YL]METHANOL                  
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    6(O4 S 2-)                                                   
FORMUL   9  EDO    3(C2 H6 O2)                                                  
FORMUL  12  B1J    C9 H8 CL N3 O                                                
FORMUL  13  HOH   *133(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 ASP A  281  CYS A  285  5                                   5    
HELIX    8 AA8 ALA A  286  ASN A  299  1                                  14    
HELIX    9 AA9 PRO A  303  GLN A  311  1                                   9    
HELIX   10 AB1 GLU A  314  PHE A  319  5                                   6    
HELIX   11 AB2 PHE A  320  TYR A  325  1                                   6    
HELIX   12 AB3 PRO A  326  LEU A  328  5                                   3    
HELIX   13 AB4 GLU A  341  ASP A  347  1                                   7    
HELIX   14 AB5 GLN A  357  LEU A  375  1                                  19    
HELIX   15 AB6 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  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  2.06  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.02  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.04  
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  
CRYST1   60.673   72.284   79.001  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      0.016482  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013834  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012658        0.00000                         
TER    2872      THR A 451                                                      
MASTER      399    0   11   15   14    0    0    6 3044    1   91   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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