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LongText Report for: 4UYW-pdb

Name Class
4UYW-pdb
HEADER    HYDROLASE                               03-SEP-14   4UYW              
TITLE     STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I HEPARIN         
TITLE    2 FRAGMENT COMPLEX - 1.7A                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN NOTUM HOMOLOG;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: GLYCOSYLATED AT N96                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    HYDROLASE, WNT, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZEBISCH,E.Y.JONES                                                   
REVDAT   1   25-FEB-15 4UYW    0                                                
JRNL        AUTH   S.KAKUGAWA,P.F.LANGTON,M.ZEBISCH,S.A.HOWELL,T.-H.CHANG,      
JRNL        AUTH 2 Y.LIU,T.FEIZI,G.BINEVA,N.O'REILLY,A.P.SNIJDERS,E.Y.JONES,    
JRNL        AUTH 3 J.-P.VINCENT                                                 
JRNL        TITL   NOTUM DEACYLATES WNT PROTEINS TO SUPPRESS SIGNALLING         
JRNL        TITL 2 ACTIVITY                                                     
JRNL        REF    NATURE                                     2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        DOI    10.1038/NATURE14259                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.99                          
REMARK   3   NUMBER OF REFLECTIONS             : 87882                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.18226                         
REMARK   3   R VALUE            (WORKING SET) : 0.18169                         
REMARK   3   FREE R VALUE                     : 0.22092                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.5                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1328                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.700                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.744                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6496                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.272                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.283                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5637                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 475                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.082                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41                                                
REMARK   3    B22 (A**2) : 1.12                                                 
REMARK   3    B33 (A**2) : -0.71                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.097         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.691         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5877 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5416 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8019 ; 1.374 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12407 ; 0.819 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   709 ; 6.077 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   288 ;32.390 ;22.257       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   942 ;12.205 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;17.460 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   856 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6636 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1480 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2786 ; 1.309 ; 1.762       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2785 ; 1.309 ; 1.761       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3475 ; 2.185 ; 2.623       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3089 ; 1.927 ; 2.123       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    85        A   451                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5003 -28.0357 -29.0765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0652 T22:   0.0417                                     
REMARK   3      T33:   0.0749 T12:   0.0243                                     
REMARK   3      T13:  -0.0173 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9482 L22:   0.0806                                     
REMARK   3      L33:   0.2976 L12:  -0.0514                                     
REMARK   3      L13:   0.0992 L23:   0.0735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0579 S12:  -0.0353 S13:   0.0677                       
REMARK   3      S21:  -0.0171 S22:   0.0199 S23:  -0.0343                       
REMARK   3      S31:  -0.0414 S32:  -0.0383 S33:   0.0379                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    86        B   451                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5225 -14.9562  -0.7144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0881 T22:   0.0965                                     
REMARK   3      T33:   0.0498 T12:   0.0885                                     
REMARK   3      T13:  -0.0154 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5329 L22:   0.4612                                     
REMARK   3      L33:   0.3916 L12:  -0.4330                                     
REMARK   3      L13:   0.0219 L23:  -0.0960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.0419 S13:  -0.0671                       
REMARK   3      S21:   0.0727 S22:   0.0211 S23:  -0.0060                       
REMARK   3      S31:  -0.0918 S32:  -0.1047 S33:  -0.0049                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4UYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61673.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89279                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       37.03200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       89.28000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.03200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       89.28000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2146   LIES ON A SPECIAL POSITION.                         
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     LYS A   194                                                      
REMARK 465     SER A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     ASN A   198                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     PRO A   355                                                      
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     PRO A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     LYS A   430                                                      
REMARK 465     GLY A   431                                                      
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 465     GLU B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     GLY B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     ALA B    82                                                      
REMARK 465     GLN B    83                                                      
REMARK 465     GLN B    84                                                      
REMARK 465     LEU B    85                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     ASN B   198                                                      
REMARK 465     THR B   352                                                      
REMARK 465     GLY B   353                                                      
REMARK 465     GLN B   354                                                      
REMARK 465     PRO B   355                                                      
REMARK 465     VAL B   356                                                      
REMARK 465     HIS B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     SER B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     ALA B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     LYS B   426                                                      
REMARK 465     THR B   427                                                      
REMARK 465     PRO B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     LYS B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     GLY B   452                                                      
REMARK 465     THR B   453                                                      
REMARK 465     LYS B   454                                                      
REMARK 465     HIS B   455                                                      
REMARK 465     HIS B   456                                                      
REMARK 465     HIS B   457                                                      
REMARK 465     HIS B   458                                                      
REMARK 465     HIS B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B 196    CG   CD   OE1  OE2                                  
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   NH2  ARG B   292     NH2  ARG B   292     2555     1.87            
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    CYS A 432   CA  -  CB  -  SG  ANGL. DEV. =   8.2 DEGREES          
REMARK 500    PRO A 433   C   -  N   -  CA  ANGL. DEV. =  12.6 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     -139.10     55.62                                   
REMARK 500    TYR A 129      172.76    179.96                                   
REMARK 500    ASN A 169       75.24   -154.24                                   
REMARK 500    SER A 232     -119.16     52.11                                   
REMARK 500    VAL A 280      -73.68   -125.25                                   
REMARK 500    PHE A 339       69.13   -119.84                                   
REMARK 500    GLU A 390      156.76     72.23                                   
REMARK 500    ILE A 391      -36.04   -160.19                                   
REMARK 500    TRP B 128     -140.05     61.59                                   
REMARK 500    TYR B 129      172.61    176.03                                   
REMARK 500    MET B 143       54.01   -147.07                                   
REMARK 500    SER B 232     -121.34     54.84                                   
REMARK 500    VAL B 280      -60.05   -121.74                                   
REMARK 500    PHE B 339       74.36   -117.99                                   
REMARK 500    GLU B 390      153.55     71.67                                   
REMARK 500    ILE B 391      -34.86   -156.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  432     PRO A  433                 -146.07                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H1S A1453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A1452  BOUND TO ASN A  96                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B1452  BOUND TO ASN B  96                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UYU   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I               
REMARK 900   IODIDE COMPLEX - 2.3A                                              
REMARK 900 RELATED ID: 4UYZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II              
REMARK 900   - 2.8A                                                             
REMARK 900 RELATED ID: 4UZ1   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM                 
REMARK 900  III - 1.4A                                                          
REMARK 900 RELATED ID: 4UZ5   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM IV              
REMARK 900   - 2.1A                                                             
REMARK 900 RELATED ID: 4UZ6   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM V               
REMARK 900   - SOS COMPLEX - 1.9A                                               
REMARK 900 RELATED ID: 4UZ7   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM               
REMARK 900  VII - SOS COMPLEX - 2.2A                                            
REMARK 900 RELATED ID: 4UZ9   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM                 
REMARK 900  VII - SOS COMPLEX - 2.2A                                            
REMARK 900 RELATED ID: 4UZA   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM                 
REMARK 900  VIII - PHOSPHATE COMPLEX - 2.4A                                     
REMARK 900 RELATED ID: 4UZJ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM                 
REMARK 900  III - 1.4A                                                          
REMARK 900 RELATED ID: 4UZK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM FROM DROSOPHILA -              
REMARK 900  CRYSTAL FORM II - 1.9A                                              
REMARK 900 RELATED ID: 4UZL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I               
REMARK 900   MYRISTOLEATE COMPLEX - 2.1A                                        
REMARK 900 RELATED ID: 4UZQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH                
REMARK 900  O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A                      
REMARK 900 RELATED ID: 4WBH   RELATED DB: PDB                                   
DBREF  4UYW A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
DBREF  4UYW B   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 4UYW GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS A  460  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 4UYW GLU B   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW THR B   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW GLY B   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW GLY B  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW THR B  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW LYS B  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW HIS B  460  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 4UYW SER B  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
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                                      
SEQRES   1 B  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG          
SEQRES   2 B  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP          
SEQRES   3 B  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY          
SEQRES   4 B  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR          
SEQRES   5 B  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR          
SEQRES   6 B  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR          
SEQRES   7 B  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU          
SEQRES   8 B  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO          
SEQRES   9 B  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS          
SEQRES  10 B  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE          
SEQRES  11 B  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU          
SEQRES  12 B  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA          
SEQRES  13 B  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA          
SEQRES  14 B  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL          
SEQRES  15 B  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS          
SEQRES  16 B  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS          
SEQRES  17 B  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP          
SEQRES  18 B  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN          
SEQRES  19 B  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL          
SEQRES  20 B  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP          
SEQRES  21 B  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS          
SEQRES  22 B  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR          
SEQRES  23 B  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS          
SEQRES  24 B  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS          
SEQRES  25 B  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL          
SEQRES  26 B  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP          
SEQRES  27 B  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO          
SEQRES  28 B  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO          
SEQRES  29 B  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS          
SEQRES  30 B  383  HIS HIS HIS HIS HIS HIS                                      
HET    NAG  A1452      14                                                       
HET    NAG  B1452      14                                                       
HET    H1S  A1453      35                                                       
HETNAM     H1S HEPARIN DISACCHARIDE I-S                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  H1S    C12 H15 N O19 S3 4-                                          
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   5  HOH   *475(H2 O)                                                    
HELIX    1   1 ASN A  132  MET A  143  1                                  12    
HELIX    2   2 ARG A  144  MET A  147  5                                   4    
HELIX    3   3 THR A  159  SER A  163  5                                   5    
HELIX    4   4 MET A  203  GLY A  217  1                                  15    
HELIX    5   5 ARG A  218  ALA A  223  5                                   6    
HELIX    6   6 SER A  232  GLY A  253  1                                  22    
HELIX    7   7 ALA A  286  ASN A  299  1                                  14    
HELIX    8   8 PRO A  303  ARG A  308  1                                   6    
HELIX    9   9 GLU A  314  PHE A  319  5                                   6    
HELIX   10  10 PHE A  320  TYR A  325  1                                   6    
HELIX   11  11 PRO A  326  LEU A  328  5                                   3    
HELIX   12  12 GLU A  341  ASP A  347  1                                   7    
HELIX   13  13 GLN A  357  LYS A  376  1                                  20    
HELIX   14  14 ARG A  394  ASP A  399  5                                   6    
HELIX   15  15 LEU A  407  HIS A  419  1                                  13    
HELIX   16  16 ASN B  132  MET B  143  1                                  12    
HELIX   17  17 ARG B  144  SER B  148  5                                   5    
HELIX   18  18 THR B  159  SER B  163  5                                   5    
HELIX   19  19 MET B  203  GLY B  217  1                                  15    
HELIX   20  20 ARG B  218  ALA B  223  5                                   6    
HELIX   21  21 SER B  232  GLY B  253  1                                  22    
HELIX   22  22 ALA B  286  TRP B  298  1                                  13    
HELIX   23  23 PRO B  303  ARG B  308  1                                   6    
HELIX   24  24 GLU B  314  PHE B  319  5                                   6    
HELIX   25  25 PHE B  320  TYR B  325  1                                   6    
HELIX   26  26 PRO B  326  LEU B  328  5                                   3    
HELIX   27  27 GLU B  341  ASP B  347  1                                   7    
HELIX   28  28 GLN B  357  LEU B  375  1                                  19    
HELIX   29  29 ARG B  394  ASP B  399  5                                   6    
HELIX   30  30 LEU B  407  LEU B  418  1                                  12    
SHEET    1  AA10 THR A 155  ARG A 156  0                                        
SHEET    2  AA10 LEU A  89  LEU A  93 -1  O  LEU A  89   N  ARG A 156           
SHEET    3  AA10 GLY A 108  LYS A 112 -1  O  TYR A 109   N  HIS A  92           
SHEET    4  AA10 ASN A 176  ILE A 180 -1  O  MET A 177   N  LYS A 112           
SHEET    5  AA10 ARG A 119  LEU A 124  1  O  ARG A 119   N  ASN A 176           
SHEET    6  AA10 VAL A 225  SER A 231  1  O  VAL A 225   N  TRP A 120           
SHEET    7  AA10 GLN A 258  ASP A 264  1  O  GLN A 258   N  LEU A 226           
SHEET    8  AA10 VAL A 332  VAL A 335  1  O  PHE A 333   N  ALA A 263           
SHEET    9  AA10 SER A 381  ALA A 383  1  N  PHE A 382   O  VAL A 334           
SHEET   10  AA10 LEU A 436  VAL A 437  1  O  LEU A 436   N  ALA A 383           
SHEET    1  AB 2 PHE A 339  ASP A 340  0                                        
SHEET    2  AB 2 LEU A 387  SER A 388  0                                        
SHEET    1  AC 2 GLN A 401  VAL A 402  0                                        
SHEET    2  AC 2 THR A 405  SER A 406 -1  O  THR A 405   N  VAL A 402           
SHEET    1  BA10 THR B 155  ARG B 156  0                                        
SHEET    2  BA10 LEU B  89  LEU B  93 -1  O  LEU B  89   N  ARG B 156           
SHEET    3  BA10 GLY B 108  LYS B 112 -1  O  TYR B 109   N  HIS B  92           
SHEET    4  BA10 ASN B 176  ILE B 180 -1  O  MET B 177   N  LYS B 112           
SHEET    5  BA10 ARG B 119  LEU B 124  1  O  ARG B 119   N  ASN B 176           
SHEET    6  BA10 VAL B 225  SER B 231  1  O  VAL B 225   N  TRP B 120           
SHEET    7  BA10 GLN B 258  ASP B 264  1  O  GLN B 258   N  LEU B 226           
SHEET    8  BA10 VAL B 332  VAL B 335  1  O  PHE B 333   N  ALA B 263           
SHEET    9  BA10 SER B 381  ALA B 383  1  N  PHE B 382   O  VAL B 334           
SHEET   10  BA10 HIS B 435  VAL B 437  1  O  LEU B 436   N  ALA B 383           
SHEET    1  BB 2 PHE B 339  ASP B 340  0                                        
SHEET    2  BB 2 LEU B 387  SER B 388  1  N  SER B 388   O  PHE B 339           
SHEET    1  BC 2 GLN B 401  VAL B 402  0                                        
SHEET    2  BC 2 THR B 405  SER B 406 -1  O  THR B 405   N  VAL B 402           
SSBOND   1 CYS A  101    CYS A  183                          1555   1555  2.13  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.05  
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.07  
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.14  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.04  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.05  
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.02  
SSBOND   8 CYS B  101    CYS B  183                          1555   1555  2.11  
SSBOND   9 CYS B  130    CYS B  136                          1555   1555  2.05  
SSBOND  10 CYS B  279    CYS B  285                          1555   1555  2.06  
SSBOND  11 CYS B  306    CYS B  318                          1555   1555  2.13  
SSBOND  12 CYS B  386    CYS B  449                          1555   1555  2.03  
SSBOND  13 CYS B  413    CYS B  432                          1555   1555  2.04  
SSBOND  14 CYS B  440    CYS B  445                          1555   1555  2.04  
LINK         ND2 ASN A  96                 C1  NAG A1452     1555   1555  1.44  
LINK         ND2 ASN B  96                 C1  NAG B1452     1555   1555  1.44  
SITE     1 AC1 16 ARG A  90  LYS A 112  GLU A 113  ARG A 115                    
SITE     2 AC1 16 GLU A 247  LYS A 251  GLU A 304  ARG A 305                    
SITE     3 AC1 16 ARG A 308  ARG A 329  HOH A2012  HOH A2034                    
SITE     4 AC1 16 HOH A2035  HOH A2037  HOH A2038  HOH A2201                    
SITE     1 AC2  4 ASN A  96  SER A  98  VAL A  99  HOH A2268                    
SITE     1 AC3  5 ASN B  96  VAL B  99  SER B 193  HOH B2014                    
SITE     2 AC3  5 HOH B2207                                                     
CRYST1   74.064  178.560   61.193  90.00  90.00  90.00 P 21 21 2     8          
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      0.013502  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005600  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016342        0.00000                         
MTRIX1   1 -0.695000  0.719000  0.005000       72.84200    1                    
MTRIX2   1  0.717000  0.693000 -0.077000      -29.65100    1                    
MTRIX3   1 -0.059000 -0.050000 -0.997000      -29.31200    1                    
TER    2837      THR A 451                                                      
TER    5639      THR B 451                                                      
MASTER      509    0    3   30   28    0    7    9 6177    2   93   60          
END                                                                             

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