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LongText Report for: 4UZJ-pdb

Name Class
4UZJ-pdb
HEADER    HYDROLASE                               05-SEP-14   4UZJ              
TITLE     STRUCTURE OF A WNT DEACYLASE REGULATOR FROM DROSOPHILA -              
TITLE    2 CRYSTAL FORM I - 2.4A                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NOTUM;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 82-415,598-617;                                   
COMPND   5 SYNONYM: NOTUM PROTEIN, WINGFUL;                                     
COMPND   6 EC: 3.1.1.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: GLYCOSYLATED AT N95                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
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_PLASMID: PHLSEC                                    
KEYWDS    HYDROLASE, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZEBISCH,E.Y.JONES                                                   
REVDAT   1   25-FEB-15 4UZJ    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.71                          
REMARK   3   NUMBER OF REFLECTIONS             : 29879                          
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) : 0.19842                         
REMARK   3   R VALUE            (WORKING SET) : 0.19685                         
REMARK   3   FREE R VALUE                     : 0.24338                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.3                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1030                            
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) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2184                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.43                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.323                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.356                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5469                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53                             
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.106                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07                                                
REMARK   3    B22 (A**2) : -3.79                                                
REMARK   3    B33 (A**2) : 1.87                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 3.07                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.401         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.254         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.748        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5659 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5238 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7701 ; 1.494 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12013 ; 0.813 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   675 ; 6.313 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   260 ;32.990 ;22.154       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   906 ;16.448 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;19.030 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   803 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6346 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1412 ; 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):  2718 ; 2.355 ; 3.646       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2717 ; 2.354 ; 3.645       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3387 ; 3.741 ; 5.461       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2941 ; 3.031 ; 4.014       
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 :   B    85        B  1617                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.6478 -31.4975  25.3906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2162 T22:   0.4629                                     
REMARK   3      T33:   0.1085 T12:   0.0402                                     
REMARK   3      T13:  -0.0914 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0332 L22:   0.9626                                     
REMARK   3      L33:   1.4697 L12:  -0.3561                                     
REMARK   3      L13:   0.1502 L23:  -1.1702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0323 S12:   0.0504 S13:  -0.0237                       
REMARK   3      S21:  -0.2342 S22:  -0.0017 S23:  -0.0017                       
REMARK   3      S31:   0.3097 S32:   0.0153 S33:   0.0340                       
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 :   A    84        A   617                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8440   7.5378  13.1459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1659 T22:   0.5304                                     
REMARK   3      T33:   0.0881 T12:   0.0309                                     
REMARK   3      T13:  -0.1043 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2294 L22:   1.0780                                     
REMARK   3      L33:   0.8019 L12:   1.1094                                     
REMARK   3      L13:   0.4103 L23:  -0.3191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1059 S12:  -0.1709 S13:   0.0217                       
REMARK   3      S21:  -0.0349 S22:   0.0705 S23:   0.0982                       
REMARK   3      S31:  -0.1905 S32:   0.0064 S33:   0.0354                       
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 4UZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-SEP-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61704.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
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   : 30929                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.0                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.80                              
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   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12 M ALCOHOLS, 0.1 M                   
REMARK 280  TRIS/BICINE 8.5, 30 % EDO_P8K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       40.69700            
REMARK 290   SMTRY3   2  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 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    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLY A    83                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     PRO A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     THR A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     ASP A   198                                                      
REMARK 465     ARG A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     GLY A   416                                                      
REMARK 465     ASN A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     ASN A   419                                                      
REMARK 465     GLY A   420                                                      
REMARK 465     CYS A   598                                                      
REMARK 465     GLY A   599                                                      
REMARK 465     GLY A   618                                                      
REMARK 465     THR A   619                                                      
REMARK 465     HIS A   620                                                      
REMARK 465     HIS A   621                                                      
REMARK 465     HIS A   622                                                      
REMARK 465     HIS A   623                                                      
REMARK 465     HIS A   624                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     HIS A   626                                                      
REMARK 465     HIS A   627                                                      
REMARK 465     HIS A   628                                                      
REMARK 465     HIS A   629                                                      
REMARK 465     GLU B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     GLY B    83                                                      
REMARK 465     ASP B    84                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     THR B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     ASN B   201                                                      
REMARK 465     SER B   202                                                      
REMARK 465     GLY B   416                                                      
REMARK 465     ASN B   417                                                      
REMARK 465     ASN B   418                                                      
REMARK 465     ASN B   419                                                      
REMARK 465     GLY B   420                                                      
REMARK 465     CYS B   598                                                      
REMARK 465     GLY B   599                                                      
REMARK 465     THR B   617                                                      
REMARK 465     GLY B   618                                                      
REMARK 465     THR B   619                                                      
REMARK 465     HIS B   620                                                      
REMARK 465     HIS B   621                                                      
REMARK 465     HIS B   622                                                      
REMARK 465     HIS B   623                                                      
REMARK 465     HIS B   624                                                      
REMARK 465     HIS B   625                                                      
REMARK 465     HIS B   626                                                      
REMARK 465     HIS B   627                                                      
REMARK 465     HIS B   628                                                      
REMARK 465     HIS B   629                                                      
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     SER A 202    OG                                                  
REMARK 470     LEU A 600    CG   CD1  CD2                                       
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 155   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 155   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG B 265   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 265   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A 127     -136.34   -121.21                                   
REMARK 500    LEU A 142       51.82   -171.99                                   
REMARK 500    ASN A 173       32.92    -99.49                                   
REMARK 500    SER A 237     -110.29     52.13                                   
REMARK 500    ASN A 256      -62.87   -100.91                                   
REMARK 500    SER A 286      -58.92    -29.40                                   
REMARK 500    TRP A 314      -12.21    -46.94                                   
REMARK 500    PHE A 337       68.85   -114.80                                   
REMARK 500    VAL A 386      -33.80   -158.18                                   
REMARK 500    SER B 116      142.35    -36.91                                   
REMARK 500    TRP B 127     -138.57   -123.64                                   
REMARK 500    LEU B 142       55.74   -154.02                                   
REMARK 500    SER B 237     -112.47     52.28                                   
REMARK 500    ASN B 256      -69.49   -101.82                                   
REMARK 500    SER B 286      -63.73    -26.39                                   
REMARK 500    PHE B 337       68.64   -119.25                                   
REMARK 500    VAL B 386      -34.32   -155.87                                   
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 MONO-SACCHARIDE                   
REMARK 800  NAG B1617  BOUND TO ASN B  95                                       
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: 4UYW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I               
REMARK 900   HEPARIN FRAGMENT COMPLEX - 1.7A                                    
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: 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                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 R416-K597 REPLACED BY GNNNG LINKER                                   
DBREF  4UZJ A   86   415  UNP    Q9VUX3   Q9VUX3_DROME    86    415             
DBREF  4UZJ A  598   617  UNP    Q9VUX3   Q9VUX3_DROME   598    617             
DBREF  4UZJ B   86   415  UNP    Q9VUX3   Q9VUX3_DROME    86    415             
DBREF  4UZJ B  598   617  UNP    Q9VUX3   Q9VUX3_DROME   598    617             
SEQADV 4UZJ GLU A   81  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ THR A   82  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ GLY A   83  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ ASP A   84  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A   85  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ GLY A  416  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN A  417  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN A  418  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN A  419  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ GLY A  420  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ GLY A  618  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ THR A  619  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  620  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  621  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  622  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  623  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  624  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  625  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  626  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  627  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  628  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS A  629  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ GLU B   81  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ THR B   82  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ GLY B   83  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ ASP B   84  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B   85  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ GLY B  416  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN B  417  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN B  418  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ ASN B  419  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ GLY B  420  UNP  Q9VUX3              LINKER                         
SEQADV 4UZJ GLY B  618  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ THR B  619  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  620  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  621  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  622  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  623  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  624  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  625  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  626  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  627  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  628  UNP  Q9VUX3              EXPRESSION TAG                 
SEQADV 4UZJ HIS B  629  UNP  Q9VUX3              EXPRESSION TAG                 
SEQRES   1 A  372  GLU THR GLY ASP HIS ARG SER LEU LYS ARG ALA ASN LEU          
SEQRES   2 A  372  ALA ASN THR SER ILE THR CYS ASN ASP GLY SER HIS ALA          
SEQRES   3 A  372  GLY PHE TYR LEU ARG LYS HIS PRO SER SER LYS LYS TRP          
SEQRES   4 A  372  ILE VAL LEU LEU GLU GLY GLY TRP HIS CYS PHE ASP VAL          
SEQRES   5 A  372  ARG SER CYS ARG SER ARG TRP MET ARG LEU ARG HIS LEU          
SEQRES   6 A  372  MET THR SER SER GLN TRP PRO GLU THR ARG ASP VAL GLY          
SEQRES   7 A  372  GLY ILE LEU SER PRO HIS PRO GLU GLU ASN PRO TYR TRP          
SEQRES   8 A  372  HIS ASN ALA ASN HIS VAL LEU ILE PRO TYR CYS SER SER          
SEQRES   9 A  372  ASP SER TRP SER GLY THR ARG THR GLU PRO ASP THR SER          
SEQRES  10 A  372  ASP ARG GLU ASN SER TRP ARG PHE MET GLY ALA LEU ILE          
SEQRES  11 A  372  LEU ARG GLN VAL ILE ALA GLU LEU ILE PRO VAL GLY LEU          
SEQRES  12 A  372  GLY ARG VAL PRO GLY GLY GLU LEU MET LEU VAL GLY SER          
SEQRES  13 A  372  SER ALA GLY GLY MET GLY VAL MET LEU ASN LEU ASP ARG          
SEQRES  14 A  372  ILE ARG ASP PHE LEU VAL ASN GLU LYS LYS LEU GLN ILE          
SEQRES  15 A  372  THR VAL ARG GLY VAL SER ASP SER GLY TRP PHE LEU ASP          
SEQRES  16 A  372  ARG GLU PRO TYR THR PRO ALA ALA VAL ALA SER ASN GLU          
SEQRES  17 A  372  ALA VAL ARG GLN GLY TRP LYS LEU TRP GLN GLY LEU LEU          
SEQRES  18 A  372  PRO GLU GLU CYS THR LYS SER TYR PRO THR GLU PRO TRP          
SEQRES  19 A  372  ARG CYS TYR TYR GLY TYR ARG LEU TYR PRO THR LEU LYS          
SEQRES  20 A  372  THR PRO LEU PHE VAL PHE GLN TRP LEU PHE ASP GLU ALA          
SEQRES  21 A  372  GLN MET ARG VAL ASP ASN VAL GLY ALA PRO VAL THR PRO          
SEQRES  22 A  372  GLN GLN TRP ASN TYR ILE HIS GLU MET GLY GLY ALA LEU          
SEQRES  23 A  372  ARG SER SER LEU ASP ASN VAL SER ALA VAL PHE ALA PRO          
SEQRES  24 A  372  SER CYS ILE GLY HIS GLY VAL LEU PHE LYS ARG ASP TRP          
SEQRES  25 A  372  VAL ASN ILE LYS ILE ASP ASP ILE SER LEU PRO SER ALA          
SEQRES  26 A  372  LEU ARG CYS TRP GLU HIS SER THR ARG SER GLY ASN ASN          
SEQRES  27 A  372  ASN GLY CYS GLY LEU ARG LEU LEU GLU ARG CYS SER TRP          
SEQRES  28 A  372  PRO GLN CYS ASN HIS SER CYS PRO THR GLY THR HIS HIS          
SEQRES  29 A  372  HIS HIS HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  372  GLU THR GLY ASP HIS ARG SER LEU LYS ARG ALA ASN LEU          
SEQRES   2 B  372  ALA ASN THR SER ILE THR CYS ASN ASP GLY SER HIS ALA          
SEQRES   3 B  372  GLY PHE TYR LEU ARG LYS HIS PRO SER SER LYS LYS TRP          
SEQRES   4 B  372  ILE VAL LEU LEU GLU GLY GLY TRP HIS CYS PHE ASP VAL          
SEQRES   5 B  372  ARG SER CYS ARG SER ARG TRP MET ARG LEU ARG HIS LEU          
SEQRES   6 B  372  MET THR SER SER GLN TRP PRO GLU THR ARG ASP VAL GLY          
SEQRES   7 B  372  GLY ILE LEU SER PRO HIS PRO GLU GLU ASN PRO TYR TRP          
SEQRES   8 B  372  HIS ASN ALA ASN HIS VAL LEU ILE PRO TYR CYS SER SER          
SEQRES   9 B  372  ASP SER TRP SER GLY THR ARG THR GLU PRO ASP THR SER          
SEQRES  10 B  372  ASP ARG GLU ASN SER TRP ARG PHE MET GLY ALA LEU ILE          
SEQRES  11 B  372  LEU ARG GLN VAL ILE ALA GLU LEU ILE PRO VAL GLY LEU          
SEQRES  12 B  372  GLY ARG VAL PRO GLY GLY GLU LEU MET LEU VAL GLY SER          
SEQRES  13 B  372  SER ALA GLY GLY MET GLY VAL MET LEU ASN LEU ASP ARG          
SEQRES  14 B  372  ILE ARG ASP PHE LEU VAL ASN GLU LYS LYS LEU GLN ILE          
SEQRES  15 B  372  THR VAL ARG GLY VAL SER ASP SER GLY TRP PHE LEU ASP          
SEQRES  16 B  372  ARG GLU PRO TYR THR PRO ALA ALA VAL ALA SER ASN GLU          
SEQRES  17 B  372  ALA VAL ARG GLN GLY TRP LYS LEU TRP GLN GLY LEU LEU          
SEQRES  18 B  372  PRO GLU GLU CYS THR LYS SER TYR PRO THR GLU PRO TRP          
SEQRES  19 B  372  ARG CYS TYR TYR GLY TYR ARG LEU TYR PRO THR LEU LYS          
SEQRES  20 B  372  THR PRO LEU PHE VAL PHE GLN TRP LEU PHE ASP GLU ALA          
SEQRES  21 B  372  GLN MET ARG VAL ASP ASN VAL GLY ALA PRO VAL THR PRO          
SEQRES  22 B  372  GLN GLN TRP ASN TYR ILE HIS GLU MET GLY GLY ALA LEU          
SEQRES  23 B  372  ARG SER SER LEU ASP ASN VAL SER ALA VAL PHE ALA PRO          
SEQRES  24 B  372  SER CYS ILE GLY HIS GLY VAL LEU PHE LYS ARG ASP TRP          
SEQRES  25 B  372  VAL ASN ILE LYS ILE ASP ASP ILE SER LEU PRO SER ALA          
SEQRES  26 B  372  LEU ARG CYS TRP GLU HIS SER THR ARG SER GLY ASN ASN          
SEQRES  27 B  372  ASN GLY CYS GLY LEU ARG LEU LEU GLU ARG CYS SER TRP          
SEQRES  28 B  372  PRO GLN CYS ASN HIS SER CYS PRO THR GLY THR HIS HIS          
SEQRES  29 B  372  HIS HIS HIS HIS HIS HIS HIS HIS                              
HET    NAG  B1617      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  HOH   *14(H2 O)                                                     
HELIX    1   1 ASP A  131  LEU A  142  1                                  12    
HELIX    2   2 ARG A  143  MET A  146  5                                   4    
HELIX    3   3 GLY A  158  SER A  162  5                                   5    
HELIX    4   4 MET A  206  ILE A  219  1                                  14    
HELIX    5   5 SER A  237  ASN A  256  1                                  20    
HELIX    6   6 ALA A  285  GLN A  298  1                                  14    
HELIX    7   7 PRO A  302  TYR A  309  1                                   8    
HELIX    8   8 GLU A  312  TYR A  317  5                                   6    
HELIX    9   9 TYR A  318  TYR A  323  1                                   6    
HELIX   10  10 PRO A  324  LEU A  326  5                                   3    
HELIX   11  11 GLU A  339  ASN A  346  1                                   8    
HELIX   12  12 THR A  352  LEU A  370  1                                  19    
HELIX   13  13 LYS A  389  ASN A  394  5                                   6    
HELIX   14  14 LEU A  402  THR A  413  1                                  12    
HELIX   15  15 ASP B  131  LEU B  142  1                                  12    
HELIX   16  16 ARG B  143  MET B  146  5                                   4    
HELIX   17  17 GLY B  158  SER B  162  5                                   5    
HELIX   18  18 MET B  206  GLY B  222  1                                  17    
HELIX   19  19 SER B  237  ASN B  256  1                                  20    
HELIX   20  20 ALA B  285  GLN B  298  1                                  14    
HELIX   21  21 PRO B  302  LYS B  307  1                                   6    
HELIX   22  22 GLU B  312  TYR B  317  5                                   6    
HELIX   23  23 TYR B  318  TYR B  323  1                                   6    
HELIX   24  24 PRO B  324  LEU B  326  5                                   3    
HELIX   25  25 GLU B  339  ASN B  346  1                                   8    
HELIX   26  26 THR B  352  LEU B  370  1                                  19    
HELIX   27  27 LYS B  389  ASN B  394  5                                   6    
HELIX   28  28 LEU B  402  SER B  412  1                                  11    
SHEET    1  AA10 THR A 154  ARG A 155  0                                        
SHEET    2  AA10 LEU A  88  ASN A  92 -1  O  LEU A  88   N  ARG A 155           
SHEET    3  AA10 GLY A 107  ARG A 111 -1  O  PHE A 108   N  ALA A  91           
SHEET    4  AA10 ASN A 175  ILE A 179 -1  O  HIS A 176   N  ARG A 111           
SHEET    5  AA10 LYS A 118  LEU A 123  1  O  LYS A 118   N  ASN A 175           
SHEET    6  AA10 GLY A 229  SER A 236  1  O  GLU A 230   N  TRP A 119           
SHEET    7  AA10 ILE A 262  ASP A 269  1  O  THR A 263   N  LEU A 231           
SHEET    8  AA10 LEU A 330  PHE A 333  1  O  PHE A 331   N  SER A 268           
SHEET    9  AA10 VAL A 376  ALA A 378  1  N  PHE A 377   O  VAL A 332           
SHEET   10  AA10 ARG A 601  LEU A 603  1  O  LEU A 602   N  ALA A 378           
SHEET    1  AB 2 PHE A 337  ASP A 338  0                                        
SHEET    2  AB 2 ILE A 382  GLY A 383  1  N  GLY A 383   O  PHE A 337           
SHEET    1  AC 2 LYS A 396  ILE A 397  0                                        
SHEET    2  AC 2 ILE A 400  SER A 401 -1  O  ILE A 400   N  ILE A 397           
SHEET    1  BA10 THR B 154  ARG B 155  0                                        
SHEET    2  BA10 LEU B  88  ASN B  92 -1  O  LEU B  88   N  ARG B 155           
SHEET    3  BA10 GLY B 107  ARG B 111 -1  O  PHE B 108   N  ALA B  91           
SHEET    4  BA10 ASN B 175  ILE B 179 -1  O  HIS B 176   N  ARG B 111           
SHEET    5  BA10 LYS B 118  LEU B 123  1  O  LYS B 118   N  ASN B 175           
SHEET    6  BA10 GLY B 229  SER B 236  1  O  GLU B 230   N  TRP B 119           
SHEET    7  BA10 ILE B 262  ASP B 269  1  O  THR B 263   N  LEU B 231           
SHEET    8  BA10 LEU B 330  PHE B 333  1  O  PHE B 331   N  SER B 268           
SHEET    9  BA10 VAL B 376  ALA B 378  1  N  PHE B 377   O  VAL B 332           
SHEET   10  BA10 ARG B 601  LEU B 603  1  O  LEU B 602   N  ALA B 378           
SHEET    1  BB 2 PHE B 337  ASP B 338  0                                        
SHEET    2  BB 2 ILE B 382  GLY B 383  1  N  GLY B 383   O  PHE B 337           
SHEET    1  BC 2 LYS B 396  ILE B 397  0                                        
SHEET    2  BC 2 ILE B 400  SER B 401 -1  O  ILE B 400   N  ILE B 397           
SSBOND   1 CYS A  100    CYS A  182                          1555   1555  2.09  
SSBOND   2 CYS A  129    CYS A  135                          1555   1555  2.07  
SSBOND   3 CYS A  305    CYS A  316                          1555   1555  2.04  
SSBOND   4 CYS A  381    CYS A  615                          1555   1555  2.06  
SSBOND   5 CYS A  606    CYS A  611                          1555   1555  2.04  
SSBOND   6 CYS B  100    CYS B  182                          1555   1555  2.07  
SSBOND   7 CYS B  129    CYS B  135                          1555   1555  2.08  
SSBOND   8 CYS B  305    CYS B  316                          1555   1555  2.09  
SSBOND   9 CYS B  381    CYS B  615                          1555   1555  2.06  
SSBOND  10 CYS B  606    CYS B  611                          1555   1555  2.04  
LINK         ND2 ASN B  95                 C1  NAG B1617     1555   1555  1.45  
SITE     1 AC1  3 ASN B  95  SER B  97  ILE B  98                               
CRYST1   59.388   81.394   86.945  90.00 105.54  90.00 P 1 21 1      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      0.016838  0.000000  0.004682        0.00000                         
SCALE2      0.000000  0.012286  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011938        0.00000                         
MTRIX1   1 -1.000000 -0.010000 -0.011000      -25.59700                         
MTRIX2   1  0.002000 -0.829000  0.560000      -32.52700                         
MTRIX3   1 -0.015000  0.560000  0.829000        9.40500                         
TER    2736      THR A 617                                                      
TER    5471      PRO B 616                                                      
MASTER      452    0    1   28   28    0    1    9 5497    2   35   58          
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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