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Database: PDB
Entry: 2YGO
LinkDB: 2YGO
Original site: 2YGO 
HEADER    SIGNALING PROTEIN                       19-APR-11   2YGO              
TITLE     WIF DOMAIN-EGF-LIKE DOMAIN 1 OF HUMAN WNT INHIBITORY FACTOR           
TITLE    2 1 IN COMPLEX WITH 1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: WNT INHIBITORY FACTOR 1;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: WIF DOMAIN-EGF-LIKE DOMAIN 1, RESIDUES 35-210;             
COMPND   5 SYNONYM: WIF-1;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: N-ACETYLGLUCOSAMINYLTRANSFERASE         
SOURCE   9  I-NEGATIVE HEK 293S GNTI(-)CELLS;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PHLSEC                                     
KEYWDS    SIGNALING PROTEIN, WNT SIGNALING PATHWAY, WNT ANTAGONIST, MORPHOGEN,  
KEYWDS   2 CANCER, GLYCOSAMINOGLYCAN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MALINAUSKAS,A.R.ARICESCU,W.LU,C.SIEBOLD,E.Y.JONES                   
REVDAT   2   17-AUG-11 2YGO    1       JRNL                                     
REVDAT   1   13-JUL-11 2YGO    0                                                
JRNL        AUTH   T.MALINAUSKAS,A.R.ARICESCU,W.LU,C.SIEBOLD,E.Y.JONES          
JRNL        TITL   MODULAR MECHANISM OF WNT SIGNALING INHIBITION BY WNT         
JRNL        TITL 2 INHIBITORY FACTOR 1                                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   886 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21743455                                                     
JRNL        DOI    10.1038/NSMB.2081                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.850                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.422                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.00                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.26                          
REMARK   3   NUMBER OF REFLECTIONS             : 17107                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1856                          
REMARK   3   R VALUE            (WORKING SET) : 0.1839                          
REMARK   3   FREE R VALUE                     : 0.2168                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.2                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 886                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.4294 -  3.3610    1.00     3012   145  0.1772 0.1831        
REMARK   3     2  3.3610 -  2.6680    0.99     2856   151  0.1726 0.2168        
REMARK   3     3  2.6680 -  2.3308    0.96     2736   149  0.1853 0.2269        
REMARK   3     4  2.3308 -  2.1177    0.95     2681   160  0.1866 0.2320        
REMARK   3     5  2.1177 -  1.9659    0.91     2576   134  0.1931 0.2638        
REMARK   3     6  1.9659 -  1.8500    0.85     2360   147  0.2364 0.2787        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.346                                         
REMARK   3   B_SOL              : 44.411                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.24             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.04            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.9344                                               
REMARK   3    B22 (A**2) : -4.8759                                              
REMARK   3    B33 (A**2) : -1.0585                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.015           1508                                  
REMARK   3   ANGLE     :  2.069           2025                                  
REMARK   3   CHIRALITY :  0.152            216                                  
REMARK   3   PLANARITY :  0.008            255                                  
REMARK   3   DIHEDRAL  : 18.794            584                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1040 -13.2309  14.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0225 T22:   0.0237                                     
REMARK   3      T33:   0.0358 T12:  -0.0117                                     
REMARK   3      T13:  -0.0160 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9297 L22:   0.5518                                     
REMARK   3      L33:   1.0348 L12:   0.4263                                     
REMARK   3      L13:   0.0996 L23:  -0.0090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.0007 S13:   0.1715                       
REMARK   3      S21:  -0.0312 S22:   0.0257 S23:   0.0797                       
REMARK   3      S31:  -0.0979 S32:  -0.0863 S33:   0.0012                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2YGO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAY-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-48076.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY SIDE                  
REMARK 200                                   DIFFRACTING SILICON 111            
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18293                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.3                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.94                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M DIAMMONIUM TARTRATE, 100           
REMARK 280  MM BIS-TRIS PROPANE PH 7.0                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       25.49800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.49800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.49800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.49800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -50.99600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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    32                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     HIS A   219                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A    88     O5   NAG A  1214              2.15            
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    PRO A 201     -159.67    -80.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1215  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 190   O                                                      
REMARK 620 2 CYS A 186   O    90.4                                              
REMARK 620 3 HOH A2138   O    60.4  69.9                                        
REMARK 620 4 HOH A2137   O   161.5  75.0 122.5                                  
REMARK 620 5 HOH A2151   O    98.0 161.2  99.8  99.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PCF A1213                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1214                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YGQ   RELATED DB: PDB                                   
REMARK 900  WIF DOMAIN-EPIDERMAL GROWTH FACTOR (EGF)-LIKE DOMAINS               
REMARK 900  1-3 OF HUMAN WNT INHIBITORY FACTOR 1 IN COMPLEX                     
REMARK 900  WITH 1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE                             
REMARK 900 RELATED ID: 2YGP   RELATED DB: PDB                                   
REMARK 900  WIF DOMAIN-EGF-LIKE DOMAIN 1 MET77TRP OF HUMAN WNT                  
REMARK 900  INHIBITORY FACTOR 1 IN COMPLEX WITH 1,2-                            
REMARK 900  DIPALMITOYLPHOSPHATIDYLCHOLINE                                      
REMARK 900 RELATED ID: 2YGN   RELATED DB: PDB                                   
REMARK 900  WIF DOMAIN OF HUMAN WNT INHIBITORY FACTOR 1 IN                      
REMARK 900  COMPLEX WITH 1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ISOFORM Q166K. THE N-TERMINAL THREE AMINO ACID RESIDUES              
REMARK 999 (ETG) AND C-TERMINAL NINE AMINO ACID RESIDUES (GTKHHHHHH)            
REMARK 999 OF THE CRYSTALLISATION CONSTRUCT ARE DERIVED FROM THE                
REMARK 999 PHLSEC VECTOR.                                                       
DBREF  2YGO A   35   210  UNP    Q9Y5W5   WIF1_HUMAN      35    210             
SEQADV 2YGO GLU A   32  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO THR A   33  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO GLY A   34  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO MLY A  166  UNP  Q9Y5W5    GLN   166 VARIANT                        
SEQADV 2YGO GLY A  211  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO THR A  212  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO LYS A  213  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  214  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  215  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  216  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  217  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  218  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQADV 2YGO HIS A  219  UNP  Q9Y5W5              EXPRESSION TAG                 
SEQRES   1 A  188  GLU THR GLY SER LEU TYR LEU TRP ILE ASP ALA HIS GLN          
SEQRES   2 A  188  ALA ARG VAL LEU ILE GLY PHE GLU GLU ASP ILE LEU ILE          
SEQRES   3 A  188  VAL SER GLU GLY MLY MET ALA PRO PHE THR HIS ASP PHE          
SEQRES   4 A  188  ARG MLY ALA GLN GLN ARG MET PRO ALA ILE PRO VAL ASN          
SEQRES   5 A  188  ILE HIS SER MET ASN PHE THR TRP GLN ALA ALA GLY GLN          
SEQRES   6 A  188  ALA GLU TYR PHE TYR GLU PHE LEU SER LEU ARG SER LEU          
SEQRES   7 A  188  ASP MLY GLY ILE MET ALA ASP PRO THR VAL ASN VAL PRO          
SEQRES   8 A  188  LEU LEU GLY THR VAL PRO HIS MLY ALA SER VAL VAL GLN          
SEQRES   9 A  188  VAL GLY PHE PRO CYS LEU GLY MLY GLN ASP GLY VAL ALA          
SEQRES  10 A  188  ALA PHE GLU VAL ASP VAL ILE VAL MET ASN SER GLU GLY          
SEQRES  11 A  188  ASN THR ILE LEU MLY THR PRO GLN ASN ALA ILE PHE PHE          
SEQRES  12 A  188  LYS THR CYS GLN GLN ALA GLU CYS PRO GLY GLY CYS ARG          
SEQRES  13 A  188  ASN GLY GLY PHE CYS ASN GLU ARG ARG ILE CYS GLU CYS          
SEQRES  14 A  188  PRO ASP GLY PHE HIS GLY PRO HIS CYS GLU GLY THR LYS          
SEQRES  15 A  188  HIS HIS HIS HIS HIS HIS                                      
MODRES 2YGO MLY A   62  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2YGO MLY A   72  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2YGO MLY A  111  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2YGO MLY A  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2YGO MLY A  143  LYS  N-DIMETHYL-LYSINE                                  
MODRES 2YGO MLY A  166  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  A  62      11                                                       
HET    MLY  A  72      11                                                       
HET    MLY  A 111      11                                                       
HET    MLY  A 130      11                                                       
HET    MLY  A 143      11                                                       
HET    MLY  A 166      11                                                       
HET    PCF  A1213      50                                                       
HET    NAG  A1214      14                                                       
HET     NA  A1215       1                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM     PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE                            
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      NA SODIUM ION                                                       
FORMUL   2  MLY    6(C8 H18 N2 O2)                                              
FORMUL   3  PCF    C40 H80 N O8 P                                               
FORMUL   4  NAG    C8 H15 N O6                                                  
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *151(H2 O)                                                    
HELIX    1   1 ASP A   41  GLY A   50  1                                  10    
HELIX    2   2 PRO A   65  HIS A   68  5                                   4    
HELIX    3   3 ASP A   69  ARG A   76  1                                   8    
SHEET    1  AA 6 MLY A  62  MET A  63  0                                        
SHEET    2  AA 6 ILE A  55  SER A  59 -1  O  SER A  59   N  MLY A  62           
SHEET    3  AA 6 LEU A  36  ILE A  40 -1  O  LEU A  38   N  ILE A  57           
SHEET    4  AA 6 SER A  86  ALA A  93 -1  O  THR A  90   N  TRP A  39           
SHEET    5  AA 6 SER A 132  GLY A 137 -1  O  SER A 132   N  TRP A  91           
SHEET    6  AA 6 THR A 118  VAL A 119 -1  O  THR A 118   N  GLY A 137           
SHEET    1  AB 4 LEU A 124  THR A 126  0                                        
SHEET    2  AB 4 PHE A 100  SER A 108 -1  O  TYR A 101   N  GLY A 125           
SHEET    3  AB 4 GLY A 146  MET A 157 -1  O  GLU A 151   N  ARG A 107           
SHEET    4  AB 4 THR A 163  MLY A 166 -1  N  ILE A 164   O  VAL A 156           
SHEET    1  AC 4 LEU A 124  THR A 126  0                                        
SHEET    2  AC 4 PHE A 100  SER A 108 -1  O  TYR A 101   N  GLY A 125           
SHEET    3  AC 4 GLY A 146  MET A 157 -1  O  GLU A 151   N  ARG A 107           
SHEET    4  AC 4 PHE A 173  CYS A 177 -1  O  PHE A 173   N  PHE A 150           
SHEET    1  AD 2 THR A 163  MLY A 166  0                                        
SHEET    2  AD 2 GLY A 146  MET A 157 -1  O  VAL A 156   N  ILE A 164           
SHEET    1  AE 2 PHE A 191  CYS A 192  0                                        
SHEET    2  AE 2 CYS A 198  GLU A 199 -1  O  GLU A 199   N  PHE A 191           
SSBOND   1 CYS A  140    CYS A  177                          1555   1555  2.04  
SSBOND   2 CYS A  182    CYS A  192                          1555   1555  2.04  
SSBOND   3 CYS A  186    CYS A  198                          1555   1555  2.04  
SSBOND   4 CYS A  200    CYS A  209                          1555   1555  2.03  
LINK         C   GLY A  61                 N   MLY A  62     1555   1555  1.34  
LINK         C   MLY A  62                 N   MET A  63     1555   1555  1.34  
LINK         C   ARG A  71                 N   MLY A  72     1555   1555  1.34  
LINK         C   MLY A  72                 N   ALA A  73     1555   1555  1.35  
LINK         ND2 ASN A  88                 C1  NAG A1214     1555   1555  1.40  
LINK         C   ASP A 110                 N   MLY A 111     1555   1555  1.34  
LINK         C   MLY A 111                 N   GLY A 112     1555   1555  1.33  
LINK         C   HIS A 129                 N   MLY A 130     1555   1555  1.32  
LINK         C   MLY A 130                 N   ALA A 131     1555   1555  1.36  
LINK         C   GLY A 142                 N   MLY A 143     1555   1555  1.34  
LINK         C   MLY A 143                 N   GLN A 144     1555   1555  1.37  
LINK         C   LEU A 165                 N   MLY A 166     1555   1555  1.34  
LINK         C   MLY A 166                 N   THR A 167     1555   1555  1.34  
LINK        NA    NA A1215                 O   HOH A2151     1555   1555  2.40  
LINK        NA    NA A1215                 O   HOH A2137     1555   1555  2.45  
LINK        NA    NA A1215                 O   HOH A2138     1555   1555  2.70  
LINK        NA    NA A1215                 O   CYS A 186     1555   1555  2.39  
LINK        NA    NA A1215                 O   GLY A 190     1555   1555  2.73  
SITE     1 AC1 10 LEU A  48  ILE A  49  ILE A  55  ARG A  76                    
SITE     2 AC1 10 MET A  77  PRO A  78  PHE A  89  VAL A 156                    
SITE     3 AC1 10 PHE A 173  ARG A 196                                          
SITE     1 AC2  7 HIS A  43  GLN A  44  GLU A  52  ASN A  88                    
SITE     2 AC2  7 HOH A2008  HOH A2149  HOH A2150                               
SITE     1 AC3  5 CYS A 186  GLY A 190  HOH A2137  HOH A2138                    
SITE     2 AC3  5 HOH A2151                                                     
CRYST1   50.996  134.260   60.403  90.00  90.00  90.00 C 2 2 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      0.019609  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007448  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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