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Database: PDB
Entry: 4CNC
LinkDB: 4CNC
Original site: 4CNC 
HEADER    CELL ADHESION                           21-JAN-14   4CNC              
TITLE     CRYSTAL STRUCTURE OF HUMAN 5T4 (WNT-ACTIVATED INHIBITORY FACTOR 1,    
TITLE    2 TROPHOBLAST GLYCOPROTEIN)                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TROPHOBLAST GLYCOPROTEIN;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 60-345;                     
COMPND   5 SYNONYM: 5T4 ONCOFETAL ANTIGEN, 5T4 ONCOFETAL TROPHOBLAST            
COMPND   6 GLYCOPROTEIN, 5T4 ONCOTROPHOBLAST GLYCOPROTEIN, M6P1,5T4, WNT-       
COMPND   7 ACTIVATED INHIBITORY FACTOR 1;                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ATCC: CRL-3022;                                                      
SOURCE   6 ORGAN: KIDNEY;                                                       
SOURCE   7 TISSUE: EMBRYONIC KIDNEY;                                            
SOURCE   8 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   9 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_VECTOR: PURD;                                      
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PURD-5T4/WAIF1ECTO                        
KEYWDS    CELL ADHESION, WAIF1, TPBG, TROVAX, CANCER, SIGNALING, LEUCINE-RICH   
KEYWDS   2 REPEATS, WNT/BETA-CATENIN SIGNALING PATHWAY                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,T.MALINAUSKAS,K.HARLOS,E.Y.JONES                               
REVDAT   4   08-MAY-19 4CNC    1       REMARK LINK                              
REVDAT   3   23-APR-14 4CNC    1       JRNL                                     
REVDAT   2   12-MAR-14 4CNC    1       JRNL                                     
REVDAT   1   26-FEB-14 4CNC    0                                                
JRNL        AUTH   Y.ZHAO,T.MALINAUSKAS,K.HARLOS,E.Y.JONES                      
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE INHIBITION OF WNT SIGNALING BY  
JRNL        TITL 2 CANCER ANTIGEN 5T4/WNT-ACTIVATED INHIBITORY FACTOR 1.        
JRNL        REF    STRUCTURE                     V.  22   612 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   24582434                                                     
JRNL        DOI    10.1016/J.STR.2014.01.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 56784                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3022                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4125                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 230                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 257                                     
REMARK   3   SOLVENT ATOMS            : 179                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.10000                                             
REMARK   3    B22 (A**2) : -0.77000                                             
REMARK   3    B33 (A**2) : 1.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.104         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4615 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4413 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6294 ; 1.905 ; 2.037       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10062 ; 0.917 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   549 ; 6.314 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;35.632 ;23.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   714 ;12.937 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;17.533 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   762 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5138 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   971 ; 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):  2208 ; 1.838 ; 2.074       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2207 ; 1.829 ; 2.073       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2753 ; 2.694 ; 3.099       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2407 ; 3.597 ; 2.815       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    60        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3101  -0.7738  31.0497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0525 T22:   0.0350                                     
REMARK   3      T33:   0.0261 T12:  -0.0053                                     
REMARK   3      T13:   0.0038 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2509 L22:   1.6120                                     
REMARK   3      L33:   0.3831 L12:  -0.6994                                     
REMARK   3      L13:  -0.2357 L23:   0.1783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:  -0.0649 S13:  -0.0388                       
REMARK   3      S21:   0.0409 S22:   0.0138 S23:   0.1957                       
REMARK   3      S31:  -0.0004 S32:   0.0159 S33:   0.0149                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    60        B   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7613  22.8682  -1.7139              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.0617                                     
REMARK   3      T33:   0.0145 T12:   0.0077                                     
REMARK   3      T13:   0.0010 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0624 L22:   0.9721                                     
REMARK   3      L33:   0.2682 L12:  -0.3404                                     
REMARK   3      L13:   0.0437 L23:   0.0913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0132 S12:  -0.0965 S13:   0.0134                       
REMARK   3      S21:   0.0020 S22:   0.0023 S23:  -0.0904                       
REMARK   3      S31:  -0.0014 S32:   0.0003 S33:   0.0109                       
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 RIDING   
REMARK   3  POSITIONS. U VALUES WITH TLS ADDED.                                 
REMARK   4                                                                      
REMARK   4 4CNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059419.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 1.06                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : KIRKPATRICK BAEZ BIMORPH MIRROR    
REMARK 200                                   PAIR FOR HORIZONTAL AND VERTICAL   
REMARK 200                                   FOCUSSING                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59830                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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: 5T4, CRYSTAL FORM WITH 1 MOLECULE IN THE             
REMARK 200  ASYMMETRIC UNIT                                                     
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTALLIZATION SITTING DROP         
REMARK 280  CONTAINED 100 NL OF CONCENTRATED 5T4/WAIF1 (5 MG/ML IN 20 MM        
REMARK 280  TRIS-HCL, PH 7.5, 150 MM NACL) PLUS 100 NL OF 0.2 M (NH4)2SO4,      
REMARK 280  30 % W/V PEG 4000., VAPOR DIFFUSION, SITTING DROP                   
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       47.91000            
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    57                                                      
REMARK 465     THR A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     SER A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     SER A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     ASP A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLN A   191                                                      
REMARK 465     ASN A   192                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     THR A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     THR A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     GLN A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     ALA A   353                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     ALA A   355                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     THR B    58                                                      
REMARK 465     GLY B    59                                                      
REMARK 465     GLU B   187                                                      
REMARK 465     ASP B   188                                                      
REMARK 465     GLU B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLN B   191                                                      
REMARK 465     ASN B   192                                                      
REMARK 465     ARG B   193                                                      
REMARK 465     ASP B   345                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     THR B   347                                                      
REMARK 465     GLU B   348                                                      
REMARK 465     THR B   349                                                      
REMARK 465     SER B   350                                                      
REMARK 465     GLN B   351                                                      
REMARK 465     VAL B   352                                                      
REMARK 465     ALA B   353                                                      
REMARK 465     PRO B   354                                                      
REMARK 465     ALA B   355                                                      
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     ASP A  60    CG   OD1  OD2                                       
REMARK 470     ARG A 114    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 114    CD   NE   CZ   NH1  NH2                             
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   O    VAL A    85     O    HOH A  2012              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU A    67     O    HOH A  2102     2656     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  62   N   -  CA  -  CB  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 292   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 299   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 240   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 319   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    CYS B 344   CA  -  CB  -  SG  ANGL. DEV. =   6.7 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    CYS A  62      118.53    116.36                                   
REMARK 500    ASP A  88       49.44   -108.26                                   
REMARK 500    ALA A 104      -59.81     62.41                                   
REMARK 500    LEU A 209       46.61    -89.67                                   
REMARK 500    LEU A 217       38.32   -140.07                                   
REMARK 500    LEU A 233       78.91   -118.62                                   
REMARK 500    ASN A 244     -156.08   -109.43                                   
REMARK 500    ASN A 268     -156.59   -104.36                                   
REMARK 500    ASP A 299     -168.82   -118.85                                   
REMARK 500    ASN B  81       37.10     39.26                                   
REMARK 500    ASP B  88       54.86    -97.40                                   
REMARK 500    ASN B 101     -169.99   -105.29                                   
REMARK 500    ALA B 104      -59.20     63.99                                   
REMARK 500    ASN B 244     -160.29   -114.00                                   
REMARK 500    THR B 250      134.52    -37.18                                   
REMARK 500    ASN B 268     -151.23   -100.11                                   
REMARK 500    ASP B 299     -162.18   -116.84                                   
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 B1360  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2074   O                                                      
REMARK 620 2 HOH B2063   O   108.9                                              
REMARK 620 3 HOH B2064   O   109.5 123.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1349                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1351                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1351                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1359                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1360                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1359                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1345 bound   
REMARK 800  to ASN A 81                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1346 through NAG A1347 bound to ASN A 124                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1348 bound   
REMARK 800  to ASN A 243                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1349 bound   
REMARK 800  to ASN A 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1350 bound   
REMARK 800  to ASN B 81                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1345 through NAG B1346 bound to ASN B 124                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG B1347 bound   
REMARK 800  to ASN B 243                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG B1348 bound   
REMARK 800  to ASN B 256                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CNM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN 5T4 (WNT-ACTIVATED INHIBITORY FACTOR 1,   
REMARK 900 TROPHOBLAST GLYCOPROTEIN)                                            
DBREF  4CNC A   60   345  UNP    Q13641   TPBG_HUMAN      60    345             
DBREF  4CNC B   60   345  UNP    Q13641   TPBG_HUMAN      60    345             
SEQADV 4CNC GLU A   57  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR A   58  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLY A   59  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLY A  346  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR A  347  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLU A  348  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR A  349  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC SER A  350  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLN A  351  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC VAL A  352  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC ALA A  353  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC PRO A  354  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC ALA A  355  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLU B   57  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR B   58  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLY B   59  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLY B  346  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR B  347  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLU B  348  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC THR B  349  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC SER B  350  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC GLN B  351  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC VAL B  352  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC ALA B  353  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC PRO B  354  UNP  Q13641              EXPRESSION TAG                 
SEQADV 4CNC ALA B  355  UNP  Q13641              EXPRESSION TAG                 
SEQRES   1 A  299  GLU THR GLY ASP GLN CYS PRO ALA LEU CYS GLU CYS SER          
SEQRES   2 A  299  GLU ALA ALA ARG THR VAL LYS CYS VAL ASN ARG ASN LEU          
SEQRES   3 A  299  THR GLU VAL PRO THR ASP LEU PRO ALA TYR VAL ARG ASN          
SEQRES   4 A  299  LEU PHE LEU THR GLY ASN GLN LEU ALA VAL LEU PRO ALA          
SEQRES   5 A  299  GLY ALA PHE ALA ARG ARG PRO PRO LEU ALA GLU LEU ALA          
SEQRES   6 A  299  ALA LEU ASN LEU SER GLY SER ARG LEU ASP GLU VAL ARG          
SEQRES   7 A  299  ALA GLY ALA PHE GLU HIS LEU PRO SER LEU ARG GLN LEU          
SEQRES   8 A  299  ASP LEU SER HIS ASN PRO LEU ALA ASP LEU SER PRO PHE          
SEQRES   9 A  299  ALA PHE SER GLY SER ASN ALA SER VAL SER ALA PRO SER          
SEQRES  10 A  299  PRO LEU VAL GLU LEU ILE LEU ASN HIS ILE VAL PRO PRO          
SEQRES  11 A  299  GLU ASP GLU ARG GLN ASN ARG SER PHE GLU GLY MET VAL          
SEQRES  12 A  299  VAL ALA ALA LEU LEU ALA GLY ARG ALA LEU GLN GLY LEU          
SEQRES  13 A  299  ARG ARG LEU GLU LEU ALA SER ASN HIS PHE LEU TYR LEU          
SEQRES  14 A  299  PRO ARG ASP VAL LEU ALA GLN LEU PRO SER LEU ARG HIS          
SEQRES  15 A  299  LEU ASP LEU SER ASN ASN SER LEU VAL SER LEU THR TYR          
SEQRES  16 A  299  VAL SER PHE ARG ASN LEU THR HIS LEU GLU SER LEU HIS          
SEQRES  17 A  299  LEU GLU ASP ASN ALA LEU LYS VAL LEU HIS ASN GLY THR          
SEQRES  18 A  299  LEU ALA GLU LEU GLN GLY LEU PRO HIS ILE ARG VAL PHE          
SEQRES  19 A  299  LEU ASP ASN ASN PRO TRP VAL CYS ASP CYS HIS MET ALA          
SEQRES  20 A  299  ASP MET VAL THR TRP LEU LYS GLU THR GLU VAL VAL GLN          
SEQRES  21 A  299  GLY LYS ASP ARG LEU THR CYS ALA TYR PRO GLU LYS MET          
SEQRES  22 A  299  ARG ASN ARG VAL LEU LEU GLU LEU ASN SER ALA ASP LEU          
SEQRES  23 A  299  ASP CYS ASP GLY THR GLU THR SER GLN VAL ALA PRO ALA          
SEQRES   1 B  299  GLU THR GLY ASP GLN CYS PRO ALA LEU CYS GLU CYS SER          
SEQRES   2 B  299  GLU ALA ALA ARG THR VAL LYS CYS VAL ASN ARG ASN LEU          
SEQRES   3 B  299  THR GLU VAL PRO THR ASP LEU PRO ALA TYR VAL ARG ASN          
SEQRES   4 B  299  LEU PHE LEU THR GLY ASN GLN LEU ALA VAL LEU PRO ALA          
SEQRES   5 B  299  GLY ALA PHE ALA ARG ARG PRO PRO LEU ALA GLU LEU ALA          
SEQRES   6 B  299  ALA LEU ASN LEU SER GLY SER ARG LEU ASP GLU VAL ARG          
SEQRES   7 B  299  ALA GLY ALA PHE GLU HIS LEU PRO SER LEU ARG GLN LEU          
SEQRES   8 B  299  ASP LEU SER HIS ASN PRO LEU ALA ASP LEU SER PRO PHE          
SEQRES   9 B  299  ALA PHE SER GLY SER ASN ALA SER VAL SER ALA PRO SER          
SEQRES  10 B  299  PRO LEU VAL GLU LEU ILE LEU ASN HIS ILE VAL PRO PRO          
SEQRES  11 B  299  GLU ASP GLU ARG GLN ASN ARG SER PHE GLU GLY MET VAL          
SEQRES  12 B  299  VAL ALA ALA LEU LEU ALA GLY ARG ALA LEU GLN GLY LEU          
SEQRES  13 B  299  ARG ARG LEU GLU LEU ALA SER ASN HIS PHE LEU TYR LEU          
SEQRES  14 B  299  PRO ARG ASP VAL LEU ALA GLN LEU PRO SER LEU ARG HIS          
SEQRES  15 B  299  LEU ASP LEU SER ASN ASN SER LEU VAL SER LEU THR TYR          
SEQRES  16 B  299  VAL SER PHE ARG ASN LEU THR HIS LEU GLU SER LEU HIS          
SEQRES  17 B  299  LEU GLU ASP ASN ALA LEU LYS VAL LEU HIS ASN GLY THR          
SEQRES  18 B  299  LEU ALA GLU LEU GLN GLY LEU PRO HIS ILE ARG VAL PHE          
SEQRES  19 B  299  LEU ASP ASN ASN PRO TRP VAL CYS ASP CYS HIS MET ALA          
SEQRES  20 B  299  ASP MET VAL THR TRP LEU LYS GLU THR GLU VAL VAL GLN          
SEQRES  21 B  299  GLY LYS ASP ARG LEU THR CYS ALA TYR PRO GLU LYS MET          
SEQRES  22 B  299  ARG ASN ARG VAL LEU LEU GLU LEU ASN SER ALA ASP LEU          
SEQRES  23 B  299  ASP CYS ASP GLY THR GLU THR SER GLN VAL ALA PRO ALA          
MODRES 4CNC ASN A   81  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN A  124  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN A  243  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN A  256  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN B   81  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN B  124  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN B  243  ASN  GLYCOSYLATION SITE                                 
MODRES 4CNC ASN B  256  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1345      14                                                       
HET    NAG  A1346      14                                                       
HET    NAG  A1347      14                                                       
HET    NAG  A1348      14                                                       
HET    NAG  A1349      14                                                       
HET    NAG  A1350      14                                                       
HET    PEG  A1351       7                                                       
HET    GOL  A1352       6                                                       
HET    SO4  A1353       5                                                       
HET    SO4  A1354       5                                                       
HET    SO4  A1355       5                                                       
HET    SO4  A1356       5                                                       
HET    SO4  A1357       5                                                       
HET    SO4  A1358       5                                                       
HET    SO4  A1359       5                                                       
HET    SO4  A1360       5                                                       
HET    NAG  B1345      14                                                       
HET    NAG  B1346      14                                                       
HET    NAG  B1347      14                                                       
HET    NAG  B1348      14                                                       
HET    PEG  B1349       7                                                       
HET    PEG  B1350       7                                                       
HET    PEG  B1351       7                                                       
HET    GOL  B1352       6                                                       
HET    GOL  B1353       6                                                       
HET    SO4  B1354       5                                                       
HET    SO4  B1355       5                                                       
HET    SO4  B1356       5                                                       
HET    SO4  B1357       5                                                       
HET    SO4  B1358       5                                                       
HET    SO4  B1359       5                                                       
HET     NA  B1360       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    10(C8 H15 N O6)                                              
FORMUL   8  PEG    4(C4 H10 O3)                                                 
FORMUL   9  GOL    3(C3 H8 O3)                                                  
FORMUL  10  SO4    14(O4 S 2-)                                                  
FORMUL  32   NA    NA 1+                                                        
FORMUL  33  HOH   *179(H2 O)                                                    
HELIX    1   1 SER A  194  ALA A  205  1                                  12    
HELIX    2   2 GLY A  206  ALA A  208  5                                   3    
HELIX    3   3 PRO A  226  LEU A  233  1                                   8    
HELIX    4   4 HIS A  274  GLY A  283  1                                  10    
HELIX    5   5 ASP A  299  HIS A  301  5                                   3    
HELIX    6   6 MET A  302  THR A  312  1                                  11    
HELIX    7   7 GLY A  317  LEU A  321  5                                   5    
HELIX    8   8 PRO A  326  ARG A  330  5                                   5    
HELIX    9   9 LEU A  334  LEU A  337  5                                   4    
HELIX   10  10 ASN A  338  LEU A  342  5                                   5    
HELIX   11  11 SER B  194  ALA B  205  1                                  12    
HELIX   12  12 GLY B  206  ALA B  208  5                                   3    
HELIX   13  13 PRO B  226  LEU B  233  1                                   8    
HELIX   14  14 SER B  253  LEU B  257  5                                   5    
HELIX   15  15 HIS B  274  GLN B  282  1                                   9    
HELIX   16  16 ASP B  299  HIS B  301  5                                   3    
HELIX   17  17 MET B  302  THR B  312  1                                  11    
HELIX   18  18 GLY B  317  LEU B  321  5                                   5    
HELIX   19  19 PRO B  326  ARG B  330  5                                   5    
HELIX   20  20 LEU B  334  LEU B  337  5                                   4    
HELIX   21  21 ASN B  338  LEU B  342  5                                   5    
SHEET    1  AA11 GLU A  67  SER A  69  0                                        
SHEET    2  AA11 THR A  74  LYS A  76 -1  O  THR A  74   N  SER A  69           
SHEET    3  AA11 ASN A  95  PHE A  97  1  O  ASN A  95   N  VAL A  75           
SHEET    4  AA11 ALA A 122  ASN A 124  1  O  ALA A 122   N  LEU A  96           
SHEET    5  AA11 GLN A 146  ASP A 148  1  O  GLN A 146   N  LEU A 123           
SHEET    6  AA11 GLU A 177  ILE A 179  1  O  GLU A 177   N  LEU A 147           
SHEET    7  AA11 ARG A 214  GLU A 216  1  O  ARG A 214   N  LEU A 178           
SHEET    8  AA11 HIS A 238  ASP A 240  1  O  HIS A 238   N  LEU A 215           
SHEET    9  AA11 SER A 262  HIS A 264  1  O  SER A 262   N  LEU A 239           
SHEET   10  AA11 ARG A 288  PHE A 290  1  O  ARG A 288   N  LEU A 263           
SHEET   11  AA11 VAL A 315  GLN A 316  1  N  GLN A 316   O  VAL A 289           
SHEET    1  AB 3 ALA A 104  LEU A 106  0                                        
SHEET    2  AB 3 LEU A 130  VAL A 133  1  N  ASP A 131   O  ALA A 104           
SHEET    3  AB 3 ASP A 156  LEU A 157  1  O  ASP A 156   N  VAL A 133           
SHEET    1  AC 2 TRP A 296  VAL A 297  0                                        
SHEET    2  AC 2 CYS A 323  TYR A 325  1  N  ALA A 324   O  TRP A 296           
SHEET    1  BA11 GLU B  67  SER B  69  0                                        
SHEET    2  BA11 THR B  74  LYS B  76 -1  O  THR B  74   N  SER B  69           
SHEET    3  BA11 ASN B  95  PHE B  97  1  O  ASN B  95   N  VAL B  75           
SHEET    4  BA11 ALA B 122  ASN B 124  1  O  ALA B 122   N  LEU B  96           
SHEET    5  BA11 GLN B 146  ASP B 148  1  O  GLN B 146   N  LEU B 123           
SHEET    6  BA11 GLU B 177  ILE B 179  1  O  GLU B 177   N  LEU B 147           
SHEET    7  BA11 ARG B 214  GLU B 216  1  O  ARG B 214   N  LEU B 178           
SHEET    8  BA11 HIS B 238  ASP B 240  1  O  HIS B 238   N  LEU B 215           
SHEET    9  BA11 SER B 262  HIS B 264  1  O  SER B 262   N  LEU B 239           
SHEET   10  BA11 ARG B 288  PHE B 290  1  O  ARG B 288   N  LEU B 263           
SHEET   11  BA11 VAL B 315  GLN B 316  1  N  GLN B 316   O  VAL B 289           
SHEET    1  BB 3 ALA B 104  LEU B 106  0                                        
SHEET    2  BB 3 LEU B 130  VAL B 133  1  N  ASP B 131   O  ALA B 104           
SHEET    3  BB 3 ASP B 156  LEU B 157  1  O  ASP B 156   N  VAL B 133           
SHEET    1  BC 2 TRP B 296  VAL B 297  0                                        
SHEET    2  BC 2 CYS B 323  TYR B 325  1  N  ALA B 324   O  TRP B 296           
SSBOND   1 CYS A   62    CYS A   68                          1555   1555  2.11  
SSBOND   2 CYS A   66    CYS A   77                          1555   1555  2.02  
SSBOND   3 CYS A  298    CYS A  323                          1555   1555  2.05  
SSBOND   4 CYS A  300    CYS A  344                          1555   1555  2.08  
SSBOND   5 CYS B   62    CYS B   68                          1555   1555  2.13  
SSBOND   6 CYS B   66    CYS B   77                          1555   1555  2.01  
SSBOND   7 CYS B  298    CYS B  323                          1555   1555  2.06  
SSBOND   8 CYS B  300    CYS B  344                          1555   1555  2.10  
LINK         ND2 ASN A  81                 C1  NAG A1345     1555   1555  1.44  
LINK         ND2 ASN A 124                 C1  NAG A1346     1555   1555  1.42  
LINK         ND2 ASN A 243                 C1  NAG A1348     1555   1555  1.46  
LINK         ND2 ASN A 256                 C1  NAG A1349     1555   1555  1.46  
LINK         O4  NAG A1346                 C1  NAG A1347     1555   1555  1.43  
LINK         ND2 ASN B  81                 C1  NAG A1350     1555   1555  1.45  
LINK         ND2 ASN B 124                 C1  NAG B1345     1555   1555  1.43  
LINK         ND2 ASN B 243                 C1  NAG B1347     1555   1555  1.45  
LINK         ND2 ASN B 256                 C1  NAG B1348     1555   1555  1.44  
LINK         O4  NAG B1345                 C1  NAG B1346     1555   1555  1.43  
LINK        NA    NA B1360                 O   HOH B2074     1555   1555  3.07  
LINK        NA    NA B1360                 O   HOH B2063     1555   1555  2.60  
LINK        NA    NA B1360                 O   HOH B2064     1555   1555  2.65  
CISPEP   1 ARG A  114    PRO A  115          0        -6.38                     
CISPEP   2 TYR A  325    PRO A  326          0        -7.49                     
CISPEP   3 ARG B  114    PRO B  115          0        -6.48                     
CISPEP   4 TYR B  325    PRO B  326          0        -9.64                     
SITE     1 AC1  3 GLN B  61  CYS B  62  CYS B  68                               
SITE     1 AC2  3 PHE B 138  HIS B 140  LEU B 141                               
SITE     1 AC3  6 ALA A 303  THR A 307  LYS A 310  SER A 339                    
SITE     2 AC3  6 LEU A 342  HOH A2102                                          
SITE     1 AC4  4 ALA B 121  ARG B 145  GLU B 177  SO4 B1358                    
SITE     1 AC5  6 SER A 126  ASP A 148  SER A 150  HIS A 151                    
SITE     2 AC5  6 ASN A 181  NAG A1346                                          
SITE     1 AC6  5 ASP B 148  SER B 150  ASN B 181  NAG B1345                    
SITE     2 AC6  5 NAG B1346                                                     
SITE     1 AC7  2 ASP B  60  GLN B  61                                          
SITE     1 AC8  5 ARG A 214  HIS A 238  SER A 262  HIS A 264                    
SITE     2 AC8  5 ARG A 288                                                     
SITE     1 AC9  4 ARG A 213  HIS A 238  GLU A 261  HOH A2105                    
SITE     1 BC1  2 PRO A 186  GLU A 187                                          
SITE     1 BC2  4 SER A  69  GLU A  70  ALA A  71  HOH A2006                    
SITE     1 BC3  3 PRO A 107  ALA A 108  ARG A 134                               
SITE     1 BC4  3 SER B  69  GLU B  70  ALA B  71                               
SITE     1 BC5  5 ARG B 214  HIS B 238  SER B 262  HIS B 264                    
SITE     2 BC5  5 ARG B 288                                                     
SITE     1 BC6  5 PRO B 107  ALA B 108  ARG B 134  ARG B 320                    
SITE     2 BC6  5 HOH B2019                                                     
SITE     1 BC7  3 SER B 253  PHE B 254  ARG B 255                               
SITE     1 BC8  5 SER A 194  PHE A 195  GLU A 196  HOH A2050                    
SITE     2 BC8  5 HOH A2061                                                     
SITE     1 BC9  3 THR A 312  LYS A 318  HOH A2095                               
SITE     1 CC1  4 ARG B 213  ARG B 214  HIS B 238  PEG B1351                    
SITE     1 CC2  4 ASN A  79  ARG B 213  ARG B 237  GLU B 261                    
SITE     1 CC3  2 HIS B 301  HOH B2062                                          
SITE     1 CC4  5 THR B 307  LYS B 310  HOH B2063  HOH B2064                    
SITE     2 CC4  5 HOH B2074                                                     
SITE     1 CC5  5 ASN A  79  ASN A  81  HIS B 238  GLU B 261                    
SITE     2 CC5  5 ARG B 288                                                     
SITE     1 CC6  7 PHE A  97  THR A  99  ASN A 124  GLN A 146                    
SITE     2 CC6  7 ASP A 148  GOL A1352  HOH A2038                               
SITE     1 CC7  3 SER A 219  HIS A 221  ASN A 243                               
SITE     1 CC8  3 ARG A 255  ASN A 256  HOH A2104                               
SITE     1 CC9  9 HIS A 238  GLU A 261  HIS A 286  ARG A 288                    
SITE     2 CC9  9 HOH A2074  HOH A2083  ASN B  79  ASN B  81                    
SITE     3 CC9  9 GLN B 102                                                     
SITE     1 DC1  6 PHE B  97  THR B  99  ASN B 124  GLN B 146                    
SITE     2 DC1  6 ASP B 148  GOL B1352                                          
SITE     1 DC2  5 HIS B 182  SER B 219  HIS B 221  ASN B 243                    
SITE     2 DC2  5 HOH B2043                                                     
SITE     1 DC3  5 LEU B 230  ALA B 231  SER B 253  ARG B 255                    
SITE     2 DC3  5 ASN B 256                                                     
CRYST1   49.600   95.820   65.970  90.00  91.14  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      0.020161  0.000000  0.000401        0.00000                         
SCALE2      0.000000  0.010436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015161        0.00000                         
MTRIX1   1 -0.999900 -0.009900 -0.009200       24.07850    1                    
MTRIX2   1  0.010600 -0.997400 -0.071200       21.88560    1                    
MTRIX3   1 -0.008500 -0.071300  0.997400       34.12350    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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