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Database: PDB
Entry: 5MW7
LinkDB: 5MW7
Original site: 5MW7 
HEADER    SIGNALING PROTEIN                       18-JAN-17   5MW7              
TITLE     HUMAN JAGGED2 C2-EGF3                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN JAGGED-2;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HJ2;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAG2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2;                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PEXS2-2                                   
KEYWDS    C2, EGF, NOTCH, SIGNALING, SIGNALING PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.SUCKLING,P.A.HANDFORD,S.M.LEA                                     
REVDAT   3   13-SEP-17 5MW7    1       REMARK                                   
REVDAT   2   09-AUG-17 5MW7    1       JRNL                                     
REVDAT   1   14-JUN-17 5MW7    0                                                
JRNL        AUTH   R.J.SUCKLING,B.KORONA,P.WHITEMAN,C.CHILLAKURI,L.HOLT,        
JRNL        AUTH 2 P.A.HANDFORD,S.M.LEA                                         
JRNL        TITL   STRUCTURAL AND FUNCTIONAL DISSECTION OF THE INTERPLAY        
JRNL        TITL 2 BETWEEN LIPID AND NOTCH BINDING BY HUMAN NOTCH LIGANDS.      
JRNL        REF    EMBO J.                       V.  36  2204 2017              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   28572448                                                     
JRNL        DOI    10.15252/EMBJ.201796632                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.25                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 8975                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.258                           
REMARK   3   R VALUE            (WORKING SET) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 454                             
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 60.2645 -  4.0382    0.98     2943   142  0.2401 0.2836        
REMARK   3     2  4.0382 -  3.2053    1.00     2790   173  0.2486 0.3189        
REMARK   3     3  3.2053 -  2.8001    0.99     2788   139  0.3016 0.3692        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           2348                                  
REMARK   3   ANGLE     :  0.662           3191                                  
REMARK   3   CHIRALITY :  0.043            318                                  
REMARK   3   PLANARITY :  0.007            422                                  
REMARK   3   DIHEDRAL  : 16.739           1400                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5MW7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003112.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8975                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.26700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.11600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 4CC1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-5000 MME, SODIUM CITRATE, PH 5.3,    
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.40700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.17850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.60250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.17850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.40700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.60250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 160 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 17890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     ARG A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     HIS A    64                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     THR A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     CYS A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     TYR A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     GLY A   341                                                      
REMARK 465     ARG A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     CYS A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     LYS A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     GLY A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     HIS A   351                                                      
REMARK 465     HIS A   352                                                      
REMARK 465     HIS A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     HIS A   356                                                      
REMARK 465     HIS A   357                                                      
REMARK 465     HIS A   358                                                      
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   OG1  THR A   322     C1   FUC A   401              1.10            
REMARK 500   OG1  THR A   322     O5   FUC A   401              2.06            
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    GLN A  79     -149.58   -119.43                                   
REMARK 500    LYS A  81      -44.85     73.16                                   
REMARK 500    ALA A 108     -122.96   -109.21                                   
REMARK 500    ALA A 110       43.09    -75.76                                   
REMARK 500    ARG A 118       16.91   -140.13                                   
REMARK 500    ALA A 119       56.84   -157.06                                   
REMARK 500    ASP A 124       89.95    -59.14                                   
REMARK 500    GLN A 125       46.31    -69.99                                   
REMARK 500    ARG A 140      -55.11     67.18                                   
REMARK 500    ASP A 152      -51.18   -129.80                                   
REMARK 500    HIS A 168      115.75   -164.59                                   
REMARK 500    PRO A 174       76.40    -59.01                                   
REMARK 500    ASP A 176       40.99    -78.31                                   
REMARK 500    VAL A 187      -54.64   -126.35                                   
REMARK 500    SER A 204      173.85     69.07                                   
REMARK 500    CYS A 211      111.68   -161.91                                   
REMARK 500    ASN A 215       76.41   -156.48                                   
REMARK 500    ASP A 216     -143.77   -152.99                                   
REMARK 500    ASN A 250       98.70    -66.84                                   
REMARK 500    CYS A 262       84.37   -159.12                                   
REMARK 500    HIS A 284       52.43   -105.99                                   
REMARK 500    GLU A 296     -160.00    -87.89                                   
REMARK 500    ASN A 309       74.88   -102.96                                   
REMARK 500    SER A 313     -135.87   -116.47                                   
REMARK 500    HIS A 314       89.11    -61.30                                   
REMARK 500    GLU A 327      156.04     68.80                                   
REMARK 500    TYR A 331     -179.12   -173.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FUC A  401                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC A 401                 
DBREF  5MW7 A   27   348  UNP    Q9Y219   JAG2_HUMAN      27    348             
SEQADV 5MW7 GLY A  349  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 SER A  350  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  351  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  352  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  353  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  354  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  355  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  356  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  357  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW7 HIS A  358  UNP  Q9Y219              EXPRESSION TAG                 
SEQRES   1 A  332  MET GLY TYR PHE GLU LEU GLN LEU SER ALA LEU ARG ASN          
SEQRES   2 A  332  VAL ASN GLY GLU LEU LEU SER GLY ALA CYS CYS ASP GLY          
SEQRES   3 A  332  ASP GLY ARG THR THR ARG ALA GLY GLY CYS GLY HIS ASP          
SEQRES   4 A  332  GLU CYS ASP THR TYR VAL ARG VAL CYS LEU LYS GLU TYR          
SEQRES   5 A  332  GLN ALA LYS VAL THR PRO THR GLY PRO CYS SER TYR GLY          
SEQRES   6 A  332  HIS GLY ALA THR PRO VAL LEU GLY GLY ASN SER PHE TYR          
SEQRES   7 A  332  LEU PRO PRO ALA GLY ALA ALA GLY ASP ARG ALA ARG ALA          
SEQRES   8 A  332  ARG ALA ARG ALA GLY GLY ASP GLN ASP PRO GLY LEU VAL          
SEQRES   9 A  332  VAL ILE PRO PHE GLN PHE ALA TRP PRO ARG SER PHE THR          
SEQRES  10 A  332  LEU ILE VAL GLU ALA TRP ASP TRP ASP ASN ASP THR THR          
SEQRES  11 A  332  PRO ASN GLU GLU LEU LEU ILE GLU ARG VAL SER HIS ALA          
SEQRES  12 A  332  GLY MET ILE ASN PRO GLU ASP ARG TRP LYS SER LEU HIS          
SEQRES  13 A  332  PHE SER GLY HIS VAL ALA HIS LEU GLU LEU GLN ILE ARG          
SEQRES  14 A  332  VAL ARG CYS ASP GLU ASN TYR TYR SER ALA THR CYS ASN          
SEQRES  15 A  332  LYS PHE CYS ARG PRO ARG ASN ASP PHE PHE GLY HIS TYR          
SEQRES  16 A  332  THR CYS ASP GLN TYR GLY ASN LYS ALA CYS MET ASP GLY          
SEQRES  17 A  332  TRP MET GLY LYS GLU CYS LYS GLU ALA VAL CYS LYS GLN          
SEQRES  18 A  332  GLY CYS ASN LEU LEU HIS GLY GLY CYS THR VAL PRO GLY          
SEQRES  19 A  332  GLU CYS ARG CYS SER TYR GLY TRP GLN GLY ARG PHE CYS          
SEQRES  20 A  332  ASP GLU CYS VAL PRO TYR PRO GLY CYS VAL HIS GLY SER          
SEQRES  21 A  332  CYS VAL GLU PRO TRP GLN CYS ASN CYS GLU THR ASN TRP          
SEQRES  22 A  332  GLY GLY LEU LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY          
SEQRES  23 A  332  SER HIS HIS PRO CYS THR ASN GLY GLY THR CYS ILE ASN          
SEQRES  24 A  332  ALA GLU PRO ASP GLN TYR ARG CYS THR CYS PRO ASP GLY          
SEQRES  25 A  332  TYR SER GLY ARG ASN CYS GLU LYS ALA GLU GLY SER HIS          
SEQRES  26 A  332  HIS HIS HIS HIS HIS HIS HIS                                  
HET    FUC  A 401      10                                                       
HETNAM     FUC ALPHA-L-FUCOSE                                                   
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3  HOH   *35(H2 O)                                                     
HELIX    1 AA1 GLY A  112  ALA A  119  1                                   8    
SHEET    1 AA1 3 PHE A 103  TYR A 104  0                                        
SHEET    2 AA1 3 GLY A  28  ARG A  38 -1  N  LEU A  37   O  PHE A 103           
SHEET    3 AA1 3 LEU A 129  PHE A 134 -1  O  PHE A 134   N  GLY A  28           
SHEET    1 AA2 4 PHE A 103  TYR A 104  0                                        
SHEET    2 AA2 4 GLY A  28  ARG A  38 -1  N  LEU A  37   O  PHE A 103           
SHEET    3 AA2 4 HIS A 189  CYS A 198 -1  O  ARG A 195   N  GLU A  31           
SHEET    4 AA2 4 LYS A 179  SER A 184 -1  N  LEU A 181   O  LEU A 192           
SHEET    1 AA3 4 GLY A  91  ALA A  94  0                                        
SHEET    2 AA3 4 THR A  69  LYS A  76 -1  N  VAL A  73   O  GLY A  93           
SHEET    3 AA3 4 SER A 141  ASP A 150 -1  O  TRP A 149   N  TYR A  70           
SHEET    4 AA3 4 LEU A 162  MET A 171 -1  O  ILE A 163   N  ALA A 148           
SHEET    1 AA4 2 TYR A 202  TYR A 203  0                                        
SHEET    2 AA4 2 LYS A 209  PHE A 210 -1  O  LYS A 209   N  TYR A 203           
SHEET    1 AA5 3 ARG A 214  ASP A 216  0                                        
SHEET    2 AA5 3 GLY A 219  CYS A 223 -1  O  GLY A 219   N  ASP A 216           
SHEET    3 AA5 3 LYS A 229  CYS A 231 -1  O  ALA A 230   N  THR A 222           
SHEET    1 AA6 2 TRP A 235  MET A 236  0                                        
SHEET    2 AA6 2 GLU A 242  ALA A 243 -1  O  GLU A 242   N  MET A 236           
SHEET    1 AA7 2 GLY A 254  GLY A 255  0                                        
SHEET    2 AA7 2 ARG A 263  CYS A 264 -1  O  ARG A 263   N  GLY A 255           
SHEET    1 AA8 2 TRP A 268  GLN A 269  0                                        
SHEET    2 AA8 2 GLU A 275  CYS A 276 -1  O  GLU A 275   N  GLN A 269           
SHEET    1 AA9 2 GLY A 285  SER A 286  0                                        
SHEET    2 AA9 2 ASN A 294  CYS A 295 -1  O  ASN A 294   N  SER A 286           
SHEET    1 AB1 2 TRP A 299  GLY A 300  0                                        
SHEET    2 AB1 2 LYS A 306  ASP A 307 -1  O  LYS A 306   N  GLY A 300           
SHEET    1 AB2 2 CYS A 323  ASN A 325  0                                        
SHEET    2 AB2 2 TYR A 331  CYS A 333 -1  O  ARG A 332   N  ILE A 324           
SSBOND   1 CYS A   49    CYS A   62                          1555   1555  2.03  
SSBOND   2 CYS A   50    CYS A   67                          1555   1555  2.03  
SSBOND   3 CYS A   74    CYS A   88                          1555   1555  2.03  
SSBOND   4 CYS A  198    CYS A  207                          1555   1555  2.03  
SSBOND   5 CYS A  211    CYS A  223                          1555   1555  2.03  
SSBOND   6 CYS A  231    CYS A  240                          1555   1555  2.03  
SSBOND   7 CYS A  245    CYS A  256                          1555   1555  2.03  
SSBOND   8 CYS A  249    CYS A  262                          1555   1555  2.03  
SSBOND   9 CYS A  264    CYS A  273                          1555   1555  2.03  
SSBOND  10 CYS A  276    CYS A  287                          1555   1555  2.04  
SSBOND  11 CYS A  282    CYS A  293                          1555   1555  2.03  
SSBOND  12 CYS A  295    CYS A  304                          1555   1555  2.03  
SSBOND  13 CYS A  311    CYS A  323                          1555   1555  2.02  
SSBOND  14 CYS A  317    CYS A  333                          1555   1555  2.03  
SITE     1 AC1  3 GLY A 320  GLY A 321  THR A 322                               
CRYST1   46.814   77.205   96.357  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010378        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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