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Database: PDB
Entry: 1G1S
LinkDB: 1G1S
Original site: 1G1S 
HEADER    IMMUNE SYSTEM, MEMBRANE PROTEIN         13-OCT-00   1G1S              
TITLE     P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P-SELECTIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LECTIN/EGF DOMAINS;                                        
COMPND   5 SYNONYM: GRANULE MEMBRANE PROTEIN 140, GMP-140, PADGEM, CD62P,       
COMPND   6 LEUKOCYTE-ENDOTHELIAL CELL ADHESION MOLECULE 3, LECAM3;              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PSGL-1 PEPTIDE;                                            
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 SYNONYM: PSGL-1;                                                     
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: CHO CELLS;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL: CHO CELLS;                                   
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SELECTIN, LECTIN, EGF, SULPHATED, SLEX, IMMUNE SYSTEM, MEMBRANE       
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.S.SOMERS,R.T.CAMPHAUSEN                                             
REVDAT   4   13-JUL-11 1G1S    1       VERSN                                    
REVDAT   3   24-FEB-09 1G1S    1       VERSN                                    
REVDAT   2   01-APR-03 1G1S    1       JRNL                                     
REVDAT   1   13-OCT-01 1G1S    0                                                
JRNL        AUTH   W.S.SOMERS,J.TANG,G.D.SHAW,R.T.CAMPHAUSEN                    
JRNL        TITL   INSIGHTS INTO THE MOLECULAR BASIS OF LEUKOCYTE TETHERING AND 
JRNL        TITL 2 ROLLING REVEALED BY STRUCTURES OF P- AND E-SELECTIN BOUND TO 
JRNL        TITL 3 SLE(X) AND PSGL-1.                                           
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 103   467 2000              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11081633                                                     
JRNL        DOI    10.1016/S0092-8674(00)00138-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 44923                          
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 SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2246                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.00                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.54                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G1S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012126.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99987                            
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.630                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.63                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: P-SELECTIN                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 10 MM TRIS, 150 MN NACL,   
REMARK 280  4 MM CACL2, 50 MM SRCL2, 5% PEG 6000, 33% MPD, PH 7.0, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP AT 291K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       31.72250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.37800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       93.64450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.72250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.37800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       93.64450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.72250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.37800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       93.64450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.72250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.37800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       93.64450            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ASP A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     LYS A   162                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     ASP B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     LYS B   162                                                      
REMARK 465     GLN C   601                                                      
REMARK 465     ALA C   602                                                      
REMARK 465     THR C   603                                                      
REMARK 465     GLU C   604                                                      
REMARK 465     TYS C   605                                                      
REMARK 465     PRO C   619                                                      
REMARK 465     ARG C   620                                                      
REMARK 465     PRO C   621                                                      
REMARK 465     MET C   622                                                      
REMARK 465     MET C   623                                                      
REMARK 465     ASP C   624                                                      
REMARK 465     ASP C   625                                                      
REMARK 465     ASP C   626                                                      
REMARK 465     ASP C   627                                                      
REMARK 465     LYS C   628                                                      
REMARK 465     GLN D   601                                                      
REMARK 465     ALA D   602                                                      
REMARK 465     THR D   603                                                      
REMARK 465     GLU D   604                                                      
REMARK 465     PRO D   619                                                      
REMARK 465     ARG D   620                                                      
REMARK 465     PRO D   621                                                      
REMARK 465     MET D   622                                                      
REMARK 465     MET D   623                                                      
REMARK 465     ASP D   624                                                      
REMARK 465     ASP D   625                                                      
REMARK 465     ASP D   626                                                      
REMARK 465     ASP D   627                                                      
REMARK 465     LYS D   628                                                      
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     LYS A  32    CG   CD   CE   NZ                                   
REMARK 470     ASN A  57    CG   OD1                                            
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ASN A  71    CG   OD1                                            
REMARK 470     ASP A 158    CG   OD1  OD2                                       
REMARK 470     ARG B  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B  57    CG   OD1                                            
REMARK 470     LYS B  58    CG   CD   CE   NZ                                   
REMARK 470     GLU B  72    CG   CD   OE1  OE2                                  
REMARK 470     MET B 125    CG   SD   CE                                        
REMARK 470     ARG B 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 606    CG   CD   OE1  OE2                                  
REMARK 470     TYS D 605    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYS D 605    S    O1   O2   O3                                   
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   O    HOH B   950     O    HOH B   950     4576     1.88            
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    TYR A  23     -137.03   -129.66                                   
REMARK 500    ALA A  28       75.29   -112.92                                   
REMARK 500    ILE A  29       91.88    -41.86                                   
REMARK 500    TYR A  48     -158.45     61.79                                   
REMARK 500    ASN A  57      -92.65     67.21                                   
REMARK 500    ASN A  83       47.43     36.22                                   
REMARK 500    ASN A  86      150.48     80.77                                   
REMARK 500    ALA A 100       56.85   -145.95                                   
REMARK 500    ASN A 139     -139.20   -163.07                                   
REMARK 500    TYR B  23     -137.34   -128.54                                   
REMARK 500    TYR B  48     -160.90     62.87                                   
REMARK 500    ASN B  57     -111.45     72.64                                   
REMARK 500    GLU B  74      132.04    -27.69                                   
REMARK 500    ASN B  75       38.39   -144.65                                   
REMARK 500    ASN B  83       45.82     33.69                                   
REMARK 500    ASN B  86      148.71     77.14                                   
REMARK 500    ALA B 100       59.94   -145.15                                   
REMARK 500    SER B 128       25.35     49.26                                   
REMARK 500    ASN B 139     -150.60   -161.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 987        DISTANCE =  5.50 ANGSTROMS                       
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     NGA C  633                                                       
REMARK 610     NGA D  633                                                       
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                              SR A 901  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 106   O                                                      
REMARK 620 2 GLU A  80   OE1 132.1                                              
REMARK 620 3 ASN A 105   OD1  76.5  66.9                                        
REMARK 620 4 ASP A 106   OD1  71.8  74.1  83.3                                  
REMARK 620 5 FUC D 632   O3   71.7 130.6  84.1 143.2                            
REMARK 620 6 FUC D 632   O4  129.8  74.6  81.1 148.5  61.6                      
REMARK 620 7 ASN A  82   OD1 144.6  71.6 136.8  97.0 115.6  76.6                
REMARK 620 8 GLU A  88   OE1  72.6 135.8 149.0  84.7  88.7 121.3  73.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              SR B 902  SR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  88   OE1                                                    
REMARK 620 2 ASN B 105   OD1 148.8                                              
REMARK 620 3 ASP B 106   O    71.4  77.6                                        
REMARK 620 4 ASP B 106   OD1  84.1  89.2  72.4                                  
REMARK 620 5 FUC C 632   O3   85.3  82.3  71.3 143.7                            
REMARK 620 6 FUC C 632   O4  119.7  78.2 128.8 150.7  61.1                      
REMARK 620 7 GLU B  80   OE1 138.6  67.1 131.5  74.8 131.5  75.9                
REMARK 620 8 ASN B  82   OD1  72.5 138.3 141.9  92.2 117.3  80.6  73.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 903  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 954   O                                                      
REMARK 620 2 HOH D 202   O    86.7                                              
REMARK 620 3 ASP D 609   OD1 155.4 116.1                                        
REMARK 620 4 HOH D 201   O    86.2 169.3  72.4                                  
REMARK 620 5 ASP D 609   OD2 149.2  77.8  52.2 104.7                            
REMARK 620 6 HOH D 203   O    75.9  84.4 113.5  86.2  76.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 904  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 609   OD1                                                    
REMARK 620 2 HOH C 185   O   148.8                                              
REMARK 620 3 HOH C 200   O   118.5  81.9                                        
REMARK 620 4 HOH C  55   O   115.6  86.1  89.2                                  
REMARK 620 5 HOH C 199   O    72.7  87.1  84.9 171.5                            
REMARK 620 6 ASP C 609   OD2  53.9 157.2  84.4  75.6 109.8                      
REMARK 620 7 ASP C 611   OD2  89.0  65.9 147.2  94.7  87.1 128.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA C 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL C 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC C 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA C 633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL C 634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA D 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC D 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA D 633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SR B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 811                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1G1Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
REMARK 900 RELATED ID: 1G1R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
REMARK 900 COMPLEXED WITH SLEX                                                  
REMARK 900 RELATED ID: 1G1T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E-SELECTIN                                      
DBREF  1G1S A    1   158  UNP    P16109   LEM3_HUMAN      42    199             
DBREF  1G1S B    1   158  UNP    P16109   LEM3_HUMAN      42    199             
DBREF  1G1S C  601   619  UNP    Q14242   SEPL_HUMAN      42     60             
DBREF  1G1S D  601   619  UNP    Q14242   SEPL_HUMAN      42     60             
SEQADV 1G1S ASP A  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1S ASP A  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S ASP A  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S ASP A  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S LYS A  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S ASP B  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1S ASP B  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S ASP B  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S ASP B  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S LYS B  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1S TYS C  605  UNP  Q14242    TYR    46 MODIFIED RESIDUE               
SEQADV 1G1S TYS C  607  UNP  Q14242    TYR    48 MODIFIED RESIDUE               
SEQADV 1G1S TYS C  610  UNP  Q14242    TYR    51 MODIFIED RESIDUE               
SEQADV 1G1S ARG C  620  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S PRO C  621  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S MET C  622  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S MET C  623  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP C  624  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP C  625  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP C  626  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP C  627  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S LYS C  628  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S TYS D  605  UNP  Q14242    TYR    46 MODIFIED RESIDUE               
SEQADV 1G1S TYS D  607  UNP  Q14242    TYR    48 MODIFIED RESIDUE               
SEQADV 1G1S TYS D  610  UNP  Q14242    TYR    51 MODIFIED RESIDUE               
SEQADV 1G1S ARG D  620  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S PRO D  621  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S MET D  622  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S MET D  623  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP D  624  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP D  625  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP D  626  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S ASP D  627  UNP  Q14242              CLONING ARTIFACT               
SEQADV 1G1S LYS D  628  UNP  Q14242              CLONING ARTIFACT               
SEQRES   1 A  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 A  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 A  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 A  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 A  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 A  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 A  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 A  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 A  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 A  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 A  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 A  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 A  162  ARG ASP ASP ASP ASP LYS                                      
SEQRES   1 B  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 B  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 B  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 B  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 B  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 B  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 B  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 B  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 B  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 B  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 B  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 B  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 B  162  ARG ASP ASP ASP ASP LYS                                      
SEQRES   1 C   28  GLN ALA THR GLU TYS GLU TYS LEU ASP TYS ASP PHE LEU          
SEQRES   2 C   28  PRO GLU THR GLU PRO PRO ARG PRO MET MET ASP ASP ASP          
SEQRES   3 C   28  ASP LYS                                                      
SEQRES   1 D   28  GLN ALA THR GLU TYS GLU TYS LEU ASP TYS ASP PHE LEU          
SEQRES   2 D   28  PRO GLU THR GLU PRO PRO ARG PRO MET MET ASP ASP ASP          
SEQRES   3 D   28  ASP LYS                                                      
MODRES 1G1S THR D  616  THR  GLYCOSYLATION SITE                                 
MODRES 1G1S THR C  616  THR  GLYCOSYLATION SITE                                 
MODRES 1G1S TYS C  607  TYR  O-SULFO-L-TYROSINE                                 
MODRES 1G1S TYS C  610  TYR  O-SULFO-L-TYROSINE                                 
MODRES 1G1S TYS D  605  TYR  O-SULFO-L-TYROSINE                                 
MODRES 1G1S TYS D  607  TYR  O-SULFO-L-TYROSINE                                 
MODRES 1G1S TYS D  610  TYR  O-SULFO-L-TYROSINE                                 
HET    TYS  C 607      16                                                       
HET    TYS  C 610      16                                                       
HET    TYS  D 605       5                                                       
HET    TYS  D 607      16                                                       
HET    TYS  D 610      16                                                       
HET    SIA  C 629      20                                                       
HET    GAL  C 630      11                                                       
HET    NAG  C 631      15                                                       
HET    FUC  C 632      10                                                       
HET    NGA  C 633      13                                                       
HET    GAL  C 634      11                                                       
HET    SIA  D 629      20                                                       
HET    GAL  D 630      11                                                       
HET    NAG  D 631      15                                                       
HET    FUC  D 632      10                                                       
HET    NGA  D 633      13                                                       
HET    GAL  D 634      11                                                       
HET     SR  A 901       1                                                       
HET     SR  B 902       1                                                       
HET     NA  B 903       1                                                       
HET     NA  C 904       1                                                       
HET    MRD  B 805       8                                                       
HET    MRD  B 806       8                                                       
HET    MRD  A 807       8                                                       
HET    MRD  B 808       8                                                       
HET    MRD  B 809       8                                                       
HET    MRD  B 810       8                                                       
HET    MRD  A 811       8                                                       
HETNAM     TYS O-SULFO-L-TYROSINE                                               
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NGA N-ACETYL-D-GALACTOSAMINE                                         
HETNAM      SR STRONTIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   3  TYS    5(C9 H11 N O6 S)                                             
FORMUL   5  SIA    2(C11 H19 N O9)                                              
FORMUL   5  GAL    4(C6 H12 O6)                                                 
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   5  FUC    2(C6 H12 O5)                                                 
FORMUL   5  NGA    2(C8 H15 N O6)                                               
FORMUL   7   SR    2(SR 2+)                                                     
FORMUL   9   NA    2(NA 1+)                                                     
FORMUL  11  MRD    7(C6 H14 O2)                                                 
FORMUL  18  HOH   *224(H2 O)                                                    
HELIX    1   1 SER A   11  TYR A   23  1                                  13    
HELIX    2   2 ASN A   31  LEU A   42  1                                  12    
HELIX    3   3 MET A  125  LYS A  129  5                                   5    
HELIX    4   4 SER B   11  TYR B   23  1                                  13    
HELIX    5   5 ASN B   31  LEU B   42  1                                  12    
SHEET    1   A 2 GLY A 131  GLU A 135  0                                        
SHEET    2   A 2 TYR A 140  CYS A 144 -1  O  THR A 141   N  LEU A 134           
SHEET    1   B 2 PHE A 148  TYR A 149  0                                        
SHEET    2   B 2 TYR A 155  VAL A 156 -1  N  TYR A 155   O  TYR A 149           
SHEET    1   C 2 GLY B 131  THR B 136  0                                        
SHEET    2   C 2 ASN B 139  CYS B 144 -1  O  ASN B 139   N  THR B 136           
SHEET    1   D 2 PHE B 148  TYR B 149  0                                        
SHEET    2   D 2 TYR B 155  VAL B 156 -1  N  TYR B 155   O  TYR B 149           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.06  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.04  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.06  
SSBOND   4 CYS A  127    CYS A  142                          1555   1555  2.06  
SSBOND   5 CYS A  144    CYS A  153                          1555   1555  2.09  
SSBOND   6 CYS B   19    CYS B  117                          1555   1555  2.07  
SSBOND   7 CYS B   90    CYS B  109                          1555   1555  2.05  
SSBOND   8 CYS B  122    CYS B  133                          1555   1555  2.05  
SSBOND   9 CYS B  127    CYS B  142                          1555   1555  2.05  
SSBOND  10 CYS B  144    CYS B  153                          1555   1555  2.08  
LINK         O4  NAG D 631                 C1  GAL D 630     1555   1555  1.39  
LINK         O4  NAG C 631                 C1  GAL C 630     1555   1555  1.39  
LINK         O3  NGA D 633                 C1  GAL D 634     1555   1555  1.40  
LINK         C6  NGA D 633                 O1  NAG D 631     1555   1555  1.40  
LINK         O3  NAG D 631                 C1  FUC D 632     1555   1555  1.40  
LINK         C1  GAL C 634                 O3  NGA C 633     1555   1555  1.41  
LINK         C6  NGA C 633                 O1  NAG C 631     1555   1555  1.41  
LINK         O3  NAG C 631                 C1  FUC C 632     1555   1555  1.42  
LINK         OG1 THR D 616                 C1  NGA D 633     1555   1555  1.43  
LINK         C1  NGA C 633                 OG1 THR C 616     1555   1555  1.43  
LINK         C2  SIA C 629                 O3  GAL C 630     1555   1555  1.44  
LINK         C2  SIA D 629                 O3  GAL D 630     1555   1555  1.45  
LINK        SR    SR A 901                 O   ASP A 106     1555   1555  2.54  
LINK        SR    SR A 901                 OE1 GLU A  80     1555   1555  2.85  
LINK        SR    SR A 901                 OD1 ASN A 105     1555   1555  2.54  
LINK        SR    SR A 901                 OD1 ASP A 106     1555   1555  2.33  
LINK        SR    SR A 901                 O3  FUC D 632     1555   1555  2.51  
LINK        SR    SR A 901                 O4  FUC D 632     1555   1555  2.76  
LINK        SR    SR A 901                 OD1 ASN A  82     1555   1555  2.58  
LINK        SR    SR A 901                 OE1 GLU A  88     1555   1555  2.60  
LINK        SR    SR B 902                 OE1 GLU B  88     1555   1555  2.58  
LINK        SR    SR B 902                 OD1 ASN B 105     1555   1555  2.54  
LINK        SR    SR B 902                 O   ASP B 106     1555   1555  2.55  
LINK        SR    SR B 902                 OD1 ASP B 106     1555   1555  2.22  
LINK        SR    SR B 902                 O3  FUC C 632     1555   1555  2.56  
LINK        SR    SR B 902                 O4  FUC C 632     1555   1555  2.73  
LINK        SR    SR B 902                 OE1 GLU B  80     1555   1555  2.65  
LINK        SR    SR B 902                 OD1 ASN B  82     1555   1555  2.60  
LINK        NA    NA B 903                 O   HOH B 954     1555   1555  2.36  
LINK         C   GLU C 606                 N   TYS C 607     1555   1555  1.33  
LINK         C   TYS C 607                 N   LEU C 608     1555   1555  1.33  
LINK         C   ASP C 609                 N   TYS C 610     1555   1555  1.33  
LINK         C   TYS C 610                 N   ASP C 611     1555   1555  1.32  
LINK        NA    NA C 904                 OD1 ASP C 609     1555   1555  2.46  
LINK        NA    NA C 904                 O   HOH C 185     1555   1555  2.41  
LINK        NA    NA C 904                 O   HOH C 200     1555   1555  2.48  
LINK        NA    NA C 904                 O   HOH C  55     1555   1555  2.22  
LINK        NA    NA C 904                 O   HOH C 199     1555   1555  2.18  
LINK        NA    NA C 904                 OD2 ASP C 609     1555   1555  2.39  
LINK         C   TYS D 605                 N   GLU D 606     1555   1555  1.33  
LINK         C   GLU D 606                 N   TYS D 607     1555   1555  1.32  
LINK         C   TYS D 607                 N   LEU D 608     1555   1555  1.33  
LINK         C   ASP D 609                 N   TYS D 610     1555   1555  1.33  
LINK         C   TYS D 610                 N   ASP D 611     1555   1555  1.33  
LINK        NA    NA B 903                 O   HOH D 202     1555   7645  2.19  
LINK        NA    NA B 903                 OD1 ASP D 609     1555   7645  2.54  
LINK        NA    NA B 903                 O   HOH D 201     1555   7645  2.28  
LINK        NA    NA B 903                 OD2 ASP D 609     1555   7645  2.48  
LINK        NA    NA B 903                 O   HOH D 203     1555   7645  2.49  
LINK         OD2 ASP C 611                NA    NA C 904     1555   1555  2.71  
CISPEP   1 GLU A   80    PRO A   81          0         0.05                     
CISPEP   2 GLU B   80    PRO B   81          0        -0.49                     
SITE     1 AC1  4 TYR B  48  SER B  99  HOH C  39  GAL C 630                    
SITE     1 AC2  9 TYR B  48  GLU B  92  TYR B  94  GLU B 107                    
SITE     2 AC2  9 HOH C  51  HOH C 154  SIA C 629  NAG C 631                    
SITE     3 AC2  9 FUC C 632                                                     
SITE     1 AC3  9 LYS B  84  ARG B  85  HOH B 946  HOH C  68                    
SITE     2 AC3  9 HOH C 212  THR C 616  GAL C 630  FUC C 632                    
SITE     3 AC3  9 NGA C 633                                                     
SITE     1 AC4 10 GLU B  80  ASN B  82  GLU B  88  ASN B 105                    
SITE     2 AC4 10 ASP B 106  GLU B 107   SR B 902  HOH C  68                    
SITE     3 AC4 10 GAL C 630  NAG C 631                                          
SITE     1 AC5  5 TYS C 610  THR C 616  GLU C 617  NAG C 631                    
SITE     2 AC5  5 GAL C 634                                                     
SITE     1 AC6  1 NGA C 633                                                     
SITE     1 AC7  7 TYR A  48  SER A  99  HOH A 950  HOH A 963                    
SITE     2 AC7  7 HOH D 117  HOH D 173  GAL D 630                               
SITE     1 AC8  8 GLU A  92  TYR A  94  GLU A 107  HOH D  49                    
SITE     2 AC8  8 HOH D  69  SIA D 629  NAG D 631  FUC D 632                    
SITE     1 AC9  9 ARG A  85  HOH A 927  HOH D  52  HOH D 192                    
SITE     2 AC9  9 HOH D 210  THR D 616  GAL D 630  FUC D 632                    
SITE     3 AC9  9 NGA D 633                                                     
SITE     1 BC1 11 GLU A  80  ASN A  82  GLU A  88  ASN A 105                    
SITE     2 BC1 11 ASP A 106  GLU A 107   SR A 901  HOH D  52                    
SITE     3 BC1 11 HOH D 183  GAL D 630  NAG D 631                               
SITE     1 BC2  6 HOH D 218  TYS D 610  THR D 616  GLU D 617                    
SITE     2 BC2  6 NAG D 631  GAL D 634                                          
SITE     1 BC3  1 NGA D 633                                                     
SITE     1 BC4  6 GLU A  80  ASN A  82  GLU A  88  ASN A 105                    
SITE     2 BC4  6 ASP A 106  FUC D 632                                          
SITE     1 BC5  6 GLU B  80  ASN B  82  GLU B  88  ASN B 105                    
SITE     2 BC5  6 ASP B 106  FUC C 632                                          
SITE     1 BC6  6 HOH B 954  HOH D 201  HOH D 202  HOH D 203                    
SITE     2 BC6  6 ASP D 609  ASP D 611                                          
SITE     1 BC7  6 HOH C  55  HOH C 185  HOH C 199  HOH C 200                    
SITE     2 BC7  6 ASP C 609  ASP C 611                                          
SITE     1 BC8  4 TRP B   1  ALA B  28  GLN B  30  TYR B 118                    
SITE     1 BC9  6 TYR B   3  TYR B  37  VAL B  41  TYR B 149                    
SITE     2 BC9  6 HOH B 909  HOH B 962                                          
SITE     1 CC1  3 ALA A  28  GLU A  34  TYR A 118                               
SITE     1 CC2  7 TRP B   1  GLN B  30  ASN B  31  ASN B  33                    
SITE     2 CC2  7 GLU B  34  ILE B 137  HOH B 955                               
SITE     1 CC3  5 ASP B  36  PRO B 101  GLU B 132  SER B 143                    
SITE     2 CC3  5 CYS B 144                                                     
SITE     1 CC4  6 TYR B  10  ILE B  14  LYS B  17  TYR B  18                    
SITE     2 CC4  6 TYS D 610  GLU D 615                                          
SITE     1 CC5  5 ASN A 139  TYR A 140  PRO A 151  GLU A 152                    
SITE     2 CC5  5 HOH A 960                                                     
CRYST1   63.445   96.756  187.289  90.00  90.00  90.00 I 2 2 2      16          
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      0.015762  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005339        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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