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Database: PDB
Entry: 1G1T
LinkDB: 1G1T
Original site: 1G1T 
HEADER    IMMUNE SYSTEM, MEMBRANE PROTEIN         13-OCT-00   1G1T              
TITLE     CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS                    
TITLE    2 COMPLEXED WITH SLEX                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E-SELECTIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LECTIN/EGF DOMAINS;                                        
COMPND   5 SYNONYM: ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1, ELAM-1,          
COMPND   6 LEUKOCYTE-ENDOTHELIAL CELL ADHESION MOLECULE 2, LECAM2,              
COMPND   7 CD62E;                                                               
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: OVARY [CHO] CELLS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    LECTIN, EGF, ADHESION MOLECULE, SLEX, IMMUNE SYSTEM,                  
KEYWDS   2 MEMBRANE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.S.SOMERS,R.T.CAMPHAUSEN                                             
REVDAT   3   24-FEB-09 1G1T    1       VERSN                                    
REVDAT   2   01-APR-03 1G1T    1       JRNL                                     
REVDAT   1   13-OCT-01 1G1T    0                                                
JRNL        AUTH   W.S.SOMERS,J.TANG,G.D.SHAW,R.T.CAMPHAUSEN                    
JRNL        TITL   INSIGHTS INTO THE MOLECULAR BASIS OF LEUKOCYTE               
JRNL        TITL 2 TETHERING AND ROLLING REVEALED BY STRUCTURES OF P-           
JRNL        TITL 3 AND E-SELECTIN BOUND TO 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   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 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) : 1.50                           
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             : 29493                          
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) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1474                            
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            : 1266                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 186                                     
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.42                            
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 1G1T 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 RCSB012127.                                      
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                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
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   : 29493                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
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     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 47.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, TRIS-HCL, CACL2, PEG 4000,        
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP AT 291K                       
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       17.25300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.78800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.19350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.78800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.25300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.19350            
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 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 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     -140.24   -122.89                                   
REMARK 500    HIS A  25     -178.23   -173.55                                   
REMARK 500    TYR A  48     -169.86     63.85                                   
REMARK 500    ASN A  75       48.66   -149.16                                   
REMARK 500    SER A 128        9.22     59.48                                   
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 A 264        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A 421        DISTANCE =  6.37 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     HOH A  328                                                       
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                              CA A 160  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE1                                                    
REMARK 620 2 FUC A 604   O3  138.0                                              
REMARK 620 3 ASP A 106   OD1  72.8 144.4                                        
REMARK 620 4 ASP A 106   O   130.0  71.6  73.6                                  
REMARK 620 5 ASN A 105   OD1  69.5  83.7  96.8  79.0                            
REMARK 620 6 ASN A  83   OD1 131.4  84.7  80.0  76.0 154.7                      
REMARK 620 7 ASN A  82   OD1  73.9 113.1  89.8 141.2 138.8  66.5                
REMARK 620 8 FUC A 604   O4   77.4  65.2 149.8 132.3  77.2 117.6  76.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 601                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A 602                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAG A 603                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 604                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 160                  
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: 1G1S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
DBREF  1G1T A    1   157  UNP    P16581   LEM2_HUMAN      22    178             
SEQRES   1 A  157  TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP          
SEQRES   2 A  157  GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU          
SEQRES   3 A  157  VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN          
SEQRES   4 A  157  SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY          
SEQRES   5 A  157  ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR          
SEQRES   6 A  157  GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO          
SEQRES   7 A  157  GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL          
SEQRES   8 A  157  GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP          
SEQRES   9 A  157  ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS          
SEQRES  10 A  157  TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS          
SEQRES  11 A  157  GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS          
SEQRES  12 A  157  CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE          
SEQRES  13 A  157  VAL                                                          
HET    SIA  A 601      20                                                       
HET    GAL  A 602      11                                                       
HET    MAG  A 603      16                                                       
HET    FUC  A 604      10                                                       
HET     CA  A 160       1                                                       
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     MAG BETA-METHYL-N-ACETYL-D-GLUCOSAMINE                               
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  SIA    C11 H19 N O9                                                 
FORMUL   2  GAL    C6 H12 O6                                                    
FORMUL   2  MAG    C9 H17 N O6                                                  
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *186(H2 O)                                                    
HELIX    1   1 THR A   11  TYR A   23  1                                  13    
HELIX    2   2 ASN A   31  LEU A   42  1                                  12    
HELIX    3   3 THR A  125  GLY A  129  5                                   5    
SHEET    1   A 3 SER A   2  THR A   5  0                                        
SHEET    2   A 3 LEU A 114  THR A 119 -1  N  CYS A 117   O  ASN A   4           
SHEET    3   A 3 HIS A  25  LEU A  26 -1  O  HIS A  25   N  TYR A 118           
SHEET    1   B 5 SER A   2  THR A   5  0                                        
SHEET    2   B 5 LEU A 114  THR A 119 -1  N  CYS A 117   O  ASN A   4           
SHEET    3   B 5 TYR A  49  ILE A  51  1  N  TRP A  50   O  LEU A 114           
SHEET    4   B 5 CYS A  90  ILE A  93 -1  O  VAL A  91   N  ILE A  51           
SHEET    5   B 5 TRP A 104  GLU A 107 -1  O  ASN A 105   N  GLU A  92           
SHEET    1   C 2 ILE A  53  VAL A  56  0                                        
SHEET    2   C 2 VAL A  59  TRP A  62 -1  O  VAL A  59   N  VAL A  56           
SHEET    1   D 2 GLY A 131  THR A 136  0                                        
SHEET    2   D 2 ASN A 139  CYS A 144 -1  O  ASN A 139   N  THR A 136           
SHEET    1   E 2 PHE A 148  SER A 149  0                                        
SHEET    2   E 2 GLN A 155  ILE A 156 -1  N  GLN A 155   O  SER A 149           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.03  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.03  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.03  
SSBOND   4 CYS A  127    CYS A  142                          1555   1555  2.03  
SSBOND   5 CYS A  144    CYS A  153                          1555   1555  2.03  
LINK         O4  MAG A 603                 C1  GAL A 602     1555   1555  1.43  
LINK         C1  FUC A 604                 O3  MAG A 603     1555   1555  1.43  
LINK         O3  GAL A 602                 C2  SIA A 601     1555   1555  1.44  
LINK        CA    CA A 160                 OE1 GLU A  80     1555   1555  2.56  
LINK        CA    CA A 160                 O3  FUC A 604     1555   1555  2.39  
LINK        CA    CA A 160                 OD1 ASP A 106     1555   1555  2.35  
LINK        CA    CA A 160                 O   ASP A 106     1555   1555  2.48  
LINK        CA    CA A 160                 OD1 ASN A 105     1555   1555  2.37  
LINK        CA    CA A 160                 OD1 ASN A  83     1555   1555  2.35  
LINK        CA    CA A 160                 OD1 ASN A  82     1555   1555  2.43  
LINK        CA    CA A 160                 O4  FUC A 604     1555   1555  2.59  
CISPEP   1 GLU A   80    PRO A   81          0        -0.03                     
SITE     1 AC1  5 TYR A  48  ARG A  97  GLU A  98  HOH A 329                    
SITE     2 AC1  5 GAL A 602                                                     
SITE     1 AC2  9 GLU A  92  TYR A  94  ARG A  97  ASN A 105                    
SITE     2 AC2  9 GLU A 107  HOH A 326  SIA A 601  MAG A 603                    
SITE     3 AC2  9 FUC A 604                                                     
SITE     1 AC3  2 GAL A 602  FUC A 604                                          
SITE     1 AC4  9 GLU A  80  ASN A  82  ASN A  83  ASN A 105                    
SITE     2 AC4  9 ASP A 106  GLU A 107   CA A 160  GAL A 602                    
SITE     3 AC4  9 MAG A 603                                                     
SITE     1 AC5  6 GLU A  80  ASN A  82  ASN A  83  ASN A 105                    
SITE     2 AC5  6 ASP A 106  FUC A 604                                          
CRYST1   34.506   72.387   77.576  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      0.028980  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013815  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012891        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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