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Database: PDB
Entry: 4CSY
LinkDB: 4CSY
Original site: 4CSY 
HEADER    CELL-ADHESION                           11-MAR-14   4CSY              
TITLE     E-SELECTIN LECTIN, EGF-LIKE AND TWO SCR DOMAINS COMPLEXED             
TITLE    2 WITH SIALYL LEWIS X                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E-SELECTIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LECTIN DOMAIN, EGF-LIKE DOMAIN, SHORT CONSENSUS REPEAT     
COMPND   5  DOMAIN 1, SHORT CONSENSUS REPEAT DOMAIN 2, RESIDUES 22-301;         
COMPND   6 SYNONYM: CD62 ANTIGEN-LIKE FAMILY MEMBER E, ENDOTHELIAL LEUKOCYTE    
COMPND   7  ADHESION MOLECULE 1, ELAM-1, LEUKOCYTE-ENDOTHELIAL CELL ADHESION    
COMPND   8  MOLECULE 2, LECAM2;                                                 
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: N-ACETYLGLUCOSAMINE RESIDUES ATTACHED TO ASN4,        
COMPND  11  ASN124, ASN139, ASN158, ASN178, ASN182, AND ASN244 ON BOTH CHAINS.  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: CYTOKINE-INDUCED VASCULAR ENDOTHELIAL CELLS;                 
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY (CHO) CELLS;      
SOURCE  10 EXPRESSION_SYSTEM_TISSUE: OVARY;                                     
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    CELL-ADHESION, HUMAN LECTIN, C-TYPE LECTIN, INFLAMMATION, LEUKOCYTE,  
KEYWDS   2 SIALYL LEWIS X, SLEX, PROTEIN CONFORMATION, LIGAND-INDUCED           
KEYWDS   3 CONFORMATIONAL CHANGE, CATCH- BOND                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.PRESTON,R.P.JAKOB,F.P.C.BINDER,C.P.SAGER,B.ERNST,T.MAIER          
REVDAT   3   27-JAN-16 4CSY    1       JRNL                                     
REVDAT   2   08-JUL-15 4CSY    1       JRNL                                     
REVDAT   1   24-SEP-14 4CSY    0                                                
JRNL        AUTH   R.C.PRESTON,R.P.JAKOB,F.P.BINDER,C.P.SAGER,B.ERNST,T.MAIER   
JRNL        TITL   E-SELECTIN LIGAND COMPLEXES ADOPT AN EXTENDED HIGH-AFFINITY  
JRNL        TITL 2 CONFORMATION.                                                
JRNL        REF    J.MOL.CELL.BIOL.              V.   8    62 2016              
JRNL        REFN                   ISSN 1759-4685                               
JRNL        PMID   26117840                                                     
JRNL        DOI    10.1093/JMCB/MJV046                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.45                          
REMARK   3   NUMBER OF REFLECTIONS             : 25216                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.2168                         
REMARK   3   R VALUE            (WORKING SET)  : 0.2148                         
REMARK   3   FREE R VALUE                      : 0.2528                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.15                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 1298                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.41                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.51                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.45                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2829                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2417                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2702                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2406                   
REMARK   3   BIN FREE R VALUE                        : 0.2629                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.49                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 127                      
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            : 4358                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 312                                     
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.3105                                              
REMARK   3    B22 (A**2) : -6.6601                                              
REMARK   3    B33 (A**2) : -7.6504                                              
REMARK   3    B12 (A**2) : -0.4928                                              
REMARK   3    B13 (A**2) : -0.4253                                              
REMARK   3    B23 (A**2) : -6.0333                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.507               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.442               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.261               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.471               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.268               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9294                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9003                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4854   ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 6664   ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1672   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 135    ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 694    ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4854   ; 20.00  ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.00   ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 704    ; 5.00   ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5465   ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.16                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.78                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    5.5214   25.9503  -13.7994           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2104 T22:    0.0134                                    
REMARK   3     T33:   -0.1586 T12:    0.0168                                    
REMARK   3     T13:   -0.0441 T23:    0.1041                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.7739 L22:    0.2739                                    
REMARK   3     L33:    0.8243 L12:   -0.4265                                    
REMARK   3     L13:    1.2899 L23:   -0.1991                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0399 S12:    0.0026 S13:    0.5059                     
REMARK   3     S21:    0.1054 S22:    0.0137 S23:    0.0437                     
REMARK   3     S31:    0.0801 S32:   -0.0112 S33:   -0.0536                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.7840    8.4486  -27.4944           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2139 T22:   -0.0078                                    
REMARK   3     T33:   -0.0973 T12:   -0.0314                                    
REMARK   3     T13:    0.0332 T23:    0.1113                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.9872 L22:    0.6541                                    
REMARK   3     L33:    0.3069 L12:    1.2390                                    
REMARK   3     L13:   -0.7044 L23:   -0.2172                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0508 S12:    0.4019 S13:   -0.2560                     
REMARK   3     S21:    0.1062 S22:   -0.0762 S23:   -0.0379                     
REMARK   3     S31:    0.0343 S32:    0.0628 S33:    0.0254                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDER IN LOOPS 227-231, 254-259 AND    
REMARK   3  N-TERMINAL RESIDUES 278-280 BUILT ACCORDING TO ACCOMPANYING         
REMARK   3  DEPOSITION EBI-57874.                                               
REMARK   4                                                                      
REMARK   4 4CSY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-59945.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99985                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25239                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.41                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.28                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 1.8                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.80                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.32                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1G1S, 3GOV, 1H04                         
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.1                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13 % PEG8000, HEPES, MOPS PH             
REMARK 280  6.2, CACL2, 10MM SLEX-OTMSE                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ALA A  28     -124.60    -91.59                                   
REMARK 500    ILE A  29      120.67    -34.86                                   
REMARK 500    TYR A  48     -159.89     68.52                                   
REMARK 500    LYS A  86      162.79     62.97                                   
REMARK 500    ASN A 139     -132.29   -155.56                                   
REMARK 500    HIS A 167       16.75     81.54                                   
REMARK 500    TYR A 181      128.76    -38.45                                   
REMARK 500    ASN A 182       -3.92     82.54                                   
REMARK 500    ASN A 244       -9.33     95.42                                   
REMARK 500    ALA B  28      -86.60    -94.70                                   
REMARK 500    ILE B  29      142.00    -21.81                                   
REMARK 500    TYR B  48     -160.88     68.83                                   
REMARK 500    LYS B  86      159.35     63.61                                   
REMARK 500    SER B 128       19.72     56.75                                   
REMARK 500    ASN B 139     -132.95   -154.50                                   
REMARK 500    ASN B 244       -8.75     91.28                                   
REMARK 500    LYS B 279     -108.57    -94.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A  63        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP A  87        24.4      L          L   OUTSIDE RANGE           
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 A2066        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A2067        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A2069        DISTANCE =  9.11 ANGSTROMS                       
REMARK 525    HOH B2068        DISTANCE =  5.66 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 SIALYL LEWIS X METHYL GLUCOSIDE (DRG): SIALYL-LEWIS-X                
REMARK 600  TETRASACCHARIDE, WITH A TRIMETHYLSILYLETHYL PROTECTING              
REMARK 600  GROUP, ONLY METHYL GLUCOSIDE WAS MODELED                            
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): REMAINS FROM ENDOGLYCOSIDASE           
REMARK 600  H TREATMENT                                                         
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 306  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE1                                                    
REMARK 620 2 ASN A  82   OD1  68.6                                              
REMARK 620 3 GLU A  88   OE1 134.1  78.0                                        
REMARK 620 4 ASN A 105   OD1  68.2 132.8 148.7                                  
REMARK 620 5 ASP A 106   O   129.2 150.4  73.4  75.3                            
REMARK 620 6 ASP A 106   OD1  71.5  92.4  79.7  91.6  75.5                      
REMARK 620 7 FUC A 304   O3  139.3 108.3  80.2  92.4  74.1 147.2                
REMARK 620 8 FUC A 304   O4   67.4  77.8 135.0  68.7 128.8 138.5  72.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 306  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  88   OE1                                                    
REMARK 620 2 ASP B 106   O    74.6                                              
REMARK 620 3 ASP B 106   OD1  84.5  72.8                                        
REMARK 620 4 GLU B  80   OE1 141.8 125.7  74.1                                  
REMARK 620 5 ASN B  82   OD1  81.8 154.6  95.8  69.6                            
REMARK 620 6 ASN B 105   OD1 148.3  73.8  88.3  63.4 129.6                      
REMARK 620 7 FUC B 304   O3   77.1  76.4 147.3 134.9 107.8  93.4                
REMARK 620 8 FUC B 304   O4  132.7 129.1 137.5  63.7  74.6  69.3  72.2          
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  CA A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 285  BOUND TO ASN A   4                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 286  BOUND TO ASN A 124                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 282  BOUND TO ASN A 139                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 283  BOUND TO ASN A 158                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 284  BOUND TO ASN A 178                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 281  BOUND TO ASN A 182                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A 287  BOUND TO ASN A 244                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 285  BOUND TO ASN B   4                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 286  BOUND TO ASN B 124                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 282  BOUND TO ASN B 139                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 283  BOUND TO ASN B 158                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 284  BOUND TO ASN B 178                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 281  BOUND TO ASN B 182                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B 287  BOUND TO ASN B 244                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES SIA A 301  THROUGH FUC A 304                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES SIA B 301  THROUGH FUC B 304                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CSS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FIMH IN COMPLEX WITH A                         
REMARK 900  SULFONAMIDE BIPHENYL ALPHA D-MANNOSIDE                              
REMARK 900 RELATED ID: 4CST   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FIMH IN COMPLEX WITH 3'-CHLORO-                
REMARK 900  4'-(ALPHA-D-MANNOPYRANOSYLOXY)-BIPHENYL-4-CARBONITRILE              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 WITHOUT N-TERMINAL SECRETION SIGNAL (AA. 1-21). SEQUENCE             
REMARK 999 OF MATURE PROTEIN STARTS WITH RESIDUE 1 FOR COMPATIBILITY            
REMARK 999 WITH PREVIOUS E-SELECTIN STRUCTURES (1ESL, 1G1T).                    
DBREF  4CSY A    1   280  UNP    P16581   LYAM2_HUMAN     22    301             
DBREF  4CSY B    1   280  UNP    P16581   LYAM2_HUMAN     22    301             
SEQRES   1 A  280  TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP          
SEQRES   2 A  280  GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU          
SEQRES   3 A  280  VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN          
SEQRES   4 A  280  SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY          
SEQRES   5 A  280  ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR          
SEQRES   6 A  280  GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO          
SEQRES   7 A  280  GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL          
SEQRES   8 A  280  GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP          
SEQRES   9 A  280  ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS          
SEQRES  10 A  280  TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS          
SEQRES  11 A  280  GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS          
SEQRES  12 A  280  CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE          
SEQRES  13 A  280  VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER          
SEQRES  14 A  280  LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN          
SEQRES  15 A  280  SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO          
SEQRES  16 A  280  SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU          
SEQRES  17 A  280  TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS          
SEQRES  18 A  280  ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS          
SEQRES  19 A  280  PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS          
SEQRES  20 A  280  THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA          
SEQRES  21 A  280  GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN          
SEQRES  22 A  280  GLU LYS PRO THR CYS LYS ALA                                  
SEQRES   1 B  280  TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP          
SEQRES   2 B  280  GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU          
SEQRES   3 B  280  VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN          
SEQRES   4 B  280  SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY          
SEQRES   5 B  280  ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR          
SEQRES   6 B  280  GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO          
SEQRES   7 B  280  GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL          
SEQRES   8 B  280  GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP          
SEQRES   9 B  280  ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS          
SEQRES  10 B  280  TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS          
SEQRES  11 B  280  GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS          
SEQRES  12 B  280  CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE          
SEQRES  13 B  280  VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER          
SEQRES  14 B  280  LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN          
SEQRES  15 B  280  SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO          
SEQRES  16 B  280  SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU          
SEQRES  17 B  280  TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS          
SEQRES  18 B  280  ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS          
SEQRES  19 B  280  PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS          
SEQRES  20 B  280  THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA          
SEQRES  21 B  280  GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN          
SEQRES  22 B  280  GLU LYS PRO THR CYS LYS ALA                                  
HET    NAG  A 281      14                                                       
HET    NAG  A 282      14                                                       
HET    NAG  A 283      14                                                       
HET    NAG  A 284      14                                                       
HET    NAG  A 285      14                                                       
HET    NAG  A 286      14                                                       
HET    NAG  A 287      14                                                       
HET    FUC  A 304      10                                                       
HET    MAG  A 303      16                                                       
HET    GAL  A 302      10                                                       
HET    SIA  A 301      21                                                       
HET     CA  A 306       1                                                       
HET    NAG  B 281      14                                                       
HET    NAG  B 282      14                                                       
HET    NAG  B 283      14                                                       
HET    NAG  B 284      14                                                       
HET    NAG  B 285      14                                                       
HET    NAG  B 286      14                                                       
HET    NAG  B 287      14                                                       
HET    FUC  B 304      10                                                       
HET    MAG  B 303      16                                                       
HET    GAL  B 302      10                                                       
HET    SIA  B 301      21                                                       
HET     CA  B 306       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     MAG BETA-METHYL-N-ACETYL-D-GLUCOSAMINE                               
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   4  GAL    2(C6 H12 O6)                                                 
FORMUL   5  NAG    14(C8 H15 N O6)                                              
FORMUL   6  MAG    2(C9 H17 N O6)                                               
FORMUL   7  SIA    2(C11 H19 N O9)                                              
FORMUL   8  HOH   *127(H2 O)                                                    
HELIX    1   1 THR A   11  ARG A   22  1                                  12    
HELIX    2   2 ASN A   31  LEU A   42  1                                  12    
HELIX    3   3 THR B   11  ARG B   22  1                                  12    
HELIX    4   4 ASN B   31  LEU B   42  1                                  12    
SHEET    1  AA 2 SER A   2  THR A   5  0                                        
SHEET    2  AA 2 LEU A 114  THR A 119 -1  O  CYS A 117   N  ASN A   4           
SHEET    1  AB 2 HIS A  25  LEU A  26  0                                        
SHEET    2  AB 2 LEU A 114  THR A 119 -1  O  TYR A 118   N  HIS A  25           
SHEET    1  AC 5 LYS A  67  PRO A  68  0                                        
SHEET    2  AC 5 VAL A  59  TRP A  62  1  N  TRP A  62   O  LYS A  67           
SHEET    3  AC 5 TYR A  49  VAL A  56 -1  O  ARG A  54   N  VAL A  61           
SHEET    4  AC 5 CYS A  90  ILE A  93 -1  O  VAL A  91   N  ILE A  51           
SHEET    5  AC 5 TRP A 104  GLU A 107 -1  O  ASN A 105   N  GLU A  92           
SHEET    1  AD 5 LYS A  67  PRO A  68  0                                        
SHEET    2  AD 5 VAL A  59  TRP A  62  1  N  TRP A  62   O  LYS A  67           
SHEET    3  AD 5 TYR A  49  VAL A  56 -1  O  ARG A  54   N  VAL A  61           
SHEET    4  AD 5 LEU A 114  THR A 119  1  O  LEU A 114   N  TRP A  50           
SHEET    5  AD 5 HIS A  25  LEU A  26 -1  O  HIS A  25   N  TYR A 118           
SHEET    1  AE 2 GLY A 131  GLU A 135  0                                        
SHEET    2  AE 2 TYR A 140  CYS A 144 -1  O  THR A 141   N  VAL A 134           
SHEET    1  AF 2 PHE A 148  SER A 149  0                                        
SHEET    2  AF 2 GLN A 155  ILE A 156 -1  O  GLN A 155   N  SER A 149           
SHEET    1  AG 3 GLY A 168  SER A 173  0                                        
SHEET    2  AG 3 SER A 184  CYS A 189 -1  O  SER A 184   N  SER A 173           
SHEET    3  AG 3 MET A 201  GLN A 202 -1  O  MET A 201   N  CYS A 185           
SHEET    1  AH 2 TYR A 193  PRO A 195  0                                        
SHEET    2  AH 2 CYS A 216  VAL A 218 -1  O  ASN A 217   N  LEU A 194           
SHEET    1  AI 3 GLY A 230  GLU A 233  0                                        
SHEET    2  AI 3 THR A 246  CYS A 251 -1  O  THR A 248   N  GLU A 233           
SHEET    3  AI 3 SER A 262  GLN A 264 -1  O  LEU A 263   N  CYS A 247           
SHEET    1  AJ 2 GLU A 256  MET A 258  0                                        
SHEET    2  AJ 2 THR A 277  LYS A 279 -1  O  THR A 277   N  MET A 258           
SHEET    1  BA 2 SER B   2  THR B   5  0                                        
SHEET    2  BA 2 LEU B 114  THR B 119 -1  O  CYS B 117   N  ASN B   4           
SHEET    1  BB 2 HIS B  25  LEU B  26  0                                        
SHEET    2  BB 2 LEU B 114  THR B 119 -1  O  TYR B 118   N  HIS B  25           
SHEET    1  BC 5 LYS B  67  PRO B  68  0                                        
SHEET    2  BC 5 VAL B  59  TRP B  62  1  N  TRP B  62   O  LYS B  67           
SHEET    3  BC 5 TYR B  49  VAL B  56 -1  O  ARG B  54   N  VAL B  61           
SHEET    4  BC 5 CYS B  90  ILE B  93 -1  O  VAL B  91   N  ILE B  51           
SHEET    5  BC 5 TRP B 104  GLU B 107 -1  O  ASN B 105   N  GLU B  92           
SHEET    1  BD 5 LYS B  67  PRO B  68  0                                        
SHEET    2  BD 5 VAL B  59  TRP B  62  1  N  TRP B  62   O  LYS B  67           
SHEET    3  BD 5 TYR B  49  VAL B  56 -1  O  ARG B  54   N  VAL B  61           
SHEET    4  BD 5 LEU B 114  THR B 119  1  O  LEU B 114   N  TRP B  50           
SHEET    5  BD 5 HIS B  25  LEU B  26 -1  O  HIS B  25   N  TYR B 118           
SHEET    1  BE 2 GLY B 131  GLU B 135  0                                        
SHEET    2  BE 2 TYR B 140  CYS B 144 -1  O  THR B 141   N  VAL B 134           
SHEET    1  BF 2 PHE B 148  SER B 149  0                                        
SHEET    2  BF 2 GLN B 155  ILE B 156 -1  O  GLN B 155   N  SER B 149           
SHEET    1  BG 3 GLY B 168  SER B 173  0                                        
SHEET    2  BG 3 SER B 184  CYS B 189 -1  O  SER B 184   N  SER B 173           
SHEET    3  BG 3 MET B 201  GLN B 202 -1  O  MET B 201   N  CYS B 185           
SHEET    1  BH 2 TYR B 193  PRO B 195  0                                        
SHEET    2  BH 2 CYS B 216  VAL B 218 -1  O  ASN B 217   N  LEU B 194           
SHEET    1  BI 3 GLY B 230  GLU B 233  0                                        
SHEET    2  BI 3 THR B 246  CYS B 251 -1  O  THR B 248   N  GLU B 233           
SHEET    3  BI 3 SER B 262  GLN B 264 -1  O  LEU B 263   N  CYS B 247           
SHEET    1  BJ 2 LEU B 257  MET B 258  0                                        
SHEET    2  BJ 2 THR B 277  CYS B 278 -1  O  THR B 277   N  MET B 258           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.06  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.06  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.06  
SSBOND   4 CYS A  127    CYS A  142                          1555   1555  2.05  
SSBOND   5 CYS A  144    CYS A  153                          1555   1555  2.07  
SSBOND   6 CYS A  159    CYS A  203                          1555   1555  2.02  
SSBOND   7 CYS A  172    CYS A  185                          1555   1555  2.07  
SSBOND   8 CYS A  189    CYS A  216                          1555   1555  2.04  
SSBOND   9 CYS A  221    CYS A  265                          1555   1555  2.03  
SSBOND  10 CYS A  234    CYS A  247                          1555   1555  2.06  
SSBOND  11 CYS A  251    CYS A  278                          1555   1555  2.04  
SSBOND  12 CYS B   19    CYS B  117                          1555   1555  2.06  
SSBOND  13 CYS B   90    CYS B  109                          1555   1555  2.05  
SSBOND  14 CYS B  122    CYS B  133                          1555   1555  2.05  
SSBOND  15 CYS B  127    CYS B  142                          1555   1555  2.05  
SSBOND  16 CYS B  144    CYS B  153                          1555   1555  2.07  
SSBOND  17 CYS B  159    CYS B  203                          1555   1555  2.03  
SSBOND  18 CYS B  172    CYS B  185                          1555   1555  2.06  
SSBOND  19 CYS B  189    CYS B  216                          1555   1555  2.04  
SSBOND  20 CYS B  221    CYS B  265                          1555   1555  2.02  
SSBOND  21 CYS B  234    CYS B  247                          1555   1555  2.06  
SSBOND  22 CYS B  251    CYS B  278                          1555   1555  2.04  
LINK         ND2 ASN A   4                 C1  NAG A 285     1555   1555  1.43  
LINK         ND2 ASN A 124                 C1  NAG A 286     1555   1555  1.43  
LINK         ND2 ASN A 139                 C1  NAG A 282     1555   1555  1.44  
LINK         ND2 ASN A 158                 C1  NAG A 283     1555   1555  1.43  
LINK         ND2 ASN A 178                 C1  NAG A 284     1555   1555  1.44  
LINK         ND2 ASN A 182                 C1  NAG A 281     1555   1555  1.43  
LINK         ND2 ASN A 244                 C1  NAG A 287     1555   1555  1.43  
LINK         O2  SIA A 301                 C3  GAL A 302     1555   1555  1.47  
LINK         C1  GAL A 302                 O4  MAG A 303     1555   1555  1.43  
LINK         O3  MAG A 303                 C1  FUC A 304     1555   1555  1.47  
LINK        CA    CA A 306                 OD1 ASN A  82     1555   1555  2.49  
LINK        CA    CA A 306                 OE1 GLU A  80     1555   1555  2.94  
LINK        CA    CA A 306                 O   ASP A 106     1555   1555  2.54  
LINK        CA    CA A 306                 O3  FUC A 304     1555   1555  2.13  
LINK        CA    CA A 306                 OD1 ASP A 106     1555   1555  2.25  
LINK        CA    CA A 306                 OE1 GLU A  88     1555   1555  2.51  
LINK        CA    CA A 306                 OD1 ASN A 105     1555   1555  2.61  
LINK        CA    CA A 306                 O4  FUC A 304     1555   1555  2.58  
LINK         ND2 ASN B   4                 C1  NAG B 285     1555   1555  1.43  
LINK         ND2 ASN B 124                 C1  NAG B 286     1555   1555  1.42  
LINK         ND2 ASN B 139                 C1  NAG B 282     1555   1555  1.44  
LINK         ND2 ASN B 158                 C1  NAG B 283     1555   1555  1.43  
LINK         ND2 ASN B 178                 C1  NAG B 284     1555   1555  1.43  
LINK         ND2 ASN B 182                 C1  NAG B 281     1555   1555  1.43  
LINK         ND2 ASN B 244                 C1  NAG B 287     1555   1555  1.43  
LINK         O2  SIA B 301                 C3  GAL B 302     1555   1555  1.47  
LINK         C1  GAL B 302                 O4  MAG B 303     1555   1555  1.43  
LINK         O3  MAG B 303                 C1  FUC B 304     1555   1555  1.47  
LINK        CA    CA B 306                 O4  FUC B 304     1555   1555  2.58  
LINK        CA    CA B 306                 O3  FUC B 304     1555   1555  2.11  
LINK        CA    CA B 306                 OD1 ASN B 105     1555   1555  2.59  
LINK        CA    CA B 306                 OD1 ASN B  82     1555   1555  2.46  
LINK        CA    CA B 306                 OE1 GLU B  80     1555   1555  3.00  
LINK        CA    CA B 306                 OD1 ASP B 106     1555   1555  2.30  
LINK        CA    CA B 306                 O   ASP B 106     1555   1555  2.57  
LINK        CA    CA B 306                 OE1 GLU B  88     1555   1555  2.51  
CISPEP   1 GLU A   80    PRO A   81          0        -3.70                     
CISPEP   2 GLU B   80    PRO B   81          0        -2.98                     
SITE     1 AC1  6 GLU A  80  ASN A  82  GLU A  88  ASN A 105                    
SITE     2 AC1  6 ASP A 106  FUC A 304                                          
SITE     1 AC2  6 GLU B  80  ASN B  82  GLU B  88  ASN B 105                    
SITE     2 AC2  6 ASP B 106  FUC B 304                                          
SITE     1 AC3  5 ASN A   4  ARG A  22  GLU A 208  LEU B 151                    
SITE     2 AC3  5 NAG B 282                                                     
SITE     1 AC4  3 ASN A 124  GLU B  71  LYS B  74                               
SITE     1 AC5  3 ASN A 139  TYR A 140  NAG B 285                               
SITE     1 AC6 10 SER A 149  GLN A 155  ILE A 156  ASN A 158                    
SITE     2 AC6 10 PRO A 238  NAG A 284  HOH A2037  HOH A2056                    
SITE     3 AC6 10 ASN B 158  NAG B 283                                          
SITE     1 AC7 10 ASN A 178  VAL A 224  THR A 225  VAL A 232                    
SITE     2 AC7 10 CYS A 234  PHE A 241  NAG A 283  HOH A2048                    
SITE     3 AC7 10 GLU B 233  NAG B 284                                          
SITE     1 AC8  1 ASN A 182                                                     
SITE     1 AC9  3 TYR A 193  TRP A 243  ASN A 244                               
SITE     1 BC1  5 LEU A 151  NAG A 282  ASN B   4  ARG B  22                    
SITE     2 BC1  5 HOH B2001                                                     
SITE     1 BC2  4 GLU A  71  LYS A  74  ASN B 124  HOH B2021                    
SITE     1 BC3  3 NAG A 285  ASN B 139  TYR B 140                               
SITE     1 BC4 10 ASN A 158  NAG A 283  HOH A2028  SER B 149                    
SITE     2 BC4 10 GLN B 155  ILE B 156  ASN B 158  PRO B 238                    
SITE     3 BC4 10 HOH B2040  HOH B2041                                          
SITE     1 BC5 12 NAG A 284  HOH A2049  ASN B 178  ALA B 223                    
SITE     2 BC5 12 VAL B 224  VAL B 232  GLU B 233  CYS B 234                    
SITE     3 BC5 12 GLY B 239  PHE B 241  HOH B2040  HOH B2060                    
SITE     1 BC6  1 ASN B 182                                                     
SITE     1 BC7  3 TYR B 193  TRP B 243  ASN B 244                               
SITE     1 BC8 13 TYR A  48  GLU A  80  ASN A  82  ARG A  84                    
SITE     2 BC8 13 GLN A  85  GLU A  88  GLU A  92  TYR A  94                    
SITE     3 BC8 13 ARG A  97  ASN A 105  ASP A 106  GLU A 107                    
SITE     4 BC8 13  CA A 306                                                     
SITE     1 BC9 27 TYR A  48  GLU A  80  ASN A  82  ARG A  84                    
SITE     2 BC9 27 GLN A  85  GLU A  88  GLU A  92  TYR A  94                    
SITE     3 BC9 27 ARG A  97  ASN A 105  ASP A 106  GLU A 107                    
SITE     4 BC9 27  CA A 306  TYR B  48  GLU B  80  ASN B  82                    
SITE     5 BC9 27 ARG B  84  GLN B  85  GLU B  88  GLU B  92                    
SITE     6 BC9 27 TYR B  94  ARG B  97  GLU B  98  ASN B 105                    
SITE     7 BC9 27 ASP B 106  GLU B 107   CA B 306                               
CRYST1   52.290   58.670   58.870  76.03  86.28  86.31 P 1           2          
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      0.019124 -0.001233 -0.000978        0.00000                         
SCALE2      0.000000  0.017080 -0.004190        0.00000                         
SCALE3      0.000000  0.000000  0.017527        0.00000                         
MTRIX1   1 -1.000000 -0.005513 -0.005256       -0.36500    1                    
MTRIX2   1  0.006443 -0.244200 -0.969700        1.47536    1                    
MTRIX3   1  0.004063 -0.969700  0.244200        1.22574    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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