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Database: PDB
Entry: 1G1R
LinkDB: 1G1R
Original site: 1G1R 
HEADER    IMMUNE SYSTEM, MEMBRANE PROTEIN         13-OCT-00   1G1R              
TITLE     CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                    
TITLE    2 COMPLEXED WITH SLEX                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P-SELECTIN;                                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: LECTIN/EGF DOMAINS;                                        
COMPND   5 SYNONYM: GRANULE MEMBRANE PROTEIN 140, GMP-140, PADGEM,              
COMPND   6 CD62P, LEUKOCYTE-ENDOTHELIAL CELL ADHESION MOLECULE 3,               
COMPND   7 LECAM3;                                                              
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 1G1R    1       VERSN                                    
REVDAT   2   01-APR-03 1G1R    1       JRNL                                     
REVDAT   1   13-OCT-01 1G1R    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.    3.40 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) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.00                          
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             : 11667                          
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) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 583                             
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            : 5264                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 175                                     
REMARK   3   SOLVENT ATOMS            : 16                                      
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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 1G1R 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 RCSB012125.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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                         : YALE/MSC MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11667                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.790                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.79                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
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   (%): 56.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, NACL, CACL2, 2-METHYL-2,       
REMARK 280  4-PENTANEDIOL, PEG 6000, PH 8.5, VAPOR DIFFUSION, HANGING DROP      
REMARK 280  AT 291K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       30.26000            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   161                                                      
REMARK 465     LYS A   162                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     LYS B   162                                                      
REMARK 465     ASP C   160                                                      
REMARK 465     ASP C   161                                                      
REMARK 465     LYS C   162                                                      
REMARK 465     ASP D   161                                                      
REMARK 465     LYS D   162                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     ASP A 159    CG   OD1  OD2                                       
REMARK 470     ASP A 160    CG   OD1  OD2                                       
REMARK 470     ASP B 159    CG   OD1  OD2                                       
REMARK 470     ASP B 160    CG   OD1  OD2                                       
REMARK 470     LYS C  17    CG   CD   CE   NZ                                   
REMARK 470     ASN C  57    CG   OD1  ND2                                       
REMARK 470     ASP C 159    CG   OD1  OD2                                       
REMARK 470     ASP D 159    CG   OD1  OD2                                       
REMARK 470     ASP D 160    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HIS A     4     N    CYS A   117              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  23     -134.90   -125.16                                   
REMARK 500    THR A  24      -60.85   -103.37                                   
REMARK 500    ASP A  25     -179.61   -177.39                                   
REMARK 500    ASP A  36      -72.54    -60.71                                   
REMARK 500    TYR A  48      178.25     58.49                                   
REMARK 500    ASN A  57     -122.23     66.93                                   
REMARK 500    GLU A  74      129.00    -36.11                                   
REMARK 500    ASN A  75       34.47   -158.29                                   
REMARK 500    ALA A  77      172.17    -58.48                                   
REMARK 500    ASN A  79      -21.47     94.28                                   
REMARK 500    ARG A  85      153.41    -49.63                                   
REMARK 500    ASN A  87       -2.96     67.48                                   
REMARK 500    TYR A  94       53.49    -66.62                                   
REMARK 500    CYS A 109      -12.14    -33.69                                   
REMARK 500    SER A 128       26.81     42.41                                   
REMARK 500    LYS A 129       -3.84     58.81                                   
REMARK 500    ILE A 137       77.38    -65.51                                   
REMARK 500    ASN A 139     -141.24   -166.41                                   
REMARK 500    ASP A 159       75.06   -102.01                                   
REMARK 500    SER B  11     -148.79    -53.52                                   
REMARK 500    TYR B  23     -136.65   -127.83                                   
REMARK 500    ASP B  25     -172.13    170.41                                   
REMARK 500    VAL B  27     -177.41    -49.41                                   
REMARK 500    TYR B  48      179.51     76.63                                   
REMARK 500    ASN B  57      -90.13     58.28                                   
REMARK 500    LYS B  58       -5.04   -140.67                                   
REMARK 500    GLU B  74      121.37    -39.75                                   
REMARK 500    ASN B  75       52.01   -163.07                                   
REMARK 500    TRP B  76     -177.87    -65.94                                   
REMARK 500    ASN B  79       60.10     67.65                                   
REMARK 500    LYS B  84      -60.67   -100.73                                   
REMARK 500    ARG B  85      162.32    -39.43                                   
REMARK 500    TYR B  94       98.79    -66.50                                   
REMARK 500    ALA B 100       63.18    175.87                                   
REMARK 500    ASN B 105      123.47    179.18                                   
REMARK 500    SER B 126      129.27     -6.20                                   
REMARK 500    SER B 128       14.87     46.25                                   
REMARK 500    GLU B 135      154.20    -49.49                                   
REMARK 500    ILE B 137       90.50    -58.64                                   
REMARK 500    ASN B 139     -125.95   -147.42                                   
REMARK 500    TYR B 140      175.98    178.55                                   
REMARK 500    CYS B 144      135.11    -15.94                                   
REMARK 500    TYR C  23     -127.33   -136.71                                   
REMARK 500    ASP C  25     -176.76    167.87                                   
REMARK 500    VAL C  27      149.07    -34.32                                   
REMARK 500    SER C  46      -19.42    -49.80                                   
REMARK 500    TYR C  48     -173.91     61.77                                   
REMARK 500    ASN C  56       64.38   -111.28                                   
REMARK 500    ASN C  57      114.96     69.27                                   
REMARK 500    LYS C  58      -40.64     50.65                                   
REMARK 500    GLU C  74      119.43    -38.82                                   
REMARK 500    PRO C  81     -170.72    -64.98                                   
REMARK 500    ASN C  82       -0.69   -165.40                                   
REMARK 500    ARG C  85      154.24    -48.21                                   
REMARK 500    ASN C  87        6.56     51.86                                   
REMARK 500    TYR C  94       71.29    -65.10                                   
REMARK 500    SER C  99      -63.34   -100.23                                   
REMARK 500    LYS C 103      158.70    -44.42                                   
REMARK 500    GLU C 107     -165.43   -127.60                                   
REMARK 500    CYS C 109      -14.43    -48.23                                   
REMARK 500    CYS C 127       15.15     55.59                                   
REMARK 500    LYS C 129       18.68     49.30                                   
REMARK 500    ASN C 139     -135.85   -129.54                                   
REMARK 500    TYR C 140      144.39   -179.11                                   
REMARK 500    CYS C 144      129.03      1.53                                   
REMARK 500    PRO C 146      132.41    -37.83                                   
REMARK 500    CYS C 153       28.98     47.51                                   
REMARK 500    ARG C 157      146.06    -38.82                                   
REMARK 500    THR D   7       18.40    -62.32                                   
REMARK 500    TYR D  18      -17.42    -47.56                                   
REMARK 500    ASN D  21      -81.25    -76.35                                   
REMARK 500    TYR D  23     -150.66   -128.07                                   
REMARK 500    ASP D  25     -158.52    177.32                                   
REMARK 500    VAL D  27      132.97    -35.63                                   
REMARK 500    ASN D  31      130.21   -172.88                                   
REMARK 500    LYS D  32      -37.16    -29.68                                   
REMARK 500    ASN D  39       -0.31    -46.37                                   
REMARK 500    TYR D  48     -153.38     77.84                                   
REMARK 500    ASN D  56      -99.63    -93.97                                   
REMARK 500    LYS D  58       -0.58    175.96                                   
REMARK 500    TRP D  60      178.58    -59.08                                   
REMARK 500    LYS D  66       -6.05     77.67                                   
REMARK 500    LEU D  69      145.26    -36.77                                   
REMARK 500    GLU D  74      108.51    -42.27                                   
REMARK 500    TRP D  76     -134.45    -62.35                                   
REMARK 500    ASN D  79      -23.91     88.24                                   
REMARK 500    ASN D  82      -54.54   -153.40                                   
REMARK 500    ASN D  87       17.90     86.75                                   
REMARK 500    TYR D  94       71.48    -66.25                                   
REMARK 500    SER D  99      -73.74    -88.07                                   
REMARK 500    CYS D 109      -11.18    -36.42                                   
REMARK 500    LYS D 111     -174.40    -58.15                                   
REMARK 500    GLN D 123     -115.54    -88.94                                   
REMARK 500    ASP D 124      -66.94   -121.60                                   
REMARK 500    MET D 125       -3.69    -54.88                                   
REMARK 500    SER D 128       45.06     33.59                                   
REMARK 500    LYS D 129       16.19     44.09                                   
REMARK 500    ILE D 137       98.77    -68.67                                   
REMARK 500    ASN D 139     -129.41   -173.37                                   
REMARK 500    TYR D 140     -177.83    168.67                                   
REMARK 500    PRO D 146      129.38    -37.16                                   
REMARK 500    ASP D 158      -72.12   -103.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  49         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 105   OD1                                                    
REMARK 620 2 ASP A 106   O    77.2                                              
REMARK 620 3 GLU A  80   OE1  84.6 131.0                                        
REMARK 620 4 GLU A  80   OE2  54.2 130.8  45.7                                  
REMARK 620 5 ASN A  82   OD1 137.9 141.1  57.9  84.3                            
REMARK 620 6 FUC A 904   O3   61.2  86.0 123.6  78.1 122.3                      
REMARK 620 7 FUC A 904   O4   82.8 140.4  79.7  48.5  72.9  54.4                
REMARK 620 8 ASN A  83   ND2 128.8  51.9 130.8 176.3  92.4 105.2 132.0          
REMARK 620 9 ASP A 106   OD1  92.9  75.2  60.6  97.6  85.1 151.1 140.2  80.4    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  80   OE1                                                    
REMARK 620 2 ASN B  82   OD1  86.5                                              
REMARK 620 3 ASN B  83   ND2 148.4  87.2                                        
REMARK 620 4 FUC B 904   O4   66.8  52.3 129.7                                  
REMARK 620 5 ASN B 105   OD1  66.3 117.7 142.1  65.5                            
REMARK 620 6 ASN B  82   ND2  45.3  41.3 123.0  44.1  92.3                      
REMARK 620 7 FUC B 904   O3  112.3  82.2  97.5  54.0  61.6  97.1                
REMARK 620 8 ASP B 106   OD2 106.7 108.9  47.1 159.1 131.8 116.8 140.1          
REMARK 620 9 ASP B 106   OD1  70.9 126.1  88.2 137.7  97.3 103.1 151.5  41.6    
REMARK 620 10 ASP B 106   O   120.4 145.5  79.7 115.6  63.5 155.4  68.3         
REMARK 620  85.0  85.5                                                          
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620     9                                                                
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  80   OE1                                                    
REMARK 620 2 ASN C 105   OD1  56.8                                              
REMARK 620 3 ASN C 105   ND2  98.0  43.7                                        
REMARK 620 4 ASP C 106   O   111.1  81.0  76.3                                  
REMARK 620 5 ASN C  82   OD1  50.8 105.3 148.6 108.5                            
REMARK 620 6 GLU C  80   OE2  41.1  54.4  75.4 134.9  80.5                      
REMARK 620 7 ASP C 106   OD1  55.9  69.8 104.5  59.7  57.5  94.9                
REMARK 620 8 ASN C  83   ND2 111.0 132.0 133.2  59.5  67.6 148.1  67.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 804  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 106   O                                                      
REMARK 620 2 ASN D  83   ND2  52.8                                              
REMARK 620 3 ASN D 105   OD1  79.3 130.2                                        
REMARK 620 4 ASN D  82   OD1 128.2  84.5 143.6                                  
REMARK 620 5 GLU D  80   OE1 138.2 166.4  59.0  89.4                            
REMARK 620 6 FUC D 904   O4  124.8 111.6  82.8  95.1  56.9                      
REMARK 620 7 ASP D 106   OD1  73.5  75.1 106.7  67.6 113.6 161.2                
REMARK 620 8 FUC D 904   O3   74.7  74.2  81.3 125.0  99.8  51.0 145.0          
REMARK 620 9 GLU D  80   OE2 136.2 141.7  81.5  62.2  40.8  90.9  75.0 139.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
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 901                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A 902                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAG A 903                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 904                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 901                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B 902                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAG B 903                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 904                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA D 901                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 902                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAG D 903                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC D 904                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 801                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 803                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 804                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 805                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 806                 
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: 1G1S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
REMARK 900 RELATED ID: 1G1T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E-SELECTIN                                      
DBREF  1G1R A    1   158  UNP    P16109   LEM3_HUMAN      42    199             
DBREF  1G1R B    1   158  UNP    P16109   LEM3_HUMAN      42    199             
DBREF  1G1R C    1   158  UNP    P16109   LEM3_HUMAN      42    199             
DBREF  1G1R D    1   158  UNP    P16109   LEM3_HUMAN      42    199             
SEQADV 1G1R ASP A  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1R ASP A  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP A  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP A  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R LYS A  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP B  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1R ASP B  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP B  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP B  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R LYS B  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP C  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1R ASP C  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP C  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP C  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R LYS C  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP D  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1R ASP D  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP D  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R ASP D  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1R LYS D  162  UNP  P16109              CLONING ARTIFACT               
SEQRES   1 A  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 A  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 A  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 A  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 A  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 A  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 A  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 A  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 A  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 A  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 A  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 A  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 A  162  ARG ASP ASP ASP ASP LYS                                      
SEQRES   1 B  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 B  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 B  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 B  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 B  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 B  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 B  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 B  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 B  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 B  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 B  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 B  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 B  162  ARG ASP ASP ASP ASP LYS                                      
SEQRES   1 C  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 C  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 C  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 C  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 C  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 C  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 C  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 C  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 C  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 C  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 C  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 C  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 C  162  ARG ASP ASP ASP ASP LYS                                      
SEQRES   1 D  162  TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN          
SEQRES   2 D  162  ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU          
SEQRES   3 D  162  VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN          
SEQRES   4 D  162  LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY          
SEQRES   5 D  162  ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR          
SEQRES   6 D  162  LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP          
SEQRES   7 D  162  ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL          
SEQRES   8 D  162  GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP          
SEQRES   9 D  162  ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS          
SEQRES  10 D  162  TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN          
SEQRES  11 D  162  GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER          
SEQRES  12 D  162  CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL          
SEQRES  13 D  162  ARG ASP ASP ASP ASP LYS                                      
HET    SIA  A 901      20                                                       
HET    GAL  A 902      11                                                       
HET    MAG  A 903      16                                                       
HET    FUC  A 904      10                                                       
HET    SIA  B 901      20                                                       
HET    GAL  B 902      11                                                       
HET    MAG  B 903      16                                                       
HET    FUC  B 904      10                                                       
HET    SIA  D 901      20                                                       
HET    GAL  D 902      11                                                       
HET    MAG  D 903      16                                                       
HET    FUC  D 904      10                                                       
HET     CA  A 801       1                                                       
HET     CA  B 802       1                                                       
HET     CA  C 803       1                                                       
HET     CA  D 804       1                                                       
HET    MRD  C 805       8                                                       
HET    MRD  A 806       8                                                       
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                                                      
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   5  SIA    3(C11 H19 N O9)                                              
FORMUL   5  GAL    3(C6 H12 O6)                                                 
FORMUL   5  MAG    3(C9 H17 N O6)                                               
FORMUL   5  FUC    3(C6 H12 O5)                                                 
FORMUL   8   CA    4(CA 2+)                                                     
FORMUL  12  MRD    2(C6 H14 O2)                                                 
HELIX    1   1 SER A   11  TYR A   23  1                                  13    
HELIX    2   2 ASN A   31  LEU A   42  1                                  12    
HELIX    3   3 MET A  125  LYS A  129  5                                   5    
HELIX    4   4 TRP B   12  TYR B   23  1                                  12    
HELIX    5   5 ASN B   31  LEU B   42  1                                  12    
HELIX    6   6 SER B  126  LYS B  129  5                                   4    
HELIX    7   7 SER C   11  TYR C   23  1                                  13    
HELIX    8   8 ASN C   31  LEU C   42  1                                  12    
HELIX    9   9 MET C  125  GLN C  130  5                                   6    
HELIX   10  10 SER D   11  TYR D   23  1                                  13    
HELIX   11  11 ASN D   31  LEU D   42  1                                  12    
HELIX   12  12 MET D  125  GLN D  130  5                                   6    
SHEET    1   A 3 THR A   2  TYR A   5  0                                        
SHEET    2   A 3 HIS A 114  THR A 119 -1  N  CYS A 117   O  HIS A   4           
SHEET    3   A 3 ASP A  25  LEU A  26 -1  O  ASP A  25   N  TYR A 118           
SHEET    1   B 5 THR A   2  TYR A   5  0                                        
SHEET    2   B 5 HIS A 114  THR A 119 -1  N  CYS A 117   O  HIS A   4           
SHEET    3   B 5 TYR A  49  TRP A  50  1  O  TRP A  50   N  LEU A 116           
SHEET    4   B 5 CYS A  90  ILE A  93 -1  N  ILE A  93   O  TYR A  49           
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  ASN A  56  0                                        
SHEET    2   C 2 THR A  59  TRP A  62 -1  O  THR A  59   N  ASN 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  TYR A 149  0                                        
SHEET    2   E 2 TYR A 155  VAL A 156 -1  O  TYR A 155   N  TYR A 149           
SHEET    1   F 3 THR B   2  TYR B   5  0                                        
SHEET    2   F 3 HIS B 114  THR B 119 -1  N  CYS B 117   O  HIS B   4           
SHEET    3   F 3 ASP B  25  LEU B  26 -1  O  ASP B  25   N  TYR B 118           
SHEET    1   G 5 THR B   2  TYR B   5  0                                        
SHEET    2   G 5 HIS B 114  THR B 119 -1  N  CYS B 117   O  HIS B   4           
SHEET    3   G 5 TYR B  49  TRP B  50  1  N  TRP B  50   O  HIS B 114           
SHEET    4   G 5 CYS B  90  ILE B  93 -1  N  ILE B  93   O  TYR B  49           
SHEET    5   G 5 TRP B 104  GLU B 107 -1  O  ASN B 105   N  GLU B  92           
SHEET    1   H 2 ILE B  53  ASN B  56  0                                        
SHEET    2   H 2 THR B  59  TRP B  62 -1  N  THR B  59   O  ASN B  56           
SHEET    1   I 2 GLY B 131  THR B 136  0                                        
SHEET    2   I 2 ASN B 139  CYS B 144 -1  O  ASN B 139   N  THR B 136           
SHEET    1   J 2 PHE B 148  TYR B 149  0                                        
SHEET    2   J 2 TYR B 155  VAL B 156 -1  N  TYR B 155   O  TYR B 149           
SHEET    1   K 3 THR C   2  TYR C   5  0                                        
SHEET    2   K 3 HIS C 114  THR C 119 -1  N  CYS C 117   O  HIS C   4           
SHEET    3   K 3 ASP C  25  LEU C  26 -1  O  ASP C  25   N  TYR C 118           
SHEET    1   L 5 THR C   2  TYR C   5  0                                        
SHEET    2   L 5 HIS C 114  THR C 119 -1  N  CYS C 117   O  HIS C   4           
SHEET    3   L 5 TYR C  49  ILE C  51  1  N  TRP C  50   O  HIS C 114           
SHEET    4   L 5 CYS C  90  ILE C  93 -1  O  VAL C  91   N  ILE C  51           
SHEET    5   L 5 TRP C 104  GLU C 107 -1  O  ASN C 105   N  GLU C  92           
SHEET    1   M 3 ARG C  54  LYS C  55  0                                        
SHEET    2   M 3 TRP C  60  TRP C  62 -1  O  THR C  61   N  ARG C  54           
SHEET    3   M 3 LYS C  67  ALA C  68 -1  O  LYS C  67   N  TRP C  62           
SHEET    1   N 2 CYS C 133  GLU C 135  0                                        
SHEET    2   N 2 TYR C 140  CYS C 142 -1  N  THR C 141   O  LEU C 134           
SHEET    1   O 2 PHE C 148  TYR C 149  0                                        
SHEET    2   O 2 TYR C 155  VAL C 156 -1  N  TYR C 155   O  TYR C 149           
SHEET    1   P 5 TRP D 104  GLU D 107  0                                        
SHEET    2   P 5 CYS D  90  ILE D  93 -1  O  CYS D  90   N  GLU D 107           
SHEET    3   P 5 TYR D  49  ARG D  54 -1  O  TYR D  49   N  ILE D  93           
SHEET    4   P 5 HIS D 114  THR D 119  1  O  HIS D 114   N  TRP D  50           
SHEET    5   P 5 THR D   2  TYR D   5 -1  O  THR D   2   N  THR D 119           
SHEET    1   Q 5 TRP D 104  GLU D 107  0                                        
SHEET    2   Q 5 CYS D  90  ILE D  93 -1  O  CYS D  90   N  GLU D 107           
SHEET    3   Q 5 TYR D  49  ARG D  54 -1  O  TYR D  49   N  ILE D  93           
SHEET    4   Q 5 HIS D 114  THR D 119  1  O  HIS D 114   N  TRP D  50           
SHEET    5   Q 5 ASP D  25  LEU D  26 -1  O  ASP D  25   N  TYR D 118           
SHEET    1   R 2 GLU D 132  THR D 136  0                                        
SHEET    2   R 2 ASN D 139  SER D 143 -1  N  ASN D 139   O  THR D 136           
SHEET    1   S 2 PHE D 148  TYR D 149  0                                        
SHEET    2   S 2 TYR D 155  VAL D 156 -1  O  TYR D 155   N  TYR D 149           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.03  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.00  
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  
SSBOND   6 CYS B   19    CYS B  117                          1555   1555  2.03  
SSBOND   7 CYS B   90    CYS B  109                          1555   1555  2.03  
SSBOND   8 CYS B  122    CYS B  133                          1555   1555  2.02  
SSBOND   9 CYS B  127    CYS B  142                          1555   1555  2.02  
SSBOND  10 CYS B  144    CYS B  153                          1555   1555  2.01  
SSBOND  11 CYS C   19    CYS C  117                          1555   1555  2.02  
SSBOND  12 CYS C   90    CYS C  109                          1555   1555  2.03  
SSBOND  13 CYS C  122    CYS C  133                          1555   1555  2.04  
SSBOND  14 CYS C  127    CYS C  142                          1555   1555  2.02  
SSBOND  15 CYS C  144    CYS C  153                          1555   1555  2.02  
SSBOND  16 CYS D   19    CYS D  117                          1555   1555  2.03  
SSBOND  17 CYS D   90    CYS D  109                          1555   1555  2.03  
SSBOND  18 CYS D  122    CYS D  133                          1555   1555  2.01  
SSBOND  19 CYS D  127    CYS D  142                          1555   1555  2.03  
SSBOND  20 CYS D  144    CYS D  153                          1555   1555  2.02  
LINK         O4  MAG A 903                 C1  GAL A 902     1555   1555  1.42  
LINK         C1  FUC B 904                 O3  MAG B 903     1555   1555  1.42  
LINK         O4  MAG B 903                 C1  GAL B 902     1555   1555  1.42  
LINK         C1  FUC D 904                 O3  MAG D 903     1555   1555  1.43  
LINK         O3  GAL B 902                 C2  SIA B 901     1555   1555  1.45  
LINK         C1  GAL D 902                 O4  MAG D 903     1555   1555  1.45  
LINK         O3  MAG A 903                 C1  FUC A 904     1555   1555  1.45  
LINK         O3  GAL A 902                 C2  SIA A 901     1555   1555  1.46  
LINK         C2  SIA D 901                 O3  GAL D 902     1555   1555  1.47  
LINK        CA    CA A 801                 OD1 ASN A 105     1555   1555  2.50  
LINK        CA    CA A 801                 O   ASP A 106     1555   1555  2.39  
LINK        CA    CA A 801                 OE1 GLU A  80     1555   1555  2.88  
LINK        CA    CA A 801                 OE2 GLU A  80     1555   1555  2.76  
LINK        CA    CA A 801                 OD1 ASN A  82     1555   1555  1.98  
LINK        CA    CA A 801                 O3  FUC A 904     1555   1555  2.71  
LINK        CA    CA A 801                 O4  FUC A 904     1555   1555  3.12  
LINK        CA    CA A 801                 ND2 ASN A  83     1555   1555  3.05  
LINK        CA    CA A 801                 OD1 ASP A 106     1555   1555  2.32  
LINK        CA    CA B 802                 OE1 GLU B  80     1555   1555  3.08  
LINK        CA    CA B 802                 OD1 ASN B  82     1555   1555  3.17  
LINK        CA    CA B 802                 ND2 ASN B  83     1555   1555  2.79  
LINK        CA    CA B 802                 O4  FUC B 904     1555   1555  3.29  
LINK        CA    CA B 802                 OD1 ASN B 105     1555   1555  2.68  
LINK        CA    CA B 802                 ND2 ASN B  82     1555   1555  3.14  
LINK        CA    CA B 802                 O3  FUC B 904     1555   1555  2.19  
LINK        CA    CA B 802                 OD2 ASP B 106     1555   1555  3.33  
LINK        CA    CA B 802                 OD1 ASP B 106     1555   1555  2.45  
LINK        CA    CA B 802                 O   ASP B 106     1555   1555  2.84  
LINK        CA    CA C 803                 OE1 GLU C  80     1555   1555  3.11  
LINK        CA    CA C 803                 OD1 ASN C 105     1555   1555  2.22  
LINK        CA    CA C 803                 ND2 ASN C 105     1555   1555  3.25  
LINK        CA    CA C 803                 O   ASP C 106     1555   1555  2.54  
LINK        CA    CA C 803                 OD1 ASN C  82     1555   1555  2.55  
LINK        CA    CA C 803                 OE2 GLU C  80     1555   1555  3.15  
LINK        CA    CA C 803                 OD1 ASP C 106     1555   1555  2.58  
LINK        CA    CA C 803                 ND2 ASN C  83     1555   1555  3.04  
LINK        CA    CA D 804                 O   ASP D 106     1555   1555  2.69  
LINK        CA    CA D 804                 ND2 ASN D  83     1555   1555  2.95  
LINK        CA    CA D 804                 OD1 ASN D 105     1555   1555  2.50  
LINK        CA    CA D 804                 OD1 ASN D  82     1555   1555  2.42  
LINK        CA    CA D 804                 OE1 GLU D  80     1555   1555  3.38  
LINK        CA    CA D 804                 O4  FUC D 904     1555   1555  3.39  
LINK        CA    CA D 804                 OD1 ASP D 106     1555   1555  2.31  
LINK        CA    CA D 804                 O3  FUC D 904     1555   1555  2.82  
LINK        CA    CA D 804                 OE2 GLU D  80     1555   1555  2.52  
CISPEP   1 GLU A   80    PRO A   81          0        -0.13                     
CISPEP   2 GLU B   80    PRO B   81          0         0.01                     
CISPEP   3 GLU C   80    PRO C   81          0        -0.53                     
CISPEP   4 GLU D   80    PRO D   81          0         0.14                     
SITE     1 AC1  3 TYR A  48  SER A  99  GAL A 902                               
SITE     1 AC2  7 GLU A  92  TYR A  94  ASN A 105  GLU A 107                    
SITE     2 AC2  7 SIA A 901  MAG A 903  FUC A 904                               
SITE     1 AC3  2 GAL A 902  FUC A 904                                          
SITE     1 AC4  8 GLU A  80  ASN A  82  ASN A 105  ASP A 106                    
SITE     2 AC4  8 GLU A 107   CA A 801  GAL A 902  MAG A 903                    
SITE     1 AC5  5 TYR B  48  TYR B  94  PRO B  98  SER B  99                    
SITE     2 AC5  5 GAL B 902                                                     
SITE     1 AC6  6 GLU B  92  TYR B  94  ASN B 105  SIA B 901                    
SITE     2 AC6  6 MAG B 903  FUC B 904                                          
SITE     1 AC7  2 GAL B 902  FUC B 904                                          
SITE     1 AC8  8 GLU B  80  ASN B  82  ASN B 105  ASP B 106                    
SITE     2 AC8  8 GLU B 107   CA B 802  GAL B 902  MAG B 903                    
SITE     1 AC9  5 TYR D  48  TYR D  94  PRO D  98  SER D  99                    
SITE     2 AC9  5 GAL D 902                                                     
SITE     1 BC1  6 GLU D  92  TYR D  94  GLU D 107  SIA D 901                    
SITE     2 BC1  6 MAG D 903  FUC D 904                                          
SITE     1 BC2  2 GAL D 902  FUC D 904                                          
SITE     1 BC3  9 GLU D  80  ASN D  82  ASN D  83  ASN D 105                    
SITE     2 BC3  9 ASP D 106  GLU D 107   CA D 804  GAL D 902                    
SITE     3 BC3  9 MAG D 903                                                     
SITE     1 BC4  6 GLU A  80  ASN A  82  ASN A  83  ASN A 105                    
SITE     2 BC4  6 ASP A 106  FUC A 904                                          
SITE     1 BC5  6 GLU B  80  ASN B  82  ASN B  83  ASN B 105                    
SITE     2 BC5  6 ASP B 106  FUC B 904                                          
SITE     1 BC6  5 GLU C  80  ASN C  82  ASN C  83  ASN C 105                    
SITE     2 BC6  5 ASP C 106                                                     
SITE     1 BC7  6 GLU D  80  ASN D  82  ASN D  83  ASN D 105                    
SITE     2 BC7  6 ASP D 106  FUC D 904                                          
SITE     1 BC8  4 THR C   2  TYR C   3  TYR C  37  GLY C 138                    
SITE     1 BC9  4 TYR A   3  TYR A  37  ILE A 137  GLY A 138                    
CRYST1   81.140   60.520   91.440  90.00 103.28  90.00 P 1 21 1      8          
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      0.012324  0.000000  0.002909        0.00000                         
SCALE2      0.000000  0.016523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011237        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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