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Database: PDB
Entry: 1G1Q
LinkDB: 1G1Q
Original site: 1G1Q 
HEADER    IMMUNE SYSTEM, MEMBRANE PROTEIN         13-OCT-00   1G1Q              
TITLE     CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                    
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, IMMUNE SYSTEM, MEMBRANE               
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.S.SOMERS,R.T.CAMPHAUSEN                                             
REVDAT   3   24-FEB-09 1G1Q    1       VERSN                                    
REVDAT   2   01-APR-03 1G1Q    1       JRNL                                     
REVDAT   1   13-OCT-01 1G1Q    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.    2.40 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) : 2.40                           
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             : 32570                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1628                            
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          : 4                                       
REMARK   3   SOLVENT ATOMS            : 150                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 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 1G1Q 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 RCSB012124.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-95                          
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   : 32570                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 7.380                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.38                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22500                            
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   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
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       30.41500            
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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS D  19   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
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     -139.05   -134.23                                   
REMARK 500    TYR A  48     -169.97     68.78                                   
REMARK 500    ASN A  57     -111.15     55.03                                   
REMARK 500    ASN A  75       47.85   -142.65                                   
REMARK 500    ALA A 100       65.89   -150.22                                   
REMARK 500    SER A 128       25.87     49.65                                   
REMARK 500    ASN A 139     -158.69   -173.35                                   
REMARK 500    TYR B  23     -135.99   -124.44                                   
REMARK 500    THR B  24      -62.00    -97.22                                   
REMARK 500    TYR B  48     -164.61     62.27                                   
REMARK 500    ASN B  57      -84.57     62.48                                   
REMARK 500    LYS B  58       14.87   -148.88                                   
REMARK 500    ASN B  75       38.90   -146.54                                   
REMARK 500    ASN B  79        3.30     82.20                                   
REMARK 500    SER B 128       18.93     56.88                                   
REMARK 500    ASN B 139     -151.88   -165.61                                   
REMARK 500    TYR C  23     -140.54   -122.07                                   
REMARK 500    ASP C  25     -171.14   -177.68                                   
REMARK 500    VAL C  27      131.76    -35.82                                   
REMARK 500    TYR C  48     -160.57     62.55                                   
REMARK 500    ASN C  56      119.44    174.35                                   
REMARK 500    LYS C  58        6.22     57.99                                   
REMARK 500    ASN C  75       44.12   -143.06                                   
REMARK 500    ASN C  79       30.56     74.18                                   
REMARK 500    ARG C  85      171.21    -58.92                                   
REMARK 500    ASN C  87       19.50     59.82                                   
REMARK 500    LYS C  96       19.95     58.78                                   
REMARK 500    SER C  99      -63.42    -96.20                                   
REMARK 500    LYS C 129       25.22     49.15                                   
REMARK 500    ASN C 139     -149.84   -151.40                                   
REMARK 500    SER D  11     -170.64    -63.30                                   
REMARK 500    TYR D  23     -140.88   -146.44                                   
REMARK 500    THR D  24      -62.23    -92.48                                   
REMARK 500    ASP D  25     -163.88   -165.92                                   
REMARK 500    TYR D  48     -172.80     76.34                                   
REMARK 500    ASN D  56     -110.43    -86.79                                   
REMARK 500    ASN D  57      -75.23    -77.63                                   
REMARK 500    LYS D  58       26.74   -141.12                                   
REMARK 500    ASN D  75       44.06   -144.72                                   
REMARK 500    ASN D  79      -25.20     87.55                                   
REMARK 500    ASN D  87       32.59     70.84                                   
REMARK 500    TYR D  94       66.50    -66.21                                   
REMARK 500    ASN D 139     -155.06    171.07                                   
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  94         0.08    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 GLU A  80   OE1                                                    
REMARK 620 2 ASN A 105   OD1  77.1                                              
REMARK 620 3 HOH A 810   O    80.1  81.0                                        
REMARK 620 4 ASN A  82   OD1  70.9 146.3  83.2                                  
REMARK 620 5 ASP A 106   O   132.4  80.2 136.3 130.0                            
REMARK 620 6 ASP A 106   OD1  73.7  99.5 152.9  81.7  69.6                      
REMARK 620 7 HOH A 857   O   153.4 118.3  81.2  88.2  73.7 120.6                
REMARK 620 N                    1     2     3     4     5     6                 
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 ASN B  82   OD1                                                    
REMARK 620 2 HOH B 833   O    68.4                                              
REMARK 620 3 ASP B 106   O   135.5  92.5                                        
REMARK 620 4 ASP B 106   OD1  77.1 112.3  73.9                                  
REMARK 620 5 HOH B 826   O    81.9  72.3 131.6 154.5                            
REMARK 620 6 GLU B  80   OE1  71.8 131.1 136.3  84.4  75.3                      
REMARK 620 7 ASN B 105   OD1 149.2 132.3  72.7 106.7  84.3  78.1                
REMARK 620 N                    1     2     3     4     5     6                 
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 ASN C 105   OD1                                                    
REMARK 620 2 ASP C 106   O    92.9                                              
REMARK 620 3 ASN C  82   OD1 136.5 128.1                                        
REMARK 620 4 ASP C 106   OD1 109.8  62.7  82.2                                  
REMARK 620 5 GLU C  80   OE1  58.9 129.2  81.3  86.7                            
REMARK 620 N                    1     2     3     4                             
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   OD1                                                    
REMARK 620 2 GLU D  80   OE2  89.6                                              
REMARK 620 3 ASN D  82   OD1  66.6  69.0                                        
REMARK 620 4 ASN D 105   OD1 107.9  77.3 145.6                                  
REMARK 620 5 ASP D 106   O    62.5 146.4 111.3  93.2                            
REMARK 620 N                    1     2     3     4                             
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 801                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 803                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 804                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 805                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
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: 1G1R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
REMARK 900 COMPLEXED WITH SLEX                                                  
REMARK 900 RELATED ID: 1G1S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS                   
REMARK 900 RELATED ID: 1G1T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E-SELECTIN                                      
DBREF  1G1Q A    1   158  UNP    P16109   LYAM3_HUMAN     42    199             
DBREF  1G1Q B    1   158  UNP    P16109   LYAM3_HUMAN     42    199             
DBREF  1G1Q C    1   158  UNP    P16109   LYAM3_HUMAN     42    199             
DBREF  1G1Q D    1   158  UNP    P16109   LYAM3_HUMAN     42    199             
SEQADV 1G1Q ASP A  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1Q ASP A  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP A  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP A  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q LYS A  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP B  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1Q ASP B  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP B  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP B  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q LYS B  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP C  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1Q ASP C  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP C  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP C  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q LYS C  162  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP D  158  UNP  P16109    GLU   199 CONFLICT                       
SEQADV 1G1Q ASP D  159  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP D  160  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q ASP D  161  UNP  P16109              CLONING ARTIFACT               
SEQADV 1G1Q 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     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      CA CALCIUM ION                                                      
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   9  MRD    2(C6 H14 O2)                                                 
FORMUL  11  HOH   *134(H2 O)                                                    
HELIX    1   1 SER A   11  TYR A   23  1                                  13    
HELIX    2   2 ASN A   31  LEU A   42  1                                  12    
HELIX    3   3 MET A  125  LYS A  129  5                                   5    
HELIX    4   4 SER B   11  TYR B   23  1                                  13    
HELIX    5   5 ASN B   31  LEU B   42  1                                  12    
HELIX    6   6 MET B  125  LYS B  129  5                                   5    
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  LYS C  129  5                                   5    
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  LYS D  129  5                                   5    
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  ILE A  51  1  N  TRP A  50   O  HIS A 114           
SHEET    4   B 5 CYS A  90  ILE A  93 -1  O  VAL A  91   N  ILE A  51           
SHEET    5   B 5 TRP A 104  GLU A 107 -1  O  ASN A 105   N  GLU A  92           
SHEET    1   C 2 ILE A  53  ASN A  56  0                                        
SHEET    2   C 2 THR A  59  TRP A  62 -1  N  THR A  59   O  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  N  TYR A 155   O  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  10  0                                        
SHEET    2   K 3 LYS C 113  THR C 119 -1  O  LYS C 113   N  TYR C  10           
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  10  0                                        
SHEET    2   L 5 LYS C 113  THR C 119 -1  O  LYS C 113   N  TYR C  10           
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 ILE C  53  ARG C  54  0                                        
SHEET    2   M 3 THR C  61  TRP C  62 -1  N  THR C  61   O  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 GLY C 131  THR C 136  0                                        
SHEET    2   N 2 ASN C 139  CYS C 144 -1  O  ASN C 139   N  THR C 136           
SHEET    1   O 2 PHE C 148  TYR C 149  0                                        
SHEET    2   O 2 TYR C 155  VAL C 156 -1  O  TYR C 155   N  TYR C 149           
SHEET    1   P 3 THR D   2  TYR D   5  0                                        
SHEET    2   P 3 HIS D 114  THR D 119 -1  N  CYS D 117   O  HIS D   4           
SHEET    3   P 3 ASP D  25  LEU D  26 -1  O  ASP D  25   N  TYR D 118           
SHEET    1   Q 5 THR D   2  TYR D   5  0                                        
SHEET    2   Q 5 HIS D 114  THR D 119 -1  N  CYS D 117   O  HIS D   4           
SHEET    3   Q 5 TYR D  49  TRP D  50  1  N  TRP D  50   O  HIS D 114           
SHEET    4   Q 5 CYS D  90  ILE D  93 -1  N  ILE D  93   O  TYR D  49           
SHEET    5   Q 5 TRP D 104  GLU D 107 -1  O  ASN D 105   N  GLU D  92           
SHEET    1   R 2 ILE D  53  LYS D  55  0                                        
SHEET    2   R 2 TRP D  60  TRP D  62 -1  N  THR D  61   O  ARG D  54           
SHEET    1   S 2 GLY D 131  THR D 136  0                                        
SHEET    2   S 2 ASN D 139  CYS D 144 -1  O  ASN D 139   N  THR D 136           
SHEET    1   T 2 PHE D 148  TYR D 149  0                                        
SHEET    2   T 2 TYR D 155  VAL D 156 -1  N  TYR D 155   O  TYR D 149           
SSBOND   1 CYS A   19    CYS A  117                          1555   1555  2.04  
SSBOND   2 CYS A   90    CYS A  109                          1555   1555  2.02  
SSBOND   3 CYS A  122    CYS A  133                          1555   1555  2.03  
SSBOND   4 CYS A  127    CYS A  142                          1555   1555  2.04  
SSBOND   5 CYS A  144    CYS A  153                          1555   1555  2.05  
SSBOND   6 CYS B   19    CYS B  117                          1555   1555  2.06  
SSBOND   7 CYS B   90    CYS B  109                          1555   1555  2.03  
SSBOND   8 CYS B  122    CYS B  133                          1555   1555  2.03  
SSBOND   9 CYS B  127    CYS B  142                          1555   1555  2.04  
SSBOND  10 CYS B  144    CYS B  153                          1555   1555  2.04  
SSBOND  11 CYS C   19    CYS C  117                          1555   1555  2.03  
SSBOND  12 CYS C   90    CYS C  109                          1555   1555  2.04  
SSBOND  13 CYS C  122    CYS C  133                          1555   1555  2.03  
SSBOND  14 CYS C  127    CYS C  142                          1555   1555  2.04  
SSBOND  15 CYS C  144    CYS C  153                          1555   1555  2.04  
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  2.04  
SSBOND  19 CYS D  127    CYS D  142                          1555   1555  2.03  
SSBOND  20 CYS D  144    CYS D  153                          1555   1555  2.05  
LINK        CA    CA A 801                 OE1 GLU A  80     1555   1555  2.60  
LINK        CA    CA A 801                 OD1 ASN A 105     1555   1555  2.32  
LINK        CA    CA A 801                 O   HOH A 810     1555   1555  2.28  
LINK        CA    CA A 801                 OD1 ASN A  82     1555   1555  2.39  
LINK        CA    CA A 801                 O   ASP A 106     1555   1555  2.46  
LINK        CA    CA A 801                 OD1 ASP A 106     1555   1555  2.16  
LINK        CA    CA A 801                 O   HOH A 857     1555   1555  2.32  
LINK        CA    CA B 802                 OD1 ASN B  82     1555   1555  2.34  
LINK        CA    CA B 802                 O   HOH B 833     1555   1555  2.36  
LINK        CA    CA B 802                 O   ASP B 106     1555   1555  2.50  
LINK        CA    CA B 802                 OD1 ASP B 106     1555   1555  2.33  
LINK        CA    CA B 802                 O   HOH B 826     1555   1555  2.49  
LINK        CA    CA B 802                 OE1 GLU B  80     1555   1555  2.68  
LINK        CA    CA B 802                 OD1 ASN B 105     1555   1555  2.29  
LINK        CA    CA C 803                 OD1 ASN C 105     1555   1555  2.62  
LINK        CA    CA C 803                 O   ASP C 106     1555   1555  2.52  
LINK        CA    CA C 803                 OD1 ASN C  82     1555   1555  2.55  
LINK        CA    CA C 803                 OD1 ASP C 106     1555   1555  2.26  
LINK        CA    CA C 803                 OE1 GLU C  80     1555   1555  2.37  
LINK        CA    CA D 804                 OD1 ASP D 106     1555   1555  2.31  
LINK        CA    CA D 804                 OE2 GLU D  80     1555   1555  2.72  
LINK        CA    CA D 804                 OD1 ASN D  82     1555   1555  2.14  
LINK        CA    CA D 804                 OD1 ASN D 105     1555   1555  2.08  
LINK        CA    CA D 804                 O   ASP D 106     1555   1555  2.59  
CISPEP   1 GLU A   80    PRO A   81          0        -0.54                     
CISPEP   2 GLU B   80    PRO B   81          0        -0.17                     
CISPEP   3 GLU C   80    PRO C   81          0        -0.52                     
CISPEP   4 GLU D   80    PRO D   81          0        -0.12                     
SITE     1 AC1  6 GLU A  80  ASN A  82  ASN A 105  ASP A 106                    
SITE     2 AC1  6 HOH A 810  HOH A 857                                          
SITE     1 AC2  6 GLU B  80  ASN B  82  ASN B 105  ASP B 106                    
SITE     2 AC2  6 HOH B 826  HOH B 833                                          
SITE     1 AC3  4 GLU C  80  ASN C  82  ASN C 105  ASP C 106                    
SITE     1 AC4  4 GLU D  80  ASN D  82  ASN D 105  ASP D 106                    
SITE     1 AC5  5 THR C   2  TYR C   3  TYR C  37  GLY C 138                    
SITE     2 AC5  5 HOH C 814                                                     
SITE     1 AC6  5 THR A   2  TYR A   3  TYR A  37  ILE A 137                    
SITE     2 AC6  5 GLY A 138                                                     
CRYST1   81.000   60.830   91.440  90.00 103.58  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      0.012346  0.000000  0.002982        0.00000                         
SCALE2      0.000000  0.016439  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011251        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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