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Database: PDB
Entry: 1YJD
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HEADER    IMMUNE SYSTEM/SIGNALING PROTEIN         14-JAN-05   1YJD              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD28 IN COMPLEX WITH THE FAB FRAGMENT OF A 
TITLE    2 MITOGENIC ANTIBODY (5.11A1)                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAB FRAGMENT OF 5.11A1 ANTIBODY LIGHT CHAIN;               
COMPND   3 CHAIN: L;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: FAB FRAGMENT OF 5.11A1 ANTIBODY HEAVY CHAIN;               
COMPND   6 CHAIN: H;                                                            
COMPND   7 FRAGMENT: IGV AND IGC1 DOMAINS;                                      
COMPND   8 MOL_ID: 3;                                                           
COMPND   9 MOLECULE: T-CELL-SPECIFIC SURFACE GLYCOPROTEIN CD28;                 
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: EXTRACELLULAR REGION;                                      
COMPND  12 SYNONYM: TP44;                                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   7 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   8 ORGANISM_TAXID: 10090;                                               
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CD28;                                                          
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: CHO LEC3.2.8.1;                            
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PEE14                                     
KEYWDS    IGSF, CD28 HOMODIMER, IMMUNE SYSTEM-SIGNALING PROTEIN COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.J.EVANS,R.M.ESNOUF,R.MANSO-SANCHO,R.J.C.GILBERT,J.R.JAMES,          
AUTHOR   2 P.SORENSEN,D.I.STUART,S.J.DAVIS                                      
REVDAT   4   13-JUL-11 1YJD    1       VERSN                                    
REVDAT   3   24-FEB-09 1YJD    1       VERSN                                    
REVDAT   2   08-MAR-05 1YJD    1       JRNL                                     
REVDAT   1   15-FEB-05 1YJD    0                                                
JRNL        AUTH   E.J.EVANS,R.M.ESNOUF,R.MANSO-SANCHO,R.J.C.GILBERT,J.R.JAMES, 
JRNL        AUTH 2 C.YU,J.A.FENNELLY,C.VOWLES,T.HANKE,B.WALSE,T.HUNIG,          
JRNL        AUTH 3 P.SORENSEN,D.I.STUART,S.J.DAVIS                              
JRNL        TITL   CRYSTAL STRUCTURE OF A SOLUBLE CD28-FAB COMPLEX              
JRNL        REF    NAT.IMMUNOL.                  V.   6   271 2005              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   15696168                                                     
JRNL        DOI    10.1038/NI1170                                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 17402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 842                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.78                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE                    : 0.4140                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72                           
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            : 4248                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 203                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 18.53800                                             
REMARK   3    B22 (A**2) : -3.91000                                             
REMARK   3    B33 (A**2) : -14.62900                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -4.28000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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) : NULL                            
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 1YJD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031578.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID13                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.008                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17413                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM FORMATE, PH 5.9,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       95.60950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.70850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       95.60950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.70850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY   
REMARK 300 THE TWO FOLD AXIS: 1-X, Y, 1-Z.                                      
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      185.64484            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       71.62543            
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     GLN H     1                                                      
REMARK 465     PRO H   219                                                      
REMARK 465     ARG H   220                                                      
REMARK 465     ASP H   221                                                      
REMARK 465     CYS H   222                                                      
REMARK 465     THR C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     LYS C   120                                                      
REMARK 465     HIS C   121                                                      
REMARK 465     LEU C   122                                                      
REMARK 465     CYS C   123                                                      
REMARK 465     PRO C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     PRO C   126                                                      
REMARK 465     LEU C   127                                                      
REMARK 465     PHE C   128                                                      
REMARK 465     PRO C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     PRO C   131                                                      
REMARK 465     SER C   132                                                      
REMARK 465     LYS C   133                                                      
REMARK 465     PRO C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     VAL C   136                                                      
REMARK 465     PRO C   137                                                      
REMARK 465     ARG C   138                                                      
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 L  23   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    CYS L  88   CA  -  CB  -  SG  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    LEU H 184   CA  -  CB  -  CG  ANGL. DEV. =  15.3 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    SER L   7      -91.19    -83.65                                   
REMARK 500    LEU L  11      132.39   -173.57                                   
REMARK 500    THR L  18       78.54   -102.70                                   
REMARK 500    TYR L  30     -112.23     62.90                                   
REMARK 500    ALA L  51      -68.87     65.16                                   
REMARK 500    SER L  77       73.70     50.09                                   
REMARK 500    ALA L  84     -173.70    178.38                                   
REMARK 500    ALA L 130      111.76   -165.38                                   
REMARK 500    ASN L 138       75.92     41.48                                   
REMARK 500    PRO L 141     -178.67    -68.99                                   
REMARK 500    ASP L 151     -102.07     76.63                                   
REMARK 500    ARG L 211       24.08    -75.80                                   
REMARK 500    PRO H  14      106.74    -42.97                                   
REMARK 500    CYS H  22      104.32   -167.95                                   
REMARK 500    SER H  25      117.78   -173.87                                   
REMARK 500    PHE H  64       27.58   -141.33                                   
REMARK 500    ARG H  85       84.97     56.40                                   
REMARK 500    SER H  88       -4.59    -58.01                                   
REMARK 500    VAL H 118       51.75   -117.53                                   
REMARK 500    ALA H 136     -162.85   -116.08                                   
REMARK 500    ALA H 137       99.02   -161.09                                   
REMARK 500    THR H 139       82.69   -169.63                                   
REMARK 500    ASN H 162       57.71     70.46                                   
REMARK 500    ASP H 180       -9.92     83.36                                   
REMARK 500    SER C  25       67.51   -110.53                                   
REMARK 500    ASN C  27      152.23     33.36                                   
REMARK 500    PHE C  29      163.25    161.13                                   
REMARK 500    SER C  30       89.79     79.98                                   
REMARK 500    SER C  43       31.20     35.00                                   
REMARK 500    ALA C  44      -90.30    -48.74                                   
REMARK 500    ASN C  53       75.45   -155.03                                   
REMARK 500    TYR C  54      -85.15     62.62                                   
REMARK 500    SER C  55      -96.25   -100.39                                   
REMARK 500    GLN C  56       99.73      9.77                                   
REMARK 500    GLN C  57      139.64    -19.60                                   
REMARK 500    ASN C  74     -102.26     56.59                                   
REMARK 500    TYR C 100      136.48    174.61                                   
REMARK 500    LYS C 109      114.23    -29.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN C  27        23.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 203                 
DBREF  1YJD C   -1   134  UNP    P10747   CD28_HUMAN      17    152             
DBREF  1YJD L    1   212  PDB    1YJD     1YJD             1    212             
DBREF  1YJD H    1   222  PDB    1YJD     1YJD             1    222             
SEQADV 1YJD LEU C  135  UNP  P10747              CLONING ARTIFACT               
SEQADV 1YJD VAL C  136  UNP  P10747              CLONING ARTIFACT               
SEQADV 1YJD PRO C  137  UNP  P10747              CLONING ARTIFACT               
SEQADV 1YJD ARG C  138  UNP  P10747              CLONING ARTIFACT               
SEQRES   1 L  212  ASP ILE GLN MET ASN GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  212  SER LEU GLY ASP THR ILE THR ILE THR CYS HIS ALA SER          
SEQRES   3 L  212  GLN ASN ILE TYR VAL TRP LEU ASN TRP TYR GLN GLN LYS          
SEQRES   4 L  212  PRO GLY ASN ILE PRO LYS LEU LEU ILE TYR LYS ALA SER          
SEQRES   5 L  212  ASN LEU HIS THR GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  212  GLY SER GLY THR GLY PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  212  GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN GLY          
SEQRES   8 L  212  GLN THR TYR PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  212  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  212  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  212  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  212  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  212  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  212  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  212  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  212  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  212  PHE ASN ARG ASN                                              
SEQRES   1 H  222  GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS          
SEQRES   2 H  222  PRO GLY THR SER VAL ARG ILE SER CYS GLU ALA SER GLY          
SEQRES   3 H  222  TYR THR PHE THR SER TYR TYR ILE HIS TRP VAL LYS GLN          
SEQRES   4 H  222  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY CYS ILE TYR          
SEQRES   5 H  222  PRO GLY ASN VAL ASN THR ASN TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  222  ASP LYS ALA THR LEU ILE VAL ASP THR SER SER ASN THR          
SEQRES   7 H  222  ALA TYR MET GLN LEU SER ARG MET THR SER GLU ASP SER          
SEQRES   8 H  222  ALA VAL TYR PHE CYS THR ARG SER HIS TYR GLY LEU ASP          
SEQRES   9 H  222  TRP ASN PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR          
SEQRES  10 H  222  VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO          
SEQRES  11 H  222  LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL          
SEQRES  12 H  222  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO          
SEQRES  13 H  222  VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY          
SEQRES  14 H  222  VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR          
SEQRES  15 H  222  THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP          
SEQRES  16 H  222  PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA          
SEQRES  17 H  222  SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP          
SEQRES  18 H  222  CYS                                                          
SEQRES   1 C  140  THR GLY ASN LYS ILE LEU VAL LYS GLN SER PRO MET LEU          
SEQRES   2 C  140  VAL ALA TYR ASP ASN ALA VAL ASN LEU SER CYS LYS TYR          
SEQRES   3 C  140  SER TYR ASN LEU PHE SER ARG GLU PHE ARG ALA SER LEU          
SEQRES   4 C  140  HIS LYS GLY LEU ASP SER ALA VAL GLU VAL CYS VAL VAL          
SEQRES   5 C  140  TYR GLY ASN TYR SER GLN GLN LEU GLN VAL TYR SER LYS          
SEQRES   6 C  140  THR GLY PHE ASN CYS ASP GLY LYS LEU GLY ASN GLU SER          
SEQRES   7 C  140  VAL THR PHE TYR LEU GLN ASN LEU TYR VAL ASN GLN THR          
SEQRES   8 C  140  ASP ILE TYR PHE CYS LYS ILE GLU VAL MET TYR PRO PRO          
SEQRES   9 C  140  PRO TYR LEU ASP ASN GLU LYS SER ASN GLY THR ILE ILE          
SEQRES  10 C  140  HIS VAL LYS GLY LYS HIS LEU CYS PRO SER PRO LEU PHE          
SEQRES  11 C  140  PRO GLY PRO SER LYS PRO LEU VAL PRO ARG                      
MODRES 1YJD ASN C   19  ASN  GLYCOSYLATION SITE                                 
MODRES 1YJD ASN C   53  ASN  GLYCOSYLATION SITE                                 
MODRES 1YJD ASN C   87  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C 201      14                                                       
HET    NAG  C 202      14                                                       
HET    NAG  C 203      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    3(C8 H15 N O6)                                               
FORMUL   7  HOH   *203(H2 O)                                                    
HELIX    1   1 GLN L   79  ILE L   83  5                                   5    
HELIX    2   2 SER L  121  THR L  126  1                                   6    
HELIX    3   3 LYS L  183  GLU L  187  1                                   5    
HELIX    4   4 THR H   28  THR H   30  5                                   3    
HELIX    5   5 GLU H   62  LYS H   65  5                                   4    
HELIX    6   6 PRO H  207  SER H  210  5                                   4    
HELIX    7   7 TYR C   85  THR C   89  5                                   5    
SHEET    1   A 4 MET L   4  GLN L   6  0                                        
SHEET    2   A 4 ILE L  19  ALA L  25 -1  O  HIS L  24   N  ASN L   5           
SHEET    3   A 4 GLY L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4   A 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1   B 6 SER L  10  SER L  14  0                                        
SHEET    2   B 6 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   B 6 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   B 6 LEU L  33  GLN L  38 -1  N  ASN L  34   O  GLN L  89           
SHEET    5   B 6 LYS L  45  TYR L  49 -1  O  LYS L  45   N  GLN L  37           
SHEET    6   B 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1   C 4 SER L  10  SER L  14  0                                        
SHEET    2   C 4 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   C 4 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   C 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   D 4 THR L 114  PHE L 118  0                                        
SHEET    2   D 4 GLY L 129  PHE L 139 -1  O  PHE L 135   N  SER L 116           
SHEET    3   D 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4   D 4 VAL L 159  TRP L 163 -1  N  LEU L 160   O  THR L 178           
SHEET    1   E 4 SER L 153  ARG L 155  0                                        
SHEET    2   E 4 ASN L 145  ILE L 150 -1  N  TRP L 148   O  ARG L 155           
SHEET    3   E 4 TYR L 192  THR L 197 -1  O  GLU L 195   N  LYS L 147           
SHEET    4   E 4 ILE L 205  PHE L 209 -1  O  LYS L 207   N  CYS L 194           
SHEET    1   F 2 GLN H   3  GLN H   6  0                                        
SHEET    2   F 2 CYS H  22  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    1   G 6 GLU H  10  LEU H  11  0                                        
SHEET    2   G 6 THR H 114  THR H 117  1  O  THR H 117   N  GLU H  10           
SHEET    3   G 6 ALA H  92  HIS H 100 -1  N  TYR H  94   O  THR H 114           
SHEET    4   G 6 TYR H  32  GLN H  39 -1  N  VAL H  37   O  PHE H  95           
SHEET    5   G 6 LEU H  45  TYR H  52 -1  O  GLY H  49   N  TRP H  36           
SHEET    6   G 6 ASN H  57  TYR H  60 -1  O  ASN H  59   N  CYS H  50           
SHEET    1   H 3 VAL H  18  ILE H  20  0                                        
SHEET    2   H 3 THR H  78  LEU H  83 -1  O  LEU H  83   N  VAL H  18           
SHEET    3   H 3 ALA H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1   I 4 SER H 127  LEU H 131  0                                        
SHEET    2   I 4 MET H 142  TYR H 152 -1  O  LEU H 148   N  TYR H 129           
SHEET    3   I 4 LEU H 181  PRO H 191 -1  O  LEU H 184   N  VAL H 149           
SHEET    4   I 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  SER H 187           
SHEET    1   J 4 SER H 127  LEU H 131  0                                        
SHEET    2   J 4 MET H 142  TYR H 152 -1  O  LEU H 148   N  TYR H 129           
SHEET    3   J 4 LEU H 181  PRO H 191 -1  O  LEU H 184   N  VAL H 149           
SHEET    4   J 4 VAL H 176  GLN H 178 -1  N  GLN H 178   O  LEU H 181           
SHEET    1   K 3 THR H 158  TRP H 161  0                                        
SHEET    2   K 3 VAL H 200  HIS H 206 -1  O  ASN H 203   N  THR H 160           
SHEET    3   K 3 THR H 211  ILE H 217 -1  O  VAL H 213   N  VAL H 204           
SHEET    1   L 4 VAL C   5  LYS C   6  0                                        
SHEET    2   L 4 VAL C  18  TYR C  24 -1  O  LYS C  23   N  LYS C   6           
SHEET    3   L 4 SER C  76  GLN C  82 -1  O  PHE C  79   N  LEU C  20           
SHEET    4   L 4 ASN C  67  LEU C  72 -1  N  ASP C  69   O  TYR C  80           
SHEET    1   M 6 MET C  10  VAL C  12  0                                        
SHEET    2   M 6 THR C 113  HIS C 116  1  O  HIS C 116   N  LEU C  11           
SHEET    3   M 6 ASP C  90  TYR C 100 -1  N  ASP C  90   O  ILE C 115           
SHEET    4   M 6 GLU C  32  LYS C  39 -1  N  GLU C  32   O  TYR C 100           
SHEET    5   M 6 GLU C  46  ASN C  53 -1  O  GLY C  52   N  PHE C  33           
SHEET    6   M 6 GLN C  59  TYR C  61 -1  O  GLN C  59   N  TYR C  51           
SHEET    1   N 4 MET C  10  VAL C  12  0                                        
SHEET    2   N 4 THR C 113  HIS C 116  1  O  HIS C 116   N  LEU C  11           
SHEET    3   N 4 ASP C  90  TYR C 100 -1  N  ASP C  90   O  ILE C 115           
SHEET    4   N 4 LEU C 105  ASP C 106 -1  O  LEU C 105   N  VAL C  98           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND   2 CYS L  134    CYS L  194                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND   4 CYS H  147    CYS H  202                          1555   1555  2.04  
SSBOND   5 CYS C   22    CYS C   94                          1555   1555  2.02  
SSBOND   6 CYS C   48    CYS C   68                          1555   1555  2.03  
LINK         ND2 ASN C  19                 C1  NAG C 201     1555   1555  1.45  
LINK         ND2 ASN C  53                 C1  NAG C 202     1555   1555  1.45  
LINK         ND2 ASN C  87                 C1  NAG C 203     1555   1555  1.45  
CISPEP   1 TYR L   94    PRO L   95          0         0.19                     
CISPEP   2 TYR L  140    PRO L  141          0        -0.99                     
CISPEP   3 PHE H  153    PRO H  154          0         0.01                     
CISPEP   4 GLU H  155    PRO H  156          0         0.60                     
CISPEP   5 TRP H  195    PRO H  196          0         0.40                     
CISPEP   6 TYR C  100    PRO C  101          0         0.17                     
CISPEP   7 PRO C  102    PRO C  103          0        -0.25                     
SITE     1 AC1  5 VAL C  18  ASN C  19  HOH C 229  ASN L 190                    
SITE     2 AC1  5 HOH L 254                                                     
SITE     1 AC2  5 TYR C  51  ASN C  53  GLN C  56  HOH C 207                    
SITE     2 AC2  5 HIS H 100                                                     
SITE     1 AC3  3 TYR C  85  ASN C  87  HOH C 230                               
CRYST1  191.219   47.417   71.842  90.00  94.45  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005230  0.000000  0.000407        0.00000                         
SCALE2      0.000000  0.021089  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013962        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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