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Database: PDB
Entry: 1I85
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Original site: 1I85 
HEADER    IMMUNE SYSTEM                           12-MAR-01   1I85              
TITLE     CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: T LYMPHOCYTE ACTIVATION ANTIGEN CD86;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: IG V-TYPE (RECEPTOR BINDING) DOMAIN;                       
COMPND   5 SYNONYM: B7-2;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED PROTEIN 4;               
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  11 SYNONYM: CTLA-4;                                                     
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD86;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CTLA4;                                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    IG V-TYPE DOMAIN, IMMUNE SYSTEM                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-C.D.SCHWARTZ,X.ZHANG,A.A.FEDOROV,S.G.NATHENSON,S.C.ALMO            
REVDAT   3   24-FEB-09 1I85    1       VERSN                                    
REVDAT   2   01-APR-03 1I85    1       JRNL                                     
REVDAT   1   04-APR-01 1I85    0                                                
JRNL        AUTH   J.C.SCHWARTZ,X.ZHANG,A.A.FEDOROV,S.G.NATHENSON,              
JRNL        AUTH 2 S.C.ALMO                                                     
JRNL        TITL   STRUCTURAL BASIS FOR CO-STIMULATION BY THE HUMAN             
JRNL        TITL 2 CTLA-4/B7-2 COMPLEX.                                         
JRNL        REF    NATURE                        V. 410   604 2001              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   11279501                                                     
JRNL        DOI    10.1038/35069112                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.200                          
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             : 6516                           
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 606                             
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 56.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 415                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3720                       
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 61                           
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            : 3515                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.40                          
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.69                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.97                            
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I85 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013024.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7080                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
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     (%) : 78.8                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG20K, HEPES, PH 7.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       27.28000            
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 300 REMARK: THE CTLA-4 HOMODIMER IS GENERATED BY CHAIN D AND THE         
REMARK 300 TRANSLATONAL SYMMETRY MATE OF CHAIN C (APPLY THE OPERATOR X,Y,Z+     
REMARK 300 1 TO CHAIN C)                                                        
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     MET B     0                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     PRO C   121                                                      
REMARK 465     CYS C   122                                                      
REMARK 465     PRO C   123                                                      
REMARK 465     ASP C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     ASP C   126                                                      
REMARK 465     LYS D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     SER D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     LYS D    30                                                      
REMARK 465     ALA D    42                                                      
REMARK 465     ASP D    43                                                      
REMARK 465     SER D    44                                                      
REMARK 465     PRO D   121                                                      
REMARK 465     CYS D   122                                                      
REMARK 465     PRO D   123                                                      
REMARK 465     ASP D   124                                                      
REMARK 465     SER D   125                                                      
REMARK 465     ASP D   126                                                      
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     THR C 112    OG1  CG2                                            
REMARK 470     THR D 112    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL D   116     N    ASP D   118              2.19            
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    LEU A   1       91.52    167.41                                   
REMARK 500    GLU A   9     -160.08   -101.47                                   
REMARK 500    GLN A  16       -3.64     60.64                                   
REMARK 500    ASN A  19      122.36    -24.86                                   
REMARK 500    GLN A  21       42.86    -84.58                                   
REMARK 500    ASN A  22       99.15      9.34                                   
REMARK 500    LEU A  25       -0.89    -50.71                                   
REMARK 500    GLU A  27       32.46    -95.61                                   
REMARK 500    LEU A  40      -82.95    -86.73                                   
REMARK 500    LEU A  45       31.97     25.96                                   
REMARK 500    ARG A  60       46.55   -166.38                                   
REMARK 500    SER A  62      113.31   -164.91                                   
REMARK 500    SER A  65      -11.11    -48.06                                   
REMARK 500    TRP A  68       -8.68     60.08                                   
REMARK 500    THR A  69     -175.56    -62.40                                   
REMARK 500    LYS A  80       94.56    -49.38                                   
REMARK 500    LYS A  90       94.65    -59.56                                   
REMARK 500    GLN B  16      -10.30     66.35                                   
REMARK 500    PHE B  17      160.20    -49.64                                   
REMARK 500    ALA B  18       65.52   -153.24                                   
REMARK 500    ASN B  19      116.87    -17.29                                   
REMARK 500    SER B  20      -61.34   -103.66                                   
REMARK 500    GLN B  21       42.43    -80.79                                   
REMARK 500    ASN B  22      100.62     12.54                                   
REMARK 500    LEU B  25        3.22    -62.34                                   
REMARK 500    ASP B  34     -160.14   -102.79                                   
REMARK 500    LEU B  40      -81.66    -90.03                                   
REMARK 500    LEU B  45       33.61     25.64                                   
REMARK 500    ASP B  51      -37.55    -38.88                                   
REMARK 500    ARG B  60       43.37   -153.89                                   
REMARK 500    SER B  62      140.49   -172.40                                   
REMARK 500    TRP B  68       11.65     51.47                                   
REMARK 500    LEU B  70      103.32   -166.02                                   
REMARK 500    ASN B  74       74.27     34.34                                   
REMARK 500    LYS B  80       95.74    -55.88                                   
REMARK 500    LYS B  90       85.40    -58.96                                   
REMARK 500    GLN B 100      114.91   -162.03                                   
REMARK 500    LYS C  30      139.75    173.96                                   
REMARK 500    ALA C  31      131.41    -34.37                                   
REMARK 500    ARG C  40      124.44   -177.68                                   
REMARK 500    ALA C  42     -103.55    -91.02                                   
REMARK 500    SER C  44      -12.59   -175.61                                   
REMARK 500    MET C  55     -171.11    -63.54                                   
REMARK 500    ASP C  64      -37.11    -35.34                                   
REMARK 500    SER C  66     -144.76    -56.50                                   
REMARK 500    SER C  73       84.69   -174.39                                   
REMARK 500    ASN C  75      -23.84     60.61                                   
REMARK 500    THR C  89      113.93    -22.83                                   
REMARK 500    MET C  99     -153.75    -67.65                                   
REMARK 500    TYR C 104     -168.75    -67.33                                   
REMARK 500    TYR C 105      105.73    171.30                                   
REMARK 500    ILE C 117       70.03    -36.96                                   
REMARK 500    ASP C 118       81.91    179.81                                   
REMARK 500    HIS D   4      107.61   -172.00                                   
REMARK 500    THR D  32      -34.31   -150.70                                   
REMARK 500    ARG D  40      118.87   -169.35                                   
REMARK 500    MET D  55     -163.55    -68.55                                   
REMARK 500    THR D  61      -68.17   -121.81                                   
REMARK 500    PHE D  62       76.95     58.11                                   
REMARK 500    LEU D  63     -105.85     41.40                                   
REMARK 500    ASP D  64      -20.47   -176.28                                   
REMARK 500    SER D  73       78.73   -167.26                                   
REMARK 500    ASN D  75      -48.03     62.16                                   
REMARK 500    THR D  89      130.26    -30.84                                   
REMARK 500    MET D  99     -158.45    -64.05                                   
REMARK 500    TYR D 104     -176.47    -67.25                                   
REMARK 500    TYR D 105      123.50    177.74                                   
REMARK 500    ILE D 117       76.03    -41.82                                   
REMARK 500    ASP D 118       86.26    171.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1I85 A    1   109  UNP    P42081   CD86_HUMAN      26    134             
DBREF  1I85 B    1   109  UNP    P42081   CD86_HUMAN      26    134             
DBREF  1I85 C    1   126  UNP    P16410   CTLA4_HUMAN     36    161             
DBREF  1I85 D    1   126  UNP    P16410   CTLA4_HUMAN     36    161             
SEQADV 1I85 MET A    0  UNP  P42081              INITIATING METHIONINE          
SEQADV 1I85 MET B    0  UNP  P42081              INITIATING METHIONINE          
SEQADV 1I85 MET C   56  UNP  P16410    THR    91 SEE REMARK 999                 
SEQADV 1I85 MET D   56  UNP  P16410    THR    91 SEE REMARK 999                 
SEQRES   1 A  110  MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA ASP          
SEQRES   2 A  110  LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER LEU          
SEQRES   3 A  110  SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN LEU          
SEQRES   4 A  110  VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE ASP          
SEQRES   5 A  110  SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE ASP          
SEQRES   6 A  110  SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN ILE          
SEQRES   7 A  110  LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS LYS          
SEQRES   8 A  110  LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN SER          
SEQRES   9 A  110  GLU LEU SER VAL LEU ALA                                      
SEQRES   1 B  110  MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA ASP          
SEQRES   2 B  110  LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER LEU          
SEQRES   3 B  110  SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN LEU          
SEQRES   4 B  110  VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE ASP          
SEQRES   5 B  110  SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE ASP          
SEQRES   6 B  110  SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN ILE          
SEQRES   7 B  110  LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS LYS          
SEQRES   8 B  110  LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN SER          
SEQRES   9 B  110  GLU LEU SER VAL LEU ALA                                      
SEQRES   1 C  126  LYS ALA MET HIS VAL ALA GLN PRO ALA VAL VAL LEU ALA          
SEQRES   2 C  126  SER SER ARG GLY ILE ALA SER PHE VAL CYS GLU TYR ALA          
SEQRES   3 C  126  SER PRO GLY LYS ALA THR GLU VAL ARG VAL THR VAL LEU          
SEQRES   4 C  126  ARG GLN ALA ASP SER GLN VAL THR GLU VAL CYS ALA ALA          
SEQRES   5 C  126  THR TYR MET MET GLY ASN GLU LEU THR PHE LEU ASP ASP          
SEQRES   6 C  126  SER ILE CYS THR GLY THR SER SER GLY ASN GLN VAL ASN          
SEQRES   7 C  126  LEU THR ILE GLN GLY LEU ARG ALA MET ASP THR GLY LEU          
SEQRES   8 C  126  TYR ILE CYS LYS VAL GLU LEU MET TYR PRO PRO PRO TYR          
SEQRES   9 C  126  TYR LEU GLY ILE GLY ASN GLY THR GLN ILE TYR VAL ILE          
SEQRES  10 C  126  ASP PRO GLU PRO CYS PRO ASP SER ASP                          
SEQRES   1 D  126  LYS ALA MET HIS VAL ALA GLN PRO ALA VAL VAL LEU ALA          
SEQRES   2 D  126  SER SER ARG GLY ILE ALA SER PHE VAL CYS GLU TYR ALA          
SEQRES   3 D  126  SER PRO GLY LYS ALA THR GLU VAL ARG VAL THR VAL LEU          
SEQRES   4 D  126  ARG GLN ALA ASP SER GLN VAL THR GLU VAL CYS ALA ALA          
SEQRES   5 D  126  THR TYR MET MET GLY ASN GLU LEU THR PHE LEU ASP ASP          
SEQRES   6 D  126  SER ILE CYS THR GLY THR SER SER GLY ASN GLN VAL ASN          
SEQRES   7 D  126  LEU THR ILE GLN GLY LEU ARG ALA MET ASP THR GLY LEU          
SEQRES   8 D  126  TYR ILE CYS LYS VAL GLU LEU MET TYR PRO PRO PRO TYR          
SEQRES   9 D  126  TYR LEU GLY ILE GLY ASN GLY THR GLN ILE TYR VAL ILE          
SEQRES  10 D  126  ASP PRO GLU PRO CYS PRO ASP SER ASP                          
SHEET    1   A 5 LYS A   2  TYR A   6  0                                        
SHEET    2   A 5 ARG A  97  LEU A 108  1  O  GLU A 104   N  ILE A   3           
SHEET    3   A 5 LEU A  82  HIS A  88 -1  N  TYR A  83   O  SER A 103           
SHEET    4   A 5 VAL A  29  GLN A  33 -1  O  VAL A  29   N  HIS A  88           
SHEET    5   A 5 VAL A  39  VAL A  43 -1  N  LEU A  40   O  TRP A  32           
SHEET    1   B 3 ALA A  11  LEU A  13  0                                        
SHEET    2   B 3 LEU A  70  LEU A  72 -1  O  LEU A  70   N  LEU A  13           
SHEET    3   B 3 THR A  61  PHE A  63 -1  O  SER A  62   N  ARG A  71           
SHEET    1   C 6 LYS B   2  TYR B   6  0                                        
SHEET    2   C 6 ARG B  97  LEU B 108  1  O  GLU B 104   N  ILE B   3           
SHEET    3   C 6 LEU B  82  HIS B  88 -1  N  TYR B  83   O  SER B 103           
SHEET    4   C 6 VAL B  29  GLN B  33 -1  O  VAL B  29   N  HIS B  88           
SHEET    5   C 6 VAL B  39  TYR B  44 -1  N  LEU B  40   O  TRP B  32           
SHEET    6   C 6 LYS B  47  GLU B  48 -1  N  LYS B  47   O  TYR B  44           
SHEET    1   D 3 ALA B  11  ASP B  12  0                                        
SHEET    2   D 3 LEU B  70  LEU B  72 -1  N  LEU B  72   O  ALA B  11           
SHEET    3   D 3 THR B  61  PHE B  63 -1  N  SER B  62   O  ARG B  71           
SHEET    1   E 4 VAL C   5  ALA C   6  0                                        
SHEET    2   E 4 VAL C  22  TYR C  25 -1  N  GLU C  24   O  ALA C   6           
SHEET    3   E 4 GLN C  76  ASN C  78 -1  N  VAL C  77   O  CYS C  23           
SHEET    4   E 4 THR C  71  SER C  72 -1  O  THR C  71   N  ASN C  78           
SHEET    1   F 3 VAL C  10  LEU C  12  0                                        
SHEET    2   F 3 THR C 112  TYR C 115  1  O  GLN C 113   N  VAL C  11           
SHEET    3   F 3 GLY C  90  TYR C  92 -1  O  GLY C  90   N  ILE C 114           
SHEET    1   G 4 CYS C  50  TYR C  54  0                                        
SHEET    2   G 4 VAL C  34  VAL C  38 -1  O  VAL C  34   N  TYR C  54           
SHEET    3   G 4 CYS C  94  LEU C  98 -1  O  LYS C  95   N  THR C  37           
SHEET    4   G 4 LEU C 106  GLY C 107 -1  O  GLY C 107   N  VAL C  96           
SHEET    1   H 4 VAL D   5  ALA D   6  0                                        
SHEET    2   H 4 VAL D  22  TYR D  25 -1  N  GLU D  24   O  ALA D   6           
SHEET    3   H 4 GLN D  76  ASN D  78 -1  O  VAL D  77   N  CYS D  23           
SHEET    4   H 4 THR D  71  SER D  72 -1  O  THR D  71   N  ASN D  78           
SHEET    1   I 3 VAL D  10  LEU D  12  0                                        
SHEET    2   I 3 THR D 112  TYR D 115  1  O  GLN D 113   N  VAL D  11           
SHEET    3   I 3 GLY D  90  TYR D  92 -1  O  GLY D  90   N  ILE D 114           
SHEET    1   J 4 CYS D  50  ALA D  51  0                                        
SHEET    2   J 4 VAL D  34  VAL D  38 -1  N  VAL D  38   O  CYS D  50           
SHEET    3   J 4 CYS D  94  LEU D  98 -1  N  LYS D  95   O  THR D  37           
SHEET    4   J 4 LEU D 106  ILE D 108 -1  O  GLY D 107   N  VAL D  96           
SSBOND   1 CYS A   15    CYS A   85                          1555   1555  2.03  
SSBOND   2 CYS B   15    CYS B   85                          1555   1555  2.03  
SSBOND   3 CYS C   23    CYS C   94                          1555   1555  2.03  
SSBOND   4 CYS C   50    CYS C   68                          1555   1555  2.02  
SSBOND   5 CYS D   23    CYS D   94                          1555   1555  2.02  
SSBOND   6 CYS D   50    CYS D   68                          1555   1555  2.04  
CISPEP   1 TYR C  100    PRO C  101          0        -0.55                     
CISPEP   2 PRO C  102    PRO C  103          0         0.20                     
CISPEP   3 TYR D  100    PRO D  101          0        -0.06                     
CISPEP   4 PRO D  102    PRO D  103          0         0.21                     
CRYST1   47.850   54.560  103.090  90.00  91.63  90.00 P 1 21 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      0.020900  0.000000  0.000590        0.00000                         
SCALE2      0.000000  0.018330  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009700        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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