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Database: PDB
Entry: 5YXK
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Original site: 5YXK 
HEADER    IMMUNE SYSTEM                           05-DEC-17   5YXK              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF HUMAN B7-2 IGV DOMAIN IN P21     
TITLE    2 SPACE GROUP                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: T-LYMPHOCYTE ACTIVATION ANTIGEN CD86;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: IG-LIKE V-TYPE;                                            
COMPND   5 SYNONYM: ACTIVATION B7-2 ANTIGEN,B70,BU63,CTLA-4 COUNTER-RECEPTOR    
COMPND   6 B7.2,FUN-1;                                                          
COMPND   7 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, CD28LG2;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
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: PNIC28-BSA4                               
KEYWDS    B7-2, CO-STIMULATORY MOLECULE, IG SUPER FAMILY, CD86, IMMUNE SYSTEM   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LANKIPALLI,U.A.RAMAGOPAL                                            
REVDAT   1   05-DEC-18 5YXK    0                                                
JRNL        AUTH   S.LANKIPALLI,U.A.RAMAGOPAL                                   
JRNL        TITL   COMPARITIVE STRUCTURAL ANALYSIS OF HUMAN B7-2: NEW INSIGHTS  
JRNL        TITL 2 ON ITS POSSIBLE DIMERIC STATE                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28723                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1473                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.89                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1556                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.3800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3603                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : -2.38000                                             
REMARK   3    B33 (A**2) : 2.48000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.13000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.043         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.037         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.819         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3736 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3364 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5049 ; 1.421 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7862 ; 0.686 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   448 ; 6.388 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   191 ;38.271 ;25.340       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   700 ;15.255 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;25.188 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   546 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4129 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   739 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.843                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.157                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5YXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300006093.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30622                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35100                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 1NCN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HCL PH 8.5, 2.4M AMMONIUM      
REMARK 280  PHOSPHATE DIBASIC, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  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       40.82000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: POSSIBLE DIMER                                               
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     SER A    -1                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     SER D    -1                                                      
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     ASN C  22    CG   OD1  ND2                                       
REMARK 470     LYS C  49    CE   NZ                                             
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    ARG A  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 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    ASN A   8       -3.17     81.74                                   
REMARK 500    GLU A   9     -146.76   -109.73                                   
REMARK 500    ASN A  22       63.71     61.93                                   
REMARK 500    GLU B   9     -162.81   -108.38                                   
REMARK 500    GLN B  16       65.28     39.20                                   
REMARK 500    GLU C   9     -144.27   -114.64                                   
REMARK 500    SER C  20      -35.53    -38.80                                   
REMARK 500    GLU D   9     -146.24   -103.55                                   
REMARK 500    GLN D  16       58.47     39.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5YXK A    1   109  UNP    P42081   CD86_HUMAN      26    134             
DBREF  5YXK B    1   109  UNP    P42081   CD86_HUMAN      26    134             
DBREF  5YXK C    1   109  UNP    P42081   CD86_HUMAN      26    134             
DBREF  5YXK D    1   109  UNP    P42081   CD86_HUMAN      26    134             
SEQADV 5YXK SER A   -1  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK MET A    0  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK SER B   -1  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK MET B    0  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK SER C   -1  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK MET C    0  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK SER D   -1  UNP  P42081              EXPRESSION TAG                 
SEQADV 5YXK MET D    0  UNP  P42081              EXPRESSION TAG                 
SEQRES   1 A  111  SER MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA          
SEQRES   2 A  111  ASP LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER          
SEQRES   3 A  111  LEU SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN          
SEQRES   4 A  111  LEU VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE          
SEQRES   5 A  111  ASP SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE          
SEQRES   6 A  111  ASP SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN          
SEQRES   7 A  111  ILE LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS          
SEQRES   8 A  111  LYS LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN          
SEQRES   9 A  111  SER GLU LEU SER VAL LEU ALA                                  
SEQRES   1 B  111  SER MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA          
SEQRES   2 B  111  ASP LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER          
SEQRES   3 B  111  LEU SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN          
SEQRES   4 B  111  LEU VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE          
SEQRES   5 B  111  ASP SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE          
SEQRES   6 B  111  ASP SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN          
SEQRES   7 B  111  ILE LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS          
SEQRES   8 B  111  LYS LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN          
SEQRES   9 B  111  SER GLU LEU SER VAL LEU ALA                                  
SEQRES   1 C  111  SER MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA          
SEQRES   2 C  111  ASP LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER          
SEQRES   3 C  111  LEU SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN          
SEQRES   4 C  111  LEU VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE          
SEQRES   5 C  111  ASP SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE          
SEQRES   6 C  111  ASP SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN          
SEQRES   7 C  111  ILE LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS          
SEQRES   8 C  111  LYS LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN          
SEQRES   9 C  111  SER GLU LEU SER VAL LEU ALA                                  
SEQRES   1 D  111  SER MET LEU LYS ILE GLN ALA TYR PHE ASN GLU THR ALA          
SEQRES   2 D  111  ASP LEU PRO CYS GLN PHE ALA ASN SER GLN ASN GLN SER          
SEQRES   3 D  111  LEU SER GLU LEU VAL VAL PHE TRP GLN ASP GLN GLU ASN          
SEQRES   4 D  111  LEU VAL LEU ASN GLU VAL TYR LEU GLY LYS GLU LYS PHE          
SEQRES   5 D  111  ASP SER VAL HIS SER LYS TYR MET GLY ARG THR SER PHE          
SEQRES   6 D  111  ASP SER ASP SER TRP THR LEU ARG LEU HIS ASN LEU GLN          
SEQRES   7 D  111  ILE LYS ASP LYS GLY LEU TYR GLN CYS ILE ILE HIS HIS          
SEQRES   8 D  111  LYS LYS PRO THR GLY MET ILE ARG ILE HIS GLN MET ASN          
SEQRES   9 D  111  SER GLU LEU SER VAL LEU ALA                                  
FORMUL   5  HOH   *81(H2 O)                                                     
HELIX    1 AA1 SER A   24  SER A   26  5                                   3    
HELIX    2 AA2 HIS A   54  MET A   58  5                                   5    
HELIX    3 AA3 GLN A   76  LYS A   80  5                                   5    
HELIX    4 AA4 SER B   24  SER B   26  5                                   3    
HELIX    5 AA5 HIS B   54  MET B   58  5                                   5    
HELIX    6 AA6 GLN B   76  LYS B   80  5                                   5    
HELIX    7 AA7 SER C   24  SER C   26  5                                   3    
HELIX    8 AA8 HIS C   54  MET C   58  5                                   5    
HELIX    9 AA9 GLN C   76  LYS C   80  5                                   5    
HELIX   10 AB1 SER D   24  SER D   26  5                                   3    
HELIX   11 AB2 HIS D   54  MET D   58  5                                   5    
HELIX   12 AB3 GLN D   76  LYS D   80  5                                   5    
SHEET    1 AA112 LYS A  47  LYS A  49  0                                        
SHEET    2 AA112 VAL A  39  TYR A  44 -1  N  TYR A  44   O  LYS A  47           
SHEET    3 AA112 LEU A  28  ASP A  34 -1  N  VAL A  30   O  VAL A  43           
SHEET    4 AA112 GLY A  81  LYS A  90 -1  O  HIS A  88   N  VAL A  29           
SHEET    5 AA112 MET A  95  LEU A 108 -1  O  LEU A 105   N  GLY A  81           
SHEET    6 AA112 LEU A   1  TYR A   6  1  N  ALA A   5   O  SER A 106           
SHEET    7 AA112 LEU B   1  TYR B   6  1  O  LYS B   2   N  GLN A   4           
SHEET    8 AA112 MET B  95  LEU B 108  1  O  GLU B 104   N  ILE B   3           
SHEET    9 AA112 GLY B  81  LYS B  90 -1  N  GLY B  81   O  LEU B 105           
SHEET   10 AA112 LEU B  28  GLN B  33 -1  N  VAL B  29   O  HIS B  88           
SHEET   11 AA112 VAL B  39  TYR B  44 -1  O  VAL B  43   N  VAL B  30           
SHEET   12 AA112 LYS B  47  LYS B  49 -1  O  LYS B  47   N  TYR B  44           
SHEET    1 AA2 3 ALA A  11  PRO A  14  0                                        
SHEET    2 AA2 3 THR A  69  LEU A  72 -1  O  LEU A  70   N  LEU A  13           
SHEET    3 AA2 3 THR A  61  ASP A  64 -1  N  SER A  62   O  ARG A  71           
SHEET    1 AA3 3 ALA B  11  PRO B  14  0                                        
SHEET    2 AA3 3 THR B  69  LEU B  72 -1  O  LEU B  70   N  LEU B  13           
SHEET    3 AA3 3 THR B  61  ASP B  64 -1  N  SER B  62   O  ARG B  71           
SHEET    1 AA412 LYS C  47  LYS C  49  0                                        
SHEET    2 AA412 VAL C  39  TYR C  44 -1  N  TYR C  44   O  LYS C  47           
SHEET    3 AA412 LEU C  28  GLN C  33 -1  N  VAL C  30   O  VAL C  43           
SHEET    4 AA412 GLY C  81  LYS C  90 -1  O  ILE C  86   N  PHE C  31           
SHEET    5 AA412 MET C  95  LEU C 108 -1  O  SER C 103   N  TYR C  83           
SHEET    6 AA412 LEU C   1  TYR C   6  1  N  ILE C   3   O  GLU C 104           
SHEET    7 AA412 LEU D   1  TYR D   6  1  O  GLN D   4   N  GLN C   4           
SHEET    8 AA412 MET D  95  LEU D 108  1  O  LEU D 108   N  ALA D   5           
SHEET    9 AA412 GLY D  81  LYS D  90 -1  N  GLY D  81   O  LEU D 105           
SHEET   10 AA412 LEU D  28  GLN D  33 -1  N  PHE D  31   O  ILE D  86           
SHEET   11 AA412 VAL D  39  TYR D  44 -1  O  LEU D  40   N  TRP D  32           
SHEET   12 AA412 LYS D  47  LYS D  49 -1  O  LYS D  47   N  TYR D  44           
SHEET    1 AA5 3 ALA C  11  PRO C  14  0                                        
SHEET    2 AA5 3 THR C  69  LEU C  72 -1  O  LEU C  70   N  LEU C  13           
SHEET    3 AA5 3 THR C  61  ASP C  64 -1  N  SER C  62   O  ARG C  71           
SHEET    1 AA6 3 ALA D  11  PRO D  14  0                                        
SHEET    2 AA6 3 THR D  69  LEU D  72 -1  O  LEU D  70   N  LEU D  13           
SHEET    3 AA6 3 THR D  61  ASP D  64 -1  N  SER D  62   O  ARG D  71           
SSBOND   1 CYS A   15    CYS A   85                          1555   1555  2.08  
SSBOND   2 CYS B   15    CYS B   85                          1555   1555  2.05  
SSBOND   3 CYS C   15    CYS C   85                          1555   1555  2.05  
SSBOND   4 CYS D   15    CYS D   85                          1555   1555  2.07  
CRYST1   32.898   81.640   73.490  90.00  90.32  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      0.030397  0.000000  0.000170        0.00000                         
SCALE2      0.000000  0.012249  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013608        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system