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Database: PDB
Entry: 1G0Y
LinkDB: 1G0Y
Original site: 1G0Y 
HEADER    IMMUNE SYSTEM                           09-OCT-00   1G0Y              
TITLE     IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 RECEPTOR, TYPE I;                            
COMPND   3 CHAIN: R;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ANTAGONIST PEPTIDE AF10847;                                
COMPND   7 CHAIN: I;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL: SF9 CELLS;                                   
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED BY SOLID-PHASE SYNTHESIS. 
KEYWDS    IMMUNOGLOBULIN, IMMUNE SYSTEM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.P.A.VIGERS,D.J.DRIPPS,C.K.EDWARDS,B.J.BRANDHUBER                    
REVDAT   6   31-JAN-18 1G0Y    1       JRNL   REMARK                            
REVDAT   5   24-JAN-18 1G0Y    1       JRNL                                     
REVDAT   4   24-FEB-09 1G0Y    1       VERSN                                    
REVDAT   3   01-APR-03 1G0Y    1       JRNL                                     
REVDAT   2   29-NOV-00 1G0Y    1       JRNL   REMARK                            
REVDAT   1   25-OCT-00 1G0Y    0                                                
JRNL        AUTH   G.P.VIGERS,D.J.DRIPPS,C.K.EDWARDS III,B.J.BRANDHUBER         
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF A SMALL ANTAGONIST PEPTIDE BOUND  
JRNL        TITL 2 TO INTERLEUKIN-1 RECEPTOR TYPE 1.                            
JRNL        REF    J.BIOL.CHEM.                  V. 275 36927 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10903327                                                     
JRNL        DOI    10.1074/JBC.M006071200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11171                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 10% OF OBSERVED                 
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.332                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1106                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2694                                    
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.910                           
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  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 1G0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012096.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 120.0                              
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11894                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 10.50                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 73.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.36900                            
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: NULL                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% POLYETHYLENE GLYCOL 4000, 0.2 M      
REMARK 280  AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 4.5, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 20K, TEMPERATURE 293.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      138.67800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.33900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      104.00850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       34.66950            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      173.34750            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      138.67800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       69.33900            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       34.66950            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      104.00850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      173.34750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP R     4                                                      
REMARK 465     LYS R     5                                                      
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    LYS R   7      107.23     65.97                                   
REMARK 500    PRO R  28       82.49    -63.76                                   
REMARK 500    PRO R  31      -78.51    -53.47                                   
REMARK 500    HIS R  34       80.32    -62.73                                   
REMARK 500    THR R  37      116.15     75.61                                   
REMARK 500    ASP R  44      165.25     61.19                                   
REMARK 500    LYS R  46     -136.16   -161.15                                   
REMARK 500    ALA R  54     -102.11    -73.65                                   
REMARK 500    SER R  55      130.15      8.34                                   
REMARK 500    VAL R  67      -72.10    -60.44                                   
REMARK 500    ALA R  69       86.68     34.44                                   
REMARK 500    ASN R  83      -72.73    -65.48                                   
REMARK 500    SER R  84      -41.70   -174.23                                   
REMARK 500    SER R  93      120.64     69.88                                   
REMARK 500    CYS R 125      105.71    -59.39                                   
REMARK 500    ASN R 133       14.77    -67.15                                   
REMARK 500    ASN R 136      -24.35     66.48                                   
REMARK 500    CYS R 147      -15.05     83.23                                   
REMARK 500    LYS R 161     -119.00     54.02                                   
REMARK 500    ILE R 199     -152.89   -111.53                                   
REMARK 500    GLU R 202     -171.74   -172.20                                   
REMARK 500    GLU R 203      -57.50     75.57                                   
REMARK 500    ASN R 204      -87.54    -80.39                                   
REMARK 500    LYS R 205       54.12   -174.76                                   
REMARK 500    SER R 213      -80.12    -67.69                                   
REMARK 500    ALA R 215       61.35   -116.14                                   
REMARK 500    ASN R 216       66.67     38.99                                   
REMARK 500    LEU R 223      -51.34    -27.15                                   
REMARK 500    SER R 225      170.68    -42.80                                   
REMARK 500    ARG R 272       69.71   -119.57                                   
REMARK 500    ASN R 299       11.91   -163.08                                   
REMARK 500    THR I   2       79.21   -119.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ITB   RELATED DB: PDB                                   
REMARK 900 TYPE 1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH IL-1BETA.               
REMARK 900 RELATED ID: 1IRA   RELATED DB: PDB                                   
REMARK 900 TYPE 1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH IL-1RA                  
DBREF  1G0Y R    4   315  UNP    P14778   IL1R1_HUMAN     21    332             
DBREF  1G0Y I    1    21  PDB    1G0Y     1G0Y             1     21             
SEQRES   1 R  312  ASP LYS CYS LYS GLU ARG GLU GLU LYS ILE ILE LEU VAL          
SEQRES   2 R  312  SER SER ALA ASN GLU ILE ASP VAL ARG PRO CYS PRO LEU          
SEQRES   3 R  312  ASN PRO ASN GLU HIS LYS GLY THR ILE THR TRP TYR LYS          
SEQRES   4 R  312  ASP ASP SER LYS THR PRO VAL SER THR GLU GLN ALA SER          
SEQRES   5 R  312  ARG ILE HIS GLN HIS LYS GLU LYS LEU TRP PHE VAL PRO          
SEQRES   6 R  312  ALA LYS VAL GLU ASP SER GLY HIS TYR TYR CYS VAL VAL          
SEQRES   7 R  312  ARG ASN SER SER TYR CYS LEU ARG ILE LYS ILE SER ALA          
SEQRES   8 R  312  LYS PHE VAL GLU ASN GLU PRO ASN LEU CYS TYR ASN ALA          
SEQRES   9 R  312  GLN ALA ILE PHE LYS GLN LYS LEU PRO VAL ALA GLY ASP          
SEQRES  10 R  312  GLY GLY LEU VAL CYS PRO TYR MET GLU PHE PHE LYS ASN          
SEQRES  11 R  312  GLU ASN ASN GLU LEU PRO LYS LEU GLN TRP TYR LYS ASP          
SEQRES  12 R  312  CYS LYS PRO LEU LEU LEU ASP ASN ILE HIS PHE SER GLY          
SEQRES  13 R  312  VAL LYS ASP ARG LEU ILE VAL MET ASN VAL ALA GLU LYS          
SEQRES  14 R  312  HIS ARG GLY ASN TYR THR CYS HIS ALA SER TYR THR TYR          
SEQRES  15 R  312  LEU GLY LYS GLN TYR PRO ILE THR ARG VAL ILE GLU PHE          
SEQRES  16 R  312  ILE THR LEU GLU GLU ASN LYS PRO THR ARG PRO VAL ILE          
SEQRES  17 R  312  VAL SER PRO ALA ASN GLU THR MET GLU VAL ASP LEU GLY          
SEQRES  18 R  312  SER GLN ILE GLN LEU ILE CYS ASN VAL THR GLY GLN LEU          
SEQRES  19 R  312  SER ASP ILE ALA TYR TRP LYS TRP ASN GLY SER VAL ILE          
SEQRES  20 R  312  ASP GLU ASP ASP PRO VAL LEU GLY GLU ASP TYR TYR SER          
SEQRES  21 R  312  VAL GLU ASN PRO ALA ASN LYS ARG ARG SER THR LEU ILE          
SEQRES  22 R  312  THR VAL LEU ASN ILE SER GLU ILE GLU SER ARG PHE TYR          
SEQRES  23 R  312  LYS HIS PRO PHE THR CYS PHE ALA LYS ASN THR HIS GLY          
SEQRES  24 R  312  ILE ASP ALA ALA TYR ILE GLN LEU ILE TYR PRO VAL THR          
SEQRES   1 I   21  GLU THR PRO PHE THR TRP GLU GLU SER ASN ALA TYR TYR          
SEQRES   2 I   21  TRP GLN PRO TYR ALA LEU PRO LEU                              
HELIX    1   1 LYS R   70  SER R   74  5                                   5    
HELIX    2   2 ASN R  106  ILE R  110  5                                   5    
HELIX    3   3 MET R  128  LYS R  132  5                                   5    
HELIX    4   4 THR I    5  TYR I   12  1                                   8    
SHEET    1   A 9 ILE R  38  TYR R  41  0                                        
SHEET    2   A 9 TYR R  78  ARG R  82 -1  N  TYR R  78   O  TYR R  41           
SHEET    3   A 9 CYS R  87  LYS R  91 -1  O  LEU R  88   N  VAL R  81           
SHEET    4   A 9 GLU R   8  GLU R  11  1  O  ARG R   9   N  LYS R  91           
SHEET    5   A 9 GLU R 217  GLU R 220 -1  O  THR R 218   N  GLU R  10           
SHEET    6   A 9 ILE R 303  ILE R 311  1  O  TYR R 307   N  GLU R 217           
SHEET    7   A 9 PHE R 293  LYS R 298 -1  N  PHE R 293   O  ILE R 308           
SHEET    8   A 9 ILE R 240  TRP R 245 -1  N  ILE R 240   O  LYS R 298           
SHEET    9   A 9 SER R 248  VAL R 249 -1  O  SER R 248   N  TRP R 245           
SHEET    1   B 2 LEU R  15  SER R  18  0                                        
SHEET    2   B 2 ALA R  94  VAL R  97  1  O  LYS R  95   N  SER R  17           
SHEET    1   C 3 ASP R  23  ARG R  25  0                                        
SHEET    2   C 3 LYS R  63  PHE R  66 -1  N  LEU R  64   O  ARG R  25           
SHEET    3   C 3 ILE R  57  HIS R  60 -1  O  HIS R  58   N  TRP R  65           
SHEET    1   D 2 LYS R 112  GLN R 113  0                                        
SHEET    2   D 2 TYR I  13  TRP I  14 -1  O  TRP I  14   N  LYS R 112           
SHEET    1   E 3 LEU R 123  VAL R 124  0                                        
SHEET    2   E 3 ARG R 163  VAL R 166 -1  N  LEU R 164   O  LEU R 123           
SHEET    3   E 3 PHE R 157  VAL R 160 -1  O  SER R 158   N  ILE R 165           
SHEET    1   F 4 LYS R 148  PRO R 149  0                                        
SHEET    2   F 4 GLN R 142  LYS R 145 -1  O  LYS R 145   N  LYS R 148           
SHEET    3   F 4 GLY R 175  THR R 184 -1  O  THR R 178   N  TYR R 144           
SHEET    4   F 4 GLN R 189  PHE R 198 -1  N  TYR R 190   O  TYR R 183           
SHEET    1   G 4 VAL R 210  ILE R 211  0                                        
SHEET    2   G 4 ILE R 227  GLY R 235 -1  N  THR R 234   O  VAL R 210           
SHEET    3   G 4 SER R 273  ILE R 281 -1  N  SER R 273   O  GLY R 235           
SHEET    4   G 4 LEU R 257  VAL R 264 -1  O  GLY R 258   N  ASN R 280           
SSBOND   1 CYS R    6    CYS R   87                          1555   1555  2.03  
SSBOND   2 CYS R   27    CYS R   79                          1555   1555  2.02  
SSBOND   3 CYS R  104    CYS R  147                          1555   1555  2.04  
SSBOND   4 CYS R  125    CYS R  179                          1555   1555  2.03  
SSBOND   5 CYS R  231    CYS R  295                          1555   1555  2.01  
CRYST1   95.898   95.898  208.017  90.00  90.00 120.00 P 65 2 2     12          
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      0.010430  0.006020  0.000000        0.00000                         
SCALE2      0.000000  0.012040  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004810        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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