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Database: PDB
Entry: 1IRA
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Original site: 1IRA 
HEADER    COMPLEX (CYTOKINE RECEPTOR/ANTAGONIST)  09-APR-98   1IRA              
TITLE     COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR 
TITLE    2 ANTAGONIST (IL1RA)                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 RECEPTOR ANTAGONIST;                         
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: IL1RA;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTERLEUKIN-1 RECEPTOR;                                    
COMPND   8 CHAIN: Y;                                                            
COMPND   9 FRAGMENT: TYPE I RECEPTOR, EXTRACELLULAR DOMAINS;                    
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: SF9;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: TAC-BSP;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 CELL_LINE: SF9;                                                      
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    CYTOKINE RECEPTOR, RECEPTOR ANTAGONIST, IMMUNOGLOBULIN FOLD, COMPLEX  
KEYWDS   2 (CYTOKINE RECEPTOR-ANTAGONIST), COMPLEX (CYTOKINE RECEPTOR-          
KEYWDS   3 ANTAGONIST) COMPLEX                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.A.SCHREUDER,C.TARDIF,S.TRAMP-KALMEYER,A.SOFFIENTINI,E.SARUBBI,      
AUTHOR   2 A.AKESON,T.BOWLIN,S.YANOFSKY,R.W.BARRETT                             
REVDAT   5   29-JUL-20 1IRA    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   04-APR-18 1IRA    1       REMARK                                   
REVDAT   3   13-JUL-11 1IRA    1       VERSN                                    
REVDAT   2   24-FEB-09 1IRA    1       VERSN                                    
REVDAT   1   17-JUN-98 1IRA    0                                                
JRNL        AUTH   H.SCHREUDER,C.TARDIF,S.TRUMP-KALLMEYER,A.SOFFIENTINI,        
JRNL        AUTH 2 E.SARUBBI,A.AKESON,T.BOWLIN,S.YANOFSKY,R.W.BARRETT           
JRNL        TITL   A NEW CYTOKINE-RECEPTOR BINDING MODE REVEALED BY THE CRYSTAL 
JRNL        TITL 2 STRUCTURE OF THE IL-1 RECEPTOR WITH AN ANTAGONIST.           
JRNL        REF    NATURE                        V. 386   194 1997              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9062194                                                      
JRNL        DOI    10.1038/386194A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.SCHREUDER,C.TARDIF,A.SOFFIENTINI,E.SARUBBI,A.AKESON,       
REMARK   1  AUTH 2 T.BOWLIN,S.YANOFSKY,R.W.BARRETT                              
REMARK   1  TITL   CRYSTALS OF SOLUBLE INTERLEUKIN-1 RECEPTOR COMPLEXED WITH    
REMARK   1  TITL 2 ITS NATURAL ANTAGONIST REVEAL A 1:1 RECEPTOR-LIGAND COMPLEX  
REMARK   1  REF    FEBS LETT.                    V. 373    39 1995              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.A.SCHREUDER,J.M.RONDEAU,C.TARDIF,A.SOFFIENTINI,E.SARUBBI,  
REMARK   1  AUTH 2 A.AKESON,T.L.BOWLIN,S.YANOFSKY,R.W.BARRETT                   
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF THE INTERLEUKIN-1 RECEPTOR      
REMARK   1  TITL 2 ANTAGONIST. PRESENCE OF A DISULFIDE LINK AND A CIS-PROLINE   
REMARK   1  REF    EUR.J.BIOCHEM.                V. 227   838 1995              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15012                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.314                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1463                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3930                       
REMARK   3   BIN FREE R VALUE                    : 0.4660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 172                          
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            : 3638                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.20                          
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) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.000                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.400 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 11.500; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 8.300 ; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 17.700; 8.000                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM3_MOD.PRO                                 
REMARK   3  PARAMETER FILE  3  : WAT.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : WAT.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174235.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 296                                
REMARK 200  PH                             : 7.0                                
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          : MACSCIENCE M18X                    
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : COLLIMATOR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15631                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR + MOLECULAR              
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: SQUASH, X-PLOR3.1                                     
REMARK 200 STARTING MODEL: IL1RA STRUCTURE (PDB ENTRY 1ILR) AND TRUNCATED CD4   
REMARK 200  DOMAIN (PDB ENTRY 2CD4)                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE COMPLEX OF THE IL-1 RECEPTOR WITH    
REMARK 280  THE ANTAGONIST WAS PREPARED BY MIXING A SOLUTION OF IL-1            
REMARK 280  RECEPTOR IN 50 MM TRIS (PH 7.5) AND 150 MM NACL WITH A SOLUTION     
REMARK 280  OF IL1RA IN THE SAME BUFFER. THE COMPLEX WAS CRYSTALLIZED USING     
REMARK 280  THE HANGING DROP METHOD. THE DROPS WERE PREPARED BY MIXING 4 UL     
REMARK 280  OF THE PROTEIN SOLUTION WITH 1 UL OF RESERVOIR SOLUTION,            
REMARK 280  CONTAINING 30% (W/V) PEG 3350, 400 MM MGCL2 IN 100 MM MOPS          
REMARK 280  BUFFER (PH 7.0)., VAPOR DIFFUSION - HANGING DROP, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.60000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.60000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y                                  
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     ARG X     1                                                      
REMARK 465     PRO X     2                                                      
REMARK 465     SER X     3                                                      
REMARK 465     GLY X     4                                                      
REMARK 465     ARG X     5                                                      
REMARK 465     LYS X     6                                                      
REMARK 465     GLU X   152                                                      
REMARK 465     LEU Y    -2                                                      
REMARK 465     GLU Y    -1                                                      
REMARK 465     ALA Y     0                                                      
REMARK 465     THR Y   312                                                      
REMARK 465     ASN Y   313                                                      
REMARK 465     PHE Y   314                                                      
REMARK 465     GLN Y   315                                                      
REMARK 465     LYS Y   316                                                      
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     SER X   7    OG                                                  
REMARK 470     ASP X  74    CG   OD1  OD2                                       
REMARK 470     LYS Y   4    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS Y 185    CG   CD   CE   NZ                                   
REMARK 470     LYS Y 202    CG   CD   CE   NZ                                   
REMARK 470     ASP Y 250    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER X   8      -77.58    -95.91                                   
REMARK 500    ASP X  74      -10.69   -141.46                                   
REMARK 500    LYS Y   2       43.34    -78.93                                   
REMARK 500    GLU Y   5      124.99     70.23                                   
REMARK 500    PRO Y  25       76.50    -63.80                                   
REMARK 500    ASP Y  40      -35.60    -32.62                                   
REMARK 500    SER Y  42       -0.99    -58.16                                   
REMARK 500    ARG Y  53      -80.78    -47.35                                   
REMARK 500    GLU Y  69        2.48    -66.90                                   
REMARK 500    SER Y  82       41.84   -146.06                                   
REMARK 500    VAL Y 114     -178.71    -67.23                                   
REMARK 500    ALA Y 115      -42.56     73.84                                   
REMARK 500    PHE Y 128       38.03    -96.95                                   
REMARK 500    LYS Y 158     -115.25     50.94                                   
REMARK 500    ASN Y 165       78.90     52.65                                   
REMARK 500    PRO Y 211     -178.95    -68.58                                   
REMARK 500    ASN Y 296     -167.09   -165.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1IRA X    1   152  UNP    P18510   IL1RA_HUMAN     26    177             
DBREF  1IRA Y   -2   316  UNP    P14778   IL1R1_HUMAN     18    336             
SEQRES   1 X  152  ARG PRO SER GLY ARG LYS SER SER LYS MET GLN ALA PHE          
SEQRES   2 X  152  ARG ILE TRP ASP VAL ASN GLN LYS THR PHE TYR LEU ARG          
SEQRES   3 X  152  ASN ASN GLN LEU VAL ALA GLY TYR LEU GLN GLY PRO ASN          
SEQRES   4 X  152  VAL ASN LEU GLU GLU LYS ILE ASP VAL VAL PRO ILE GLU          
SEQRES   5 X  152  PRO HIS ALA LEU PHE LEU GLY ILE HIS GLY GLY LYS MET          
SEQRES   6 X  152  CYS LEU SER CYS VAL LYS SER GLY ASP GLU THR ARG LEU          
SEQRES   7 X  152  GLN LEU GLU ALA VAL ASN ILE THR ASP LEU SER GLU ASN          
SEQRES   8 X  152  ARG LYS GLN ASP LYS ARG PHE ALA PHE ILE ARG SER ASP          
SEQRES   9 X  152  SER GLY PRO THR THR SER PHE GLU SER ALA ALA CYS PRO          
SEQRES  10 X  152  GLY TRP PHE LEU CYS THR ALA MET GLU ALA ASP GLN PRO          
SEQRES  11 X  152  VAL SER LEU THR ASN MET PRO ASP GLU GLY VAL MET VAL          
SEQRES  12 X  152  THR LYS PHE TYR PHE GLN GLU ASP GLU                          
SEQRES   1 Y  319  LEU GLU ALA ASP LYS CYS LYS GLU ARG GLU GLU LYS ILE          
SEQRES   2 Y  319  ILE LEU VAL SER SER ALA ASN GLU ILE ASP VAL ARG PRO          
SEQRES   3 Y  319  CYS PRO LEU ASN PRO ASN GLU HIS LYS GLY THR ILE THR          
SEQRES   4 Y  319  TRP TYR LYS ASP ASP SER LYS THR PRO VAL SER THR GLU          
SEQRES   5 Y  319  GLN ALA SER ARG ILE HIS GLN HIS LYS GLU LYS LEU TRP          
SEQRES   6 Y  319  PHE VAL PRO ALA LYS VAL GLU ASP SER GLY HIS TYR TYR          
SEQRES   7 Y  319  CYS VAL VAL ARG ASN SER SER TYR CYS LEU ARG ILE LYS          
SEQRES   8 Y  319  ILE SER ALA LYS PHE VAL GLU ASN GLU PRO ASN LEU CYS          
SEQRES   9 Y  319  TYR ASN ALA GLN ALA ILE PHE LYS GLN LYS LEU PRO VAL          
SEQRES  10 Y  319  ALA GLY ASP GLY GLY LEU VAL CYS PRO TYR MET GLU PHE          
SEQRES  11 Y  319  PHE LYS ASN GLU ASN ASN GLU LEU PRO LYS LEU GLN TRP          
SEQRES  12 Y  319  TYR LYS ASP CYS LYS PRO LEU LEU LEU ASP ASN ILE HIS          
SEQRES  13 Y  319  PHE SER GLY VAL LYS ASP ARG LEU ILE VAL MET ASN VAL          
SEQRES  14 Y  319  ALA GLU LYS HIS ARG GLY ASN TYR THR CYS HIS ALA SER          
SEQRES  15 Y  319  TYR THR TYR LEU GLY LYS GLN TYR PRO ILE THR ARG VAL          
SEQRES  16 Y  319  ILE GLU PHE ILE THR LEU GLU GLU ASN LYS PRO THR ARG          
SEQRES  17 Y  319  PRO VAL ILE VAL SER PRO ALA ASN GLU THR MET GLU VAL          
SEQRES  18 Y  319  ASP LEU GLY SER GLN ILE GLN LEU ILE CYS ASN VAL THR          
SEQRES  19 Y  319  GLY GLN LEU SER ASP ILE ALA TYR TRP LYS TRP ASN GLY          
SEQRES  20 Y  319  SER VAL ILE ASP GLU ASP ASP PRO VAL LEU GLY GLU ASP          
SEQRES  21 Y  319  TYR TYR SER VAL GLU ASN PRO ALA ASN LYS ARG ARG SER          
SEQRES  22 Y  319  THR LEU ILE THR VAL LEU ASN ILE SER GLU ILE GLU SER          
SEQRES  23 Y  319  ARG PHE TYR LYS HIS PRO PHE THR CYS PHE ALA LYS ASN          
SEQRES  24 Y  319  THR HIS GLY ILE ASP ALA ALA TYR ILE GLN LEU ILE TYR          
SEQRES  25 Y  319  PRO VAL THR ASN PHE GLN LYS                                  
MODRES 1IRA ASN Y  173  ASN  GLYCOSYLATION SITE                                 
MODRES 1IRA ASN Y  213  ASN  GLYCOSYLATION SITE                                 
MODRES 1IRA ASN Y  229  ASN  GLYCOSYLATION SITE                                 
MODRES 1IRA ASN Y  243  ASN  GLYCOSYLATION SITE                                 
HET    NAG  Y 401      14                                                       
HET    NAG  Y 402      14                                                       
HET    NAG  Y 403      14                                                       
HET    NAG  Y 404      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   7  HOH   *86(H2 O)                                                     
HELIX    1   1 GLY X   37  LEU X   42  5                                   6    
HELIX    2   2 ILE X   85  ASP X   87  5                                   3    
HELIX    3   3 LYS X   93  PHE X   98  5                                   6    
HELIX    4   4 PRO X  137  GLU X  139  5                                   3    
HELIX    5   5 PRO Y   28  GLU Y   30  5                                   3    
HELIX    6   6 VAL Y   68  ASP Y   70  5                                   3    
HELIX    7   7 ALA Y  104  ALA Y  106  5                                   3    
HELIX    8   8 MET Y  125  PHE Y  128  5                                   4    
HELIX    9   9 GLU Y  168  HIS Y  170  5                                   3    
HELIX   10  10 LYS Y  267  ARG Y  269  5                                   3    
HELIX   11  11 SER Y  283  TYR Y  286  5                                   4    
SHEET    1   A 6 PHE X 146  GLU X 150  0                                        
SHEET    2   A 6 GLN X  11  ASP X  17 -1  N  TRP X  16   O  TYR X 147           
SHEET    3   A 6 ILE X  46  GLU X  52 -1  N  VAL X  48   O  GLN X  11           
SHEET    4   A 6 ALA X  55  GLY X  59 -1  N  GLY X  59   O  ASP X  47           
SHEET    5   A 6 ALA X  99  SER X 105 -1  N  PHE X 100   O  LEU X  56           
SHEET    6   A 6 THR X 108  SER X 113 -1  N  GLU X 112   O  ILE X 101           
SHEET    1   B 2 THR X  22  ARG X  26  0                                        
SHEET    2   B 2 GLN X  29  GLY X  33 -1  N  GLY X  33   O  THR X  22           
SHEET    1   C 2 CYS X  66  SER X  72  0                                        
SHEET    2   C 2 GLU X  75  GLU X  81 -1  N  GLU X  81   O  CYS X  66           
SHEET    1   D 2 PHE X 120  CYS X 122  0                                        
SHEET    2   D 2 SER X 132  THR X 134 -1  N  THR X 134   O  PHE X 120           
SHEET    1   E 4 LEU Y  12  SER Y  15  0                                        
SHEET    2   E 4 TYR Y  83  VAL Y  94  1  N  LYS Y  92   O  LEU Y  12           
SHEET    3   E 4 GLY Y  72  ASN Y  80 -1  N  ASN Y  80   O  TYR Y  83           
SHEET    4   E 4 THR Y  34  TYR Y  38 -1  N  TYR Y  38   O  TYR Y  75           
SHEET    1   F 3 ASP Y  20  ARG Y  22  0                                        
SHEET    2   F 3 LYS Y  60  PHE Y  63 -1  N  PHE Y  63   O  ASP Y  20           
SHEET    3   F 3 ILE Y  54  HIS Y  57 -1  N  HIS Y  57   O  LYS Y  60           
SHEET    1   G 4 PHE Y 108  PRO Y 113  0                                        
SHEET    2   G 4 LYS Y 185  LEU Y 198  1  N  GLU Y 194   O  PHE Y 108           
SHEET    3   G 4 GLY Y 172  TYR Y 182 -1  N  TYR Y 182   O  LYS Y 185           
SHEET    4   G 4 GLN Y 139  LYS Y 142 -1  N  TYR Y 141   O  THR Y 175           
SHEET    1   H 3 GLY Y 118  VAL Y 121  0                                        
SHEET    2   H 3 ARG Y 160  VAL Y 163 -1  N  VAL Y 163   O  GLY Y 118           
SHEET    3   H 3 PHE Y 154  VAL Y 157 -1  N  VAL Y 157   O  ARG Y 160           
SHEET    1   I 4 GLU Y 214  GLU Y 217  0                                        
SHEET    2   I 4 ILE Y 300  ILE Y 308  1  N  GLN Y 306   O  GLU Y 214           
SHEET    3   I 4 PHE Y 290  LYS Y 295 -1  N  ALA Y 294   O  ASP Y 301           
SHEET    4   I 4 ILE Y 237  TRP Y 242 -1  N  LYS Y 241   O  THR Y 291           
SHEET    1   J 4 LEU Y 254  VAL Y 261  0                                        
SHEET    2   J 4 SER Y 270  ILE Y 278 -1  N  ASN Y 277   O  GLY Y 255           
SHEET    3   J 4 ILE Y 224  GLY Y 232 -1  N  GLY Y 232   O  SER Y 270           
SHEET    4   J 4 VAL Y 207  SER Y 210 -1  N  SER Y 210   O  ASN Y 229           
SSBOND   1 CYS X   69    CYS X  116                          1555   1555  2.03  
SSBOND   2 CYS Y    3    CYS Y   84                          1555   1555  2.03  
SSBOND   3 CYS Y   24    CYS Y   76                          1555   1555  2.03  
SSBOND   4 CYS Y  101    CYS Y  144                          1555   1555  2.03  
SSBOND   5 CYS Y  122    CYS Y  176                          1555   1555  2.03  
SSBOND   6 CYS Y  228    CYS Y  292                          1555   1555  2.02  
LINK         ND2 ASN Y 173                 C1  NAG Y 401     1555   1555  1.45  
LINK         ND2 ASN Y 213                 C1  NAG Y 402     1555   1555  1.45  
LINK         ND2 ASN Y 229                 C1  NAG Y 403     1555   1555  1.45  
LINK         ND2 ASN Y 243                 C1  NAG Y 404     1555   1555  1.45  
CISPEP   1 VAL Y   64    PRO Y   65          0        -0.29                     
CISPEP   2 SER Y  210    PRO Y  211          0        -0.02                     
CRYST1   47.200   84.600  140.200  90.00  90.00  90.00 P 21 21 21    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      0.021186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011820  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007133        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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