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Database: PDB
Entry: 1ITB
LinkDB: 1ITB
Original site: 1ITB 
HEADER    COMPLEX (IMMUNOGLOBULIN/RECEPTOR)       15-JAN-97   1ITB              
TITLE     TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1            
TITLE    2 BETA                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 BETA;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TYPE 1 INTERLEUKIN-1 RECEPTOR;                             
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: SECRETED;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 CELLULAR_LOCATION: CELL SURFACE;                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNOGLOBULIN FOLD, TRANSMEMBRANE, GLYCOPROTEIN, RECEPTOR,           
KEYWDS   2 SIGNAL, COMPLEX (IMMUNOGLOBULIN/RECEPTOR)                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.P.A.VIGERS,L.J.ANDERSON,P.CAFFES,B.J.BRANDHUBER                     
REVDAT   2   24-FEB-09 1ITB    1       VERSN                                    
REVDAT   1   04-FEB-98 1ITB    0                                                
JRNL        AUTH   G.P.VIGERS,L.J.ANDERSON,P.CAFFES,B.J.BRANDHUBER              
JRNL        TITL   CRYSTAL STRUCTURE OF THE TYPE-I INTERLEUKIN-1                
JRNL        TITL 2 RECEPTOR COMPLEXED WITH INTERLEUKIN-1BETA.                   
JRNL        REF    NATURE                        V. 386   190 1997              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9062193                                                      
JRNL        DOI    10.1038/386190A0                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20723                          
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) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.325                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2061                            
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           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1246                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4308                       
REMARK   3   BIN FREE R VALUE                    : 0.5528                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 128                          
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            : 3587                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.70                          
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) : 0.44                            
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) : 1.98                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.55                            
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) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
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  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION WITH              
REMARK   3  SOLDENSITY = 0.40, SOLRAD = 0.25, B = 50                            
REMARK   4                                                                      
REMARK   4 1ITB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUL-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
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 RUH3R                       
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20723                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.900                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY HANGING      
REMARK 280  DROP DIFFUSION AGAINST 2.8M AMMONIUM SULFATE, 100MM MES PH          
REMARK 280  6.0, VAPOR DIFFUSION - HANGING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       73.47600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.22600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.47600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.22600            
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 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 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     LEU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     LYS B     5                                                      
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    GLU B 134   N   -  CA  -  C   ANGL. DEV. = -16.2 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    LEU A  10      122.74     63.25                                   
REMARK 500    SER A  21       61.59   -111.86                                   
REMARK 500    PRO A  23      118.27    -27.39                                   
REMARK 500    TYR A  24        8.41    110.04                                   
REMARK 500    GLU A  51       93.34    -68.90                                   
REMARK 500    ASN A  53      -53.54     77.74                                   
REMARK 500    LYS A  63      -97.66    -14.89                                   
REMARK 500    GLU A  64       54.53   -114.66                                   
REMARK 500    ASP A  75       34.99     70.38                                   
REMARK 500    ILE A 106      -85.02    -87.14                                   
REMARK 500    ASN A 107       63.36   -109.42                                   
REMARK 500    PHE A 117       72.51   -114.44                                   
REMARK 500    LYS A 138      -70.07     63.97                                   
REMARK 500    GLN A 141      -15.97    143.62                                   
REMARK 500    LYS B   7     -115.18   -119.05                                   
REMARK 500    GLU B  10     -108.69    -93.06                                   
REMARK 500    GLU B  11       71.97     97.78                                   
REMARK 500    ASN B  20       -8.51    105.31                                   
REMARK 500    PRO B  28      100.00    -69.55                                   
REMARK 500    ASN B  30     -132.73    -68.09                                   
REMARK 500    GLU B  33      -72.32   -111.05                                   
REMARK 500    HIS B  34      128.58     74.57                                   
REMARK 500    THR B  37      -25.55   -157.88                                   
REMARK 500    SER B  45       96.52     43.32                                   
REMARK 500    LYS B  46     -137.85   -124.01                                   
REMARK 500    PRO B  48       84.14    -61.75                                   
REMARK 500    VAL B  49       75.25    -11.03                                   
REMARK 500    SER B  50      174.87     51.34                                   
REMARK 500    THR B  51       14.94   -155.42                                   
REMARK 500    ARG B  56      -83.66    -87.00                                   
REMARK 500    HIS B  60     -129.74   -125.24                                   
REMARK 500    LYS B  61       71.52    -60.24                                   
REMARK 500    VAL B  67      -92.40     47.89                                   
REMARK 500    ALA B  69      120.20     37.86                                   
REMARK 500    SER B  74       83.23    -50.35                                   
REMARK 500    ARG B  82       84.01   -164.85                                   
REMARK 500    SER B  85      -30.42   -169.99                                   
REMARK 500    TYR B  86       62.29    -60.41                                   
REMARK 500    LEU B  88       -1.02   -147.62                                   
REMARK 500    ARG B  89      101.42     32.38                                   
REMARK 500    ILE B  92      -78.59   -105.19                                   
REMARK 500    SER B  93       92.02     83.33                                   
REMARK 500    ASN B 102      -19.72     75.12                                   
REMARK 500    TYR B 127       43.35     34.44                                   
REMARK 500    ASN B 133       97.08    -48.78                                   
REMARK 500    GLU B 134       56.05   -156.78                                   
REMARK 500    ASN B 135       34.67     75.96                                   
REMARK 500    LYS B 161     -135.53     57.83                                   
REMARK 500    LYS B 172       15.08    -69.69                                   
REMARK 500    LEU B 186       50.05     72.36                                   
REMARK 500    ALA B 215       61.49    -62.51                                   
REMARK 500    SER B 225     -175.28    -49.71                                   
REMARK 500    ASN B 246       61.89     60.07                                   
REMARK 500    ASP B 253       31.75    -94.58                                   
REMARK 500    ASN B 269       95.96   -162.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  68         0.07    SIDE_CHAIN                              
REMARK 500    TYR B  41         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1ITB A    1   153  UNP    P01584   IL1B_HUMAN     117    269             
DBREF  1ITB B    1   315  UNP    P14778   IL1R1_HUMAN     18    332             
SEQRES   1 A  153  ALA PRO VAL ARG SER LEU ASN CYS THR LEU ARG ASP SER          
SEQRES   2 A  153  GLN GLN LYS SER LEU VAL MET SER GLY PRO TYR GLU LEU          
SEQRES   3 A  153  LYS ALA LEU HIS LEU GLN GLY GLN ASP MET GLU GLN GLN          
SEQRES   4 A  153  VAL VAL PHE SER MET SER PHE VAL GLN GLY GLU GLU SER          
SEQRES   5 A  153  ASN ASP LYS ILE PRO VAL ALA LEU GLY LEU LYS GLU LYS          
SEQRES   6 A  153  ASN LEU TYR LEU SER CYS VAL LEU LYS ASP ASP LYS PRO          
SEQRES   7 A  153  THR LEU GLN LEU GLU SER VAL ASP PRO LYS ASN TYR PRO          
SEQRES   8 A  153  LYS LYS LYS MET GLU LYS ARG PHE VAL PHE ASN LYS ILE          
SEQRES   9 A  153  GLU ILE ASN ASN LYS LEU GLU PHE GLU SER ALA GLN PHE          
SEQRES  10 A  153  PRO ASN TRP TYR ILE SER THR SER GLN ALA GLU ASN MET          
SEQRES  11 A  153  PRO VAL PHE LEU GLY GLY THR LYS GLY GLY GLN ASP ILE          
SEQRES  12 A  153  THR ASP PHE THR MET GLN PHE VAL SER SER                      
SEQRES   1 B  315  LEU GLU ALA ASP LYS CYS LYS GLU ARG GLU GLU LYS ILE          
SEQRES   2 B  315  ILE LEU VAL SER SER ALA ASN GLU ILE ASP VAL ARG PRO          
SEQRES   3 B  315  CYS PRO LEU ASN PRO ASN GLU HIS LYS GLY THR ILE THR          
SEQRES   4 B  315  TRP TYR LYS ASP ASP SER LYS THR PRO VAL SER THR GLU          
SEQRES   5 B  315  GLN ALA SER ARG ILE HIS GLN HIS LYS GLU LYS LEU TRP          
SEQRES   6 B  315  PHE VAL PRO ALA LYS VAL GLU ASP SER GLY HIS TYR TYR          
SEQRES   7 B  315  CYS VAL VAL ARG ASN SER SER TYR CYS LEU ARG ILE LYS          
SEQRES   8 B  315  ILE SER ALA LYS PHE VAL GLU ASN GLU PRO ASN LEU CYS          
SEQRES   9 B  315  TYR ASN ALA GLN ALA ILE PHE LYS GLN LYS LEU PRO VAL          
SEQRES  10 B  315  ALA GLY ASP GLY GLY LEU VAL CYS PRO TYR MET GLU PHE          
SEQRES  11 B  315  PHE LYS ASN GLU ASN ASN GLU LEU PRO LYS LEU GLN TRP          
SEQRES  12 B  315  TYR LYS ASP CYS LYS PRO LEU LEU LEU ASP ASN ILE HIS          
SEQRES  13 B  315  PHE SER GLY VAL LYS ASP ARG LEU ILE VAL MET ASN VAL          
SEQRES  14 B  315  ALA GLU LYS HIS ARG GLY ASN TYR THR CYS HIS ALA SER          
SEQRES  15 B  315  TYR THR TYR LEU GLY LYS GLN TYR PRO ILE THR ARG VAL          
SEQRES  16 B  315  ILE GLU PHE ILE THR LEU GLU GLU ASN LYS PRO THR ARG          
SEQRES  17 B  315  PRO VAL ILE VAL SER PRO ALA ASN GLU THR MET GLU VAL          
SEQRES  18 B  315  ASP LEU GLY SER GLN ILE GLN LEU ILE CYS ASN VAL THR          
SEQRES  19 B  315  GLY GLN LEU SER ASP ILE ALA TYR TRP LYS TRP ASN GLY          
SEQRES  20 B  315  SER VAL ILE ASP GLU ASP ASP PRO VAL LEU GLY GLU ASP          
SEQRES  21 B  315  TYR TYR SER VAL GLU ASN PRO ALA ASN LYS ARG ARG SER          
SEQRES  22 B  315  THR LEU ILE THR VAL LEU ASN ILE SER GLU ILE GLU SER          
SEQRES  23 B  315  ARG PHE TYR LYS HIS PRO PHE THR CYS PHE ALA LYS ASN          
SEQRES  24 B  315  THR HIS GLY ILE ASP ALA ALA TYR ILE GLN LEU ILE TYR          
SEQRES  25 B  315  PRO VAL THR                                                  
FORMUL   3  HOH   *24(H2 O)                                                     
HELIX    1   1 ASP A   35  GLN A   38  5                                   4    
HELIX    2   2 LYS A   97  PHE A   99  5                                   3    
HELIX    3   3 VAL B   71  ASP B   73  5                                   3    
HELIX    4   4 ALA B  107  ALA B  109  5                                   3    
HELIX    5   5 GLU B  171  HIS B  173  5                                   3    
HELIX    6   6 SER B  286  TYR B  289  5                                   4    
SHEET    1   A 5 ARG A   4  CYS A   8  0                                        
SHEET    2   A 5 PHE A  42  PHE A  46 -1  N  PHE A  46   O  ARG A   4           
SHEET    3   A 5 LYS A  55  LEU A  62 -1  N  GLY A  61   O  SER A  43           
SHEET    4   A 5 PHE A 101  GLU A 105 -1  N  LYS A 103   O  ILE A  56           
SHEET    5   A 5 LEU A 110  SER A 114 -1  N  GLU A 113   O  ASN A 102           
SHEET    1   B 2 SER A  17  MET A  20  0                                        
SHEET    2   B 2 LEU A  26  LEU A  29 -1  N  LEU A  29   O  SER A  17           
SHEET    1   C 2 LEU A  67  LYS A  74  0                                        
SHEET    2   C 2 LYS A  77  SER A  84 -1  N  GLU A  83   O  TYR A  68           
SHEET    1   D 2 TYR A 121  SER A 123  0                                        
SHEET    2   D 2 PHE A 133  GLY A 135 -1  N  GLY A 135   O  TYR A 121           
SHEET    1   E 2 LEU B  15  SER B  18  0                                        
SHEET    2   E 2 ALA B  94  VAL B  97  1  N  LYS B  95   O  LEU B  15           
SHEET    1   F 3 ASP B  23  ARG B  25  0                                        
SHEET    2   F 3 LYS B  63  PHE B  66 -1  N  PHE B  66   O  ASP B  23           
SHEET    3   F 3 ILE B  57  HIS B  60 -1  N  HIS B  60   O  LYS B  63           
SHEET    1   G 2 HIS B  76  CYS B  79  0                                        
SHEET    2   G 2 ILE B  90  SER B  93 -1  N  ILE B  92   O  TYR B  77           
SHEET    1   H 4 ILE B 110  PRO B 116  0                                        
SHEET    2   H 4 GLY B 187  THR B 200  1  N  ARG B 194   O  PHE B 111           
SHEET    3   H 4 GLY B 175  TYR B 185 -1  N  TYR B 185   O  GLY B 187           
SHEET    4   H 4 GLN B 142  LYS B 145 -1  N  TYR B 144   O  THR B 178           
SHEET    1   I 3 GLY B 121  VAL B 124  0                                        
SHEET    2   I 3 ARG B 163  VAL B 166 -1  N  VAL B 166   O  GLY B 121           
SHEET    3   I 3 PHE B 157  VAL B 160 -1  N  VAL B 160   O  ARG B 163           
SHEET    1   J 4 GLU B 217  GLU B 220  0                                        
SHEET    2   J 4 GLY B 302  ILE B 311  1  N  GLN B 309   O  GLU B 217           
SHEET    3   J 4 PHE B 293  ASN B 299 -1  N  ASN B 299   O  GLY B 302           
SHEET    4   J 4 ILE B 240  TRP B 245 -1  N  LYS B 244   O  THR B 294           
SHEET    1   K 3 ILE B 227  GLY B 235  0                                        
SHEET    2   K 3 SER B 273  ILE B 281 -1  N  ILE B 281   O  ILE B 227           
SHEET    3   K 3 LEU B 257  VAL B 264 -1  N  VAL B 264   O  THR B 274           
SSBOND   1 CYS B    6    CYS B   87                          1555   1555  2.03  
SSBOND   2 CYS B   27    CYS B   79                          1555   1555  2.03  
SSBOND   3 CYS B  104    CYS B  147                          1555   1555  2.04  
SSBOND   4 CYS B  125    CYS B  179                          1555   1555  2.02  
SSBOND   5 CYS B  231    CYS B  295                          1555   1555  2.01  
CISPEP   1 TYR A   90    PRO A   91          0        -0.08                     
CRYST1  146.952   68.452   65.867  90.00 108.95  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006805  0.000000  0.002336        0.00000                         
SCALE2      0.000000  0.014609  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016052        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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