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Database: PDB
Entry: 1I1R
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Original site: 1I1R 
HEADER    CYTOKINE                                02-FEB-01   1I1R              
TITLE     CRYSTAL STRUCTURE OF A CYTOKINE/RECEPTOR COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-6 RECEPTOR BETA CHAIN;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DOMAINS 1, 2, 3 OF THE GP130 EXTRACELLULAR                 
COMPND   5 DOMAIN (RESIDUES 1-303);                                             
COMPND   6 SYNONYM: GP130;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: EXPRESSED IN THE PRESENCE OF INHIBITOR OF N-          
COMPND   9 LINKED GLYCOSYLATION (TUNICAMYCIN);                                  
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: VIRAL IL-6;                                                
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: FUNCTIONAL INTERLEUKIN-6 HOMOLOG;                           
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 OTHER_DETAILS: NON-GLYCOSYLATED                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;                            
SOURCE  13 ORGANISM_TAXID: 37296;                                               
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_TYPE: BACULOVIRUS;                          
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    CYTOKINE/RECEPTOR COMPLEX, GP130, VIRAL IL-6, CRYSTAL                 
KEYWDS   2 STRUCTURE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.CHOW,X.HE,A.L.SNOW,S.ROSE-JOHN,K.C.GARCIA                           
REVDAT   2   24-FEB-09 1I1R    1       VERSN                                    
REVDAT   1   28-MAR-01 1I1R    0                                                
JRNL        AUTH   D.CHOW,X.HE,A.L.SNOW,S.ROSE-JOHN,K.C.GARCIA                  
JRNL        TITL   STRUCTURE OF AN EXTRACELLULAR GP130 CYTOKINE                 
JRNL        TITL 2 RECEPTOR SIGNALING COMPLEX.                                  
JRNL        REF    SCIENCE                       V. 291  2150 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11251120                                                     
JRNL        DOI    10.1126/SCIENCE.1058308                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 34376                          
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                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3425                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 353                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3783                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 370                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 13.53000                                             
REMARK   3    B13 (A**2) : -13.12000                                            
REMARK   3    B23 (A**2) : -5.74000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: WILSON B VALUE 50.2                       
REMARK   4                                                                      
REMARK   4 1I1R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012795.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34376                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: HUMAN INTERLEUKIN-6 1ALU, GP130 D2D3 DOMAINS         
REMARK 200  1BQU                                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 2000, SODIUM CITRATE, PH 6.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
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       51.50000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.65500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.50000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.65500            
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC                             
REMARK 300 ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S).                        
REMARK 300 SEE REMARK 350 FOR INFORMATION ON                                    
REMARK 300 GENERATING THE BIOLOGICAL MOLECULE(S).                               
REMARK 300 THE BIOLOGICAL ASSEMBLY IS A TETRAMER,                               
REMARK 300 OF WHICH HALF (ONE VIL-6, ONE GP130) IS IN                           
REMARK 300 THE ASYMMETRIC UNIT.  THE DYAD-AXIS OF THE                           
REMARK 300 TETRAMER IS THE C2 CRYSTALLOGRAPHIC AXIS.                            
REMARK 300 NOTE:  COORDINATES FOR THE ENTIRE TETRAMER                           
REMARK 300 CAN BE OBTAINED DIRECTLY FROM THE AUTHORS                            
REMARK 300 (KCGARCIA@STANFORD.EDU).                                             
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       74.19668            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       71.18338            
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     GLU A     1                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     VAL B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     PRO B   176                                                      
REMARK 465     ASP B   177                                                      
REMARK 465     VAL B   178                                                      
REMARK 465     HIS B   179                                                      
REMARK 465     ASP B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   452     O    HOH A   468     2657     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLY A 126   N   -  CA  -  C   ANGL. DEV. = -15.6 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   3       51.86     72.48                                   
REMARK 500    SER A  13       79.38   -154.73                                   
REMARK 500    LYS A  54      -33.04    -37.27                                   
REMARK 500    HIS A 145      134.07   -171.28                                   
REMARK 500    THR A 156       77.94   -111.72                                   
REMARK 500    GLU A 213       35.32    -88.15                                   
REMARK 500    ILE A 227       -5.59    -57.22                                   
REMARK 500    PHE A 270       44.99     36.12                                   
REMARK 500    LEU B  41       88.60   -164.91                                   
REMARK 500    HIS B  48       24.71   -147.59                                   
REMARK 500    ASN B  66      113.69    178.08                                   
REMARK 500    THR B  68      -76.26    -37.75                                   
REMARK 500    THR B 121     -164.68   -120.76                                   
REMARK 500    PRO B 128      172.05    -43.88                                   
REMARK 500    TYR B 143     -148.55     58.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1I1R A    1   303  UNP    P40189   IL6RB_HUMAN     23    325             
DBREF  1I1R B    1   181  UNP    Q98823   Q98823_HHV8     24    204             
SEQRES   1 A  303  GLU LEU LEU ASP PRO CYS GLY TYR ILE SER PRO GLU SER          
SEQRES   2 A  303  PRO VAL VAL GLN LEU HIS SER ASN PHE THR ALA VAL CYS          
SEQRES   3 A  303  VAL LEU LYS GLU LYS CYS MET ASP TYR PHE HIS VAL ASN          
SEQRES   4 A  303  ALA ASN TYR ILE VAL TRP LYS THR ASN HIS PHE THR ILE          
SEQRES   5 A  303  PRO LYS GLU GLN TYR THR ILE ILE ASN ARG THR ALA SER          
SEQRES   6 A  303  SER VAL THR PHE THR ASP ILE ALA SER LEU ASN ILE GLN          
SEQRES   7 A  303  LEU THR CYS ASN ILE LEU THR PHE GLY GLN LEU GLU GLN          
SEQRES   8 A  303  ASN VAL TYR GLY ILE THR ILE ILE SER GLY LEU PRO PRO          
SEQRES   9 A  303  GLU LYS PRO LYS ASN LEU SER CYS ILE VAL ASN GLU GLY          
SEQRES  10 A  303  LYS LYS MET ARG CYS GLU TRP ASP GLY GLY ARG GLU THR          
SEQRES  11 A  303  HIS LEU GLU THR ASN PHE THR LEU LYS SER GLU TRP ALA          
SEQRES  12 A  303  THR HIS LYS PHE ALA ASP CYS LYS ALA LYS ARG ASP THR          
SEQRES  13 A  303  PRO THR SER CYS THR VAL ASP TYR SER THR VAL TYR PHE          
SEQRES  14 A  303  VAL ASN ILE GLU VAL TRP VAL GLU ALA GLU ASN ALA LEU          
SEQRES  15 A  303  GLY LYS VAL THR SER ASP HIS ILE ASN PHE ASP PRO VAL          
SEQRES  16 A  303  TYR LYS VAL LYS PRO ASN PRO PRO HIS ASN LEU SER VAL          
SEQRES  17 A  303  ILE ASN SER GLU GLU LEU SER SER ILE LEU LYS LEU THR          
SEQRES  18 A  303  TRP THR ASN PRO SER ILE LYS SER VAL ILE ILE LEU LYS          
SEQRES  19 A  303  TYR ASN ILE GLN TYR ARG THR LYS ASP ALA SER THR TRP          
SEQRES  20 A  303  SER GLN ILE PRO PRO GLU ASP THR ALA SER THR ARG SER          
SEQRES  21 A  303  SER PHE THR VAL GLN ASP LEU LYS PRO PHE THR GLU TYR          
SEQRES  22 A  303  VAL PHE ARG ILE ARG CYS MET LYS GLU ASP GLY LYS GLY          
SEQRES  23 A  303  TYR TRP SER ASP TRP SER GLU GLU ALA SER GLY ILE THR          
SEQRES  24 A  303  TYR GLU ASP ARG                                              
SEQRES   1 B  181  LEU PRO ASP ALA PRO GLU PHE GLU LYS ASP LEU LEU ILE          
SEQRES   2 B  181  GLN ARG LEU ASN TRP MET LEU TRP VAL ILE ASP GLU CYS          
SEQRES   3 B  181  PHE ARG ASP LEU CYS TYR ARG THR GLY ILE CYS LYS GLY          
SEQRES   4 B  181  ILE LEU GLU PRO ALA ALA ILE PHE HIS LEU LYS LEU PRO          
SEQRES   5 B  181  ALA ILE ASN ASP THR ASP HIS CYS GLY LEU ILE GLY PHE          
SEQRES   6 B  181  ASN GLU THR SER CYS LEU LYS LYS LEU ALA ASP GLY PHE          
SEQRES   7 B  181  PHE GLU PHE GLU VAL LEU PHE LYS PHE LEU THR THR GLU          
SEQRES   8 B  181  PHE GLY LYS SER VAL ILE ASN VAL ASP VAL MET GLU LEU          
SEQRES   9 B  181  LEU THR LYS THR LEU GLY TRP ASP ILE GLN GLU GLU LEU          
SEQRES  10 B  181  ASN LYS LEU THR LYS THR HIS TYR SER PRO PRO LYS PHE          
SEQRES  11 B  181  ASP ARG GLY LEU LEU GLY ARG LEU GLN GLY LEU LYS TYR          
SEQRES  12 B  181  TRP VAL ARG HIS PHE ALA SER PHE TYR VAL LEU SER ALA          
SEQRES  13 B  181  MET GLU LYS PHE ALA GLY GLN ALA VAL ARG VAL LEU ASP          
SEQRES  14 B  181  SER ILE PRO ASP VAL THR PRO ASP VAL HIS ASP LYS              
FORMUL   3  HOH   *370(H2 O)                                                    
HELIX    1   1 LYS A   29  HIS A   37  1                                   9    
HELIX    2   2 ASN A   39  ASN A   41  5                                   3    
HELIX    3   3 PRO A   53  TYR A   57  5                                   5    
HELIX    4   4 ASP A  193  TYR A  196  5                                   4    
HELIX    5   5 PRO A  225  VAL A  230  5                                   6    
HELIX    6   6 PRO A  251  ALA A  256  5                                   6    
HELIX    7   7 GLU B    8  GLY B   35  1                                  28    
HELIX    8   8 ASN B   66  GLY B   93  1                                  28    
HELIX    9   9 ASN B   98  ASP B  100  5                                   3    
HELIX   10  10 VAL B  101  THR B  121  1                                  21    
HELIX   11  11 ASP B  131  GLN B  139  1                                   9    
HELIX   12  12 TRP B  144  SER B  170  1                                  27    
SHEET    1   A 4 GLY A   7  SER A  10  0                                        
SHEET    2   A 4 PHE A  22  LEU A  28 -1  N  VAL A  25   O  SER A  10           
SHEET    3   A 4 ALA A  64  PHE A  69 -1  O  SER A  65   N  CYS A  26           
SHEET    4   A 4 THR A  58  ASN A  61 -1  N  THR A  58   O  SER A  66           
SHEET    1   B 5 PHE A  50  THR A  51  0                                        
SHEET    2   B 5 ILE A  43  THR A  47 -1  O  THR A  47   N  PHE A  50           
SHEET    3   B 5 ASN A  76  THR A  85 -1  N  THR A  80   O  LYS A  46           
SHEET    4   B 5 LEU A  89  GLY A 101 -1  N  LEU A  89   O  THR A  85           
SHEET    5   B 5 VAL A  15  GLN A  17  1  N  VAL A  16   O  ILE A  99           
SHEET    1   C 4 VAL A 198  LYS A 199  0                                        
SHEET    2   C 4 LYS A 108  ASN A 115  1  O  VAL A 114   N  LYS A 199           
SHEET    3   C 4 ARG A 121  ASP A 125 -1  O  ARG A 121   N  ILE A 113           
SHEET    4   C 4 SER A 159  THR A 161 -1  O  CYS A 160   N  CYS A 122           
SHEET    1   D 8 HIS A 145  LYS A 146  0                                        
SHEET    2   D 8 ASN A 135  TRP A 142 -1  N  TRP A 142   O  HIS A 145           
SHEET    3   D 8 CYS A 150  LYS A 151 -1  O  CYS A 150   N  LEU A 138           
SHEET    4   D 8 ASN A 135  TRP A 142 -1  N  LEU A 138   O  CYS A 150           
SHEET    5   D 8 ILE A 172  ASN A 180 -1  N  GLU A 173   O  GLU A 141           
SHEET    6   D 8 GLY A 183  THR A 186 -1  N  GLY A 183   O  ASN A 180           
SHEET    7   D 8 ILE A 172  ASN A 180 -1  N  ALA A 178   O  VAL A 185           
SHEET    8   D 8 ILE A 190  PHE A 192 -1  N  ILE A 190   O  VAL A 174           
SHEET    1   E 3 HIS A 204  ILE A 209  0                                        
SHEET    2   E 3 LEU A 218  THR A 223 -1  O  LYS A 219   N  ILE A 209           
SHEET    3   E 3 SER A 261  VAL A 264 -1  O  PHE A 262   N  LEU A 220           
SHEET    1   F 4 SER A 248  GLN A 249  0                                        
SHEET    2   F 4 LEU A 233  THR A 241 -1  O  TYR A 239   N  SER A 248           
SHEET    3   F 4 GLU A 272  LYS A 281 -1  N  VAL A 274   O  ARG A 240           
SHEET    4   F 4 ALA A 295  ILE A 298 -1  O  ALA A 295   N  PHE A 275           
SSBOND   1 CYS A    6    CYS A   32                          1555   1555  2.03  
SSBOND   2 CYS A   26    CYS A   81                          1555   1555  2.03  
SSBOND   3 CYS A  112    CYS A  122                          1555   1555  2.04  
SSBOND   4 CYS A  150    CYS A  160                          1555   1555  2.04  
SSBOND   5 CYS B   31    CYS B   37                          1555   1555  2.03  
SSBOND   6 CYS B   60    CYS B   70                          1555   1555  2.02  
CISPEP   1 SER A   10    PRO A   11          0        -0.24                     
CRYST1  103.000  123.310   76.790  90.00 112.03  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      0.009709  0.000000  0.003928        0.00000                         
SCALE2      0.000000  0.008110  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014048        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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