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Database: PDB
Entry: 1BQU
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Original site: 1BQU 
HEADER    SIGNALING PROTEIN                       18-AUG-98   1BQU              
TITLE     CYTOKYNE-BINDING REGION OF GP130                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GP130);                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CYTOKINE-BINDING REGION DOMAINS;                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: INTERLEUKIN-6 RECEPTOR BETA FRAGMENT INTERLEUKIN 6    
COMPND   7 SIGNAL TRANSDUCER MEMBRANE GLYCOPROTEIN 130 GP130 ONCOSTATIN M       
COMPND   8 RECEPTOR                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL6ST;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HW1110;                                    
SOURCE   9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMALP2                                    
KEYWDS    CYTOKINE RECEPTOR, GLYCOPROTEIN 130, GP130, INTERLEUKINE 6 RECEPTOR   
KEYWDS   2 BETA SUBUNIT, SIGNALING PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BRAVO,D.STAUNTON,J.K.HEATH,E.Y.JONES                                
REVDAT   4   13-JUL-11 1BQU    1       VERSN                                    
REVDAT   3   24-FEB-09 1BQU    1       VERSN                                    
REVDAT   2   22-DEC-99 1BQU    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   26-AUG-98 1BQU    0                                                
JRNL        AUTH   J.BRAVO,D.STAUNTON,J.K.HEATH,E.Y.JONES                       
JRNL        TITL   CRYSTAL STRUCTURE OF A CYTOKINE-BINDING REGION OF GP130.     
JRNL        REF    EMBO J.                       V.  17  1665 1998              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   9501088                                                      
JRNL        DOI    10.1093/EMBOJ/17.6.1665                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 44627                          
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) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3380                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6499                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 554                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3358                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.60                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
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) : 1.560 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.420 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.950 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.310 ; 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  : GOL.PAR                                        
REMARK   3  PARAMETER FILE  4  : SO4.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : GOL.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : SO4.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1BQU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008108.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48189                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.20600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-2.1M AMMONIUM SULFATE, 0.1M TRIS     
REMARK 280  PH 8.0                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       60.96650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.96650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       42.24000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.14750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       42.24000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.14750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.96650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       42.24000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.14750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       60.96650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       42.24000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.14750            
REMARK 290   SMTRY3   8  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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 TER                                                                  
REMARK 400  ALA: RESIDUES 207 - 214 CORRESPOND TO A 3 ALA LINKER AND A          
REMARK 400  C-MYC TAG                                                           
REMARK 400  ALA: RESIDUES 207 - 215 CORRESPOND TO A 3 ALA LINKER AND A          
REMARK 400  C-MYC TAG                                                           
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     PRO A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     GLU A   117                                                      
REMARK 465     TRP A   215                                                      
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     ARG A  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  59    CG   OD1  OD2                                       
REMARK 470     PRO A 208    CG   CD                                             
REMARK 470     SER A 209    OG                                                  
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     PRO A 212    CG   CD                                             
REMARK 470     SER A 213    OG                                                  
REMARK 470     PHE A 214    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 208    CG   CD                                             
REMARK 470     SER B 209    OG                                                  
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     PRO B 212    CG   CD                                             
REMARK 470     SER B 213    OG                                                  
REMARK 470     PHE B 214    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP B 215    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 215    CZ3  CH2                                            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  123   CB   CG   CD   CE   NZ                              
REMARK 480     GLU B   37   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B   55   CB   CG   CD   CE   NZ                              
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    GLU A  45      145.40   -175.49                                   
REMARK 500    ASN A 114       68.51   -165.08                                   
REMARK 500    LYS A 146       -6.90    -50.77                                   
REMARK 500    HIS B  49      145.89   -175.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505                 
DBREF  1BQU A    1   215  UNP    P40189   IL6RB_HUMAN    119    333             
DBREF  1BQU B    1   215  UNP    P40189   IL6RB_HUMAN    119    333             
SEQADV 1BQU PRO A    1  UNP  P40189    THR   119 SEQUENCE CONFLICT              
SEQADV 1BQU GLY A    2  UNP  P40189    ILE   120 SEQUENCE CONFLICT              
SEQADV 1BQU SER A    3  UNP  P40189    ILE   121 SEQUENCE CONFLICT              
SEQADV 1BQU GLU A  211  UNP  P40189    ALA   329 SEQUENCE CONFLICT              
SEQADV 1BQU PRO B    1  UNP  P40189    THR   119 SEQUENCE CONFLICT              
SEQADV 1BQU GLY B    2  UNP  P40189    ILE   120 SEQUENCE CONFLICT              
SEQADV 1BQU SER B    3  UNP  P40189    ILE   121 SEQUENCE CONFLICT              
SEQADV 1BQU GLU B  211  UNP  P40189    ALA   329 SEQUENCE CONFLICT              
SEQRES   1 A  215  PRO GLY SER SER GLY LEU PRO PRO GLU LYS PRO LYS ASN          
SEQRES   2 A  215  LEU SER CYS ILE VAL ASN GLU GLY LYS LYS MET ARG CYS          
SEQRES   3 A  215  GLU TRP ASP GLY GLY ARG GLU THR HIS LEU GLU THR ASN          
SEQRES   4 A  215  PHE THR LEU LYS SER GLU TRP ALA THR HIS LYS PHE ALA          
SEQRES   5 A  215  ASP CYS LYS ALA LYS ARG ASP THR PRO THR SER CYS THR          
SEQRES   6 A  215  VAL ASP TYR SER THR VAL TYR PHE VAL ASN ILE GLU VAL          
SEQRES   7 A  215  TRP VAL GLU ALA GLU ASN ALA LEU GLY LYS VAL THR SER          
SEQRES   8 A  215  ASP HIS ILE ASN PHE ASP PRO VAL TYR LYS VAL LYS PRO          
SEQRES   9 A  215  ASN PRO PRO HIS ASN LEU SER VAL ILE ASN SER GLU GLU          
SEQRES  10 A  215  LEU SER SER ILE LEU LYS LEU THR TRP THR ASN PRO SER          
SEQRES  11 A  215  ILE LYS SER VAL ILE ILE LEU LYS TYR ASN ILE GLN TYR          
SEQRES  12 A  215  ARG THR LYS ASP ALA SER THR TRP SER GLN ILE PRO PRO          
SEQRES  13 A  215  GLU ASP THR ALA SER THR ARG SER SER PHE THR VAL GLN          
SEQRES  14 A  215  ASP LEU LYS PRO PHE THR GLU TYR VAL PHE ARG ILE ARG          
SEQRES  15 A  215  CYS MET LYS GLU ASP GLY LYS GLY TYR TRP SER ASP TRP          
SEQRES  16 A  215  SER GLU GLU ALA SER GLY ILE THR TYR GLU ASP ARG PRO          
SEQRES  17 A  215  SER LYS GLU PRO SER PHE TRP                                  
SEQRES   1 B  215  PRO GLY SER SER GLY LEU PRO PRO GLU LYS PRO LYS ASN          
SEQRES   2 B  215  LEU SER CYS ILE VAL ASN GLU GLY LYS LYS MET ARG CYS          
SEQRES   3 B  215  GLU TRP ASP GLY GLY ARG GLU THR HIS LEU GLU THR ASN          
SEQRES   4 B  215  PHE THR LEU LYS SER GLU TRP ALA THR HIS LYS PHE ALA          
SEQRES   5 B  215  ASP CYS LYS ALA LYS ARG ASP THR PRO THR SER CYS THR          
SEQRES   6 B  215  VAL ASP TYR SER THR VAL TYR PHE VAL ASN ILE GLU VAL          
SEQRES   7 B  215  TRP VAL GLU ALA GLU ASN ALA LEU GLY LYS VAL THR SER          
SEQRES   8 B  215  ASP HIS ILE ASN PHE ASP PRO VAL TYR LYS VAL LYS PRO          
SEQRES   9 B  215  ASN PRO PRO HIS ASN LEU SER VAL ILE ASN SER GLU GLU          
SEQRES  10 B  215  LEU SER SER ILE LEU LYS LEU THR TRP THR ASN PRO SER          
SEQRES  11 B  215  ILE LYS SER VAL ILE ILE LEU LYS TYR ASN ILE GLN TYR          
SEQRES  12 B  215  ARG THR LYS ASP ALA SER THR TRP SER GLN ILE PRO PRO          
SEQRES  13 B  215  GLU ASP THR ALA SER THR ARG SER SER PHE THR VAL GLN          
SEQRES  14 B  215  ASP LEU LYS PRO PHE THR GLU TYR VAL PHE ARG ILE ARG          
SEQRES  15 B  215  CYS MET LYS GLU ASP GLY LYS GLY TYR TRP SER ASP TRP          
SEQRES  16 B  215  SER GLU GLU ALA SER GLY ILE THR TYR GLU ASP ARG PRO          
SEQRES  17 B  215  SER LYS GLU PRO SER PHE TRP                                  
HET    SO4  B 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    GOL  B 501       6                                                       
HET    GOL  B 502       6                                                       
HET    GOL  B 503       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  A 505       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  GOL    5(C3 H8 O3)                                                  
FORMUL  14  HOH   *277(H2 O)                                                    
HELIX    1   1 PRO A   98  TYR A  100  5                                   3    
HELIX    2   2 SER A  130  SER A  133  5                                   4    
HELIX    3   3 PRO A  156  THR A  159  5                                   4    
HELIX    4   4 ARG A  207  PRO A  212  1                                   6    
HELIX    5   5 PRO B   98  TYR B  100  5                                   3    
HELIX    6   6 SER B  130  SER B  133  5                                   4    
HELIX    7   7 PRO B  156  ASP B  158  5                                   3    
HELIX    8   8 ARG B  207  SER B  213  1                                   7    
SHEET    1   A 3 SER A  15  ILE A  17  0                                        
SHEET    2   A 3 ARG A  25  GLU A  27 -1  N  GLU A  27   O  SER A  15           
SHEET    3   A 3 SER A  63  THR A  65 -1  N  CYS A  64   O  CYS A  26           
SHEET    1   B 3 ASN A  39  GLU A  45  0                                        
SHEET    2   B 3 ASN A  75  GLU A  83 -1  N  GLU A  83   O  ASN A  39           
SHEET    3   B 3 ILE A  94  ASP A  97 -1  N  PHE A  96   O  ILE A  76           
SHEET    1   C 2 GLU A  81  ASN A  84  0                                        
SHEET    2   C 2 GLY A  87  THR A  90 -1  N  VAL A  89   O  ALA A  82           
SHEET    1   D 3 SER A 111  ILE A 113  0                                        
SHEET    2   D 3 LEU A 122  THR A 125 -1  N  THR A 125   O  SER A 111           
SHEET    3   D 3 SER A 165  VAL A 168 -1  N  VAL A 168   O  LEU A 122           
SHEET    1   E 3 LEU A 137  THR A 145  0                                        
SHEET    2   E 3 THR A 175  LYS A 185 -1  N  MET A 184   O  LYS A 138           
SHEET    3   E 3 ALA A 199  THR A 203 -1  N  THR A 203   O  THR A 175           
SHEET    1   F 3 SER B  15  ILE B  17  0                                        
SHEET    2   F 3 ARG B  25  GLU B  27 -1  N  GLU B  27   O  SER B  15           
SHEET    3   F 3 SER B  63  THR B  65 -1  N  CYS B  64   O  CYS B  26           
SHEET    1   G 3 ASN B  39  TRP B  46  0                                        
SHEET    2   G 3 ASN B  75  GLU B  83 -1  N  GLU B  83   O  ASN B  39           
SHEET    3   G 3 ILE B  94  ASP B  97 -1  N  PHE B  96   O  ILE B  76           
SHEET    1   H 2 GLU B  81  ASN B  84  0                                        
SHEET    2   H 2 GLY B  87  THR B  90 -1  N  VAL B  89   O  ALA B  82           
SHEET    1   I 3 SER B 111  ILE B 113  0                                        
SHEET    2   I 3 LEU B 122  THR B 125 -1  N  THR B 125   O  SER B 111           
SHEET    3   I 3 SER B 165  VAL B 168 -1  N  VAL B 168   O  LEU B 122           
SHEET    1   J 3 LEU B 137  THR B 145  0                                        
SHEET    2   J 3 GLU B 176  LYS B 185 -1  N  MET B 184   O  LYS B 138           
SHEET    3   J 3 ALA B 199  ILE B 202 -1  N  GLY B 201   O  TYR B 177           
SSBOND   1 CYS A   16    CYS A   26                          1555   1555  2.05  
SSBOND   2 CYS A   54    CYS A   64                          1555   1555  2.04  
SSBOND   3 CYS B   16    CYS B   26                          1555   1555  2.03  
SSBOND   4 CYS B   54    CYS B   64                          1555   1555  2.04  
SITE     1 AC1  5 THR B 127  ASN B 128  LYS B 132  SER B 164                    
SITE     2 AC1  5 HOH B 600                                                     
SITE     1 AC2  4 THR A 127  ASN A 128  LYS A 132  SER A 164                    
SITE     1 AC3  4 LYS A 132  HOH A 593  HOH A 635  ARG B 182                    
SITE     1 AC4  3 ARG A 182  TRP A 192  HOH B 524                               
SITE     1 AC5  3 HOH A 593  ARG B 180  HOH B 624                               
SITE     1 AC6  4 ARG B 163  PHE B 166  THR B 167  HOH B 622                    
SITE     1 AC7  6 GLU B  20  ASN B 105  PRO B 129  SER B 130                    
SITE     2 AC7  6 HOH B 509  HOH B 557                                          
SITE     1 AC8  5 SER B  15  CYS B  16  ILE B  17  ARG B  25                    
SITE     2 AC8  5 TYR B 191                                                     
SITE     1 AC9  4 LYS A 189  LYS B  23  ASP B  67  SER B  69                    
SITE     1 BC1  5 LYS A  57  THR A  60  SER A  63  CYS A  64                    
SITE     2 BC1  5 THR A  65                                                     
SITE     1 BC2  7 ASN A 105  PRO A 106  HIS A 108  ASN A 128                    
SITE     2 BC2  7 PRO A 129  SER A 130  HOH A 595                               
CRYST1   84.480  132.295  121.933  90.00  90.00  90.00 C 2 2 21     16          
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      0.011837  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007559  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008201        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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