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Database: PDB
Entry: 1PVH
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Original site: 1PVH 
HEADER    SIGNALING PROTEIN/CYTOKINE              27-JUN-03   1PVH              
TITLE     CRYSTAL STRUCTURE OF LEUKEMIA INHIBITORY FACTOR IN COMPLEX            
TITLE    2 WITH GP130                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-6 RECEPTOR BETA CHAIN;                         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: DOMAINS D2 AND D3;                                         
COMPND   5 SYNONYM: IL-6R-BETA, INTERLEUKIN 6 SIGNAL TRANSDUCER,                
COMPND   6 MEMBRANE GLYCOPROTEIN 130, GP130, ONCOSTATIN M RECEPTOR,             
COMPND   7 CDW130, CD130 ANTIGEN;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LEUKEMIA INHIBITORY FACTOR;                                
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 SYNONYM: LIF, DIFFERENTIATION-STIMULATING FACTOR, D FACTOR,          
COMPND  13 MELANOMA-DERIVED LPL INHIBITOR, MLPLI;                               
COMPND  14 ENGINEERED: YES                                                      
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: LIF OR HILDA;                                                  
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CYTOKINE, RECEPTOR, SIGNALING, BETA SHEET, FOUR HELIX                 
KEYWDS   2 BUNDLE, SIGNALING PROTEIN/CYTOKINE COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.BOULANGER,A.J.BANKOVICH,T.KORTEMME,D.BAKER,K.C.GARCIA             
REVDAT   3   24-FEB-09 1PVH    1       VERSN                                    
REVDAT   2   30-NOV-04 1PVH    1       DBREF                                    
REVDAT   1   14-OCT-03 1PVH    0                                                
JRNL        AUTH   M.J.BOULANGER,A.J.BANKOVICH,T.KORTEMME,D.BAKER,              
JRNL        AUTH 2 K.C.GARCIA                                                   
JRNL        TITL   CONVERGENT MECHANISMS FOR RECOGNITION OF DIVERGENT           
JRNL        TITL 2 CYTOKINES BY THE SHARED SIGNALING RECEPTOR GP130.            
JRNL        REF    MOL.CELL                      V.  12   577 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   14527405                                                     
JRNL        DOI    10.1016/S1097-2765(03)00365-4                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.86                          
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)   (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 32566                          
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) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2616                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4257                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE                    : 0.4170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 379                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5832                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 192                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -20.48000                                            
REMARK   3    B22 (A**2) : 20.61000                                             
REMARK   3    B33 (A**2) : -0.13000                                             
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) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.49                            
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) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.58                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.93                            
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) : 1.250 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.180 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.610 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.470 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 28.86                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PVH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019604.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32573                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
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) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: LIF - PDB ENTRY 1LKI, GP130 - PDB ENTRY 1I1R         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM IODIDE, IMIDAZOLE,      
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.85500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.21500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.21500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.85500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 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     ASP B 149    CB   CG   OD1  OD2                                  
REMARK 470     THR B 150    CB   OG1  CG2                                       
REMARK 470     SER B 151    CB   OG                                             
REMARK 470     LYS B 153    CB   CG   CD   CE   NZ                              
REMARK 470     ASP B 154    CB   CG   OD1  OD2                                  
REMARK 470     ASP D 149    CB   CG   OD1  OD2                                  
REMARK 470     THR D 150    CB   OG1  CG2                                       
REMARK 470     SER D 151    CB   OG                                             
REMARK 470     LYS D 153    CB   CG   CD   CE   NZ                              
REMARK 470     ASP D 154    CB   CG   OD1  OD2                                  
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 B   58   CG    CD    CE    NZ                                
REMARK 480     LYS D   58   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    ASN A 109       33.44     71.93                                   
REMARK 500    HIS A 131       -2.96     73.11                                   
REMARK 500    ALA A 181      -34.89    -34.90                                   
REMARK 500    PRO A 200      173.08    -55.25                                   
REMARK 500    SER A 211       55.13    -59.53                                   
REMARK 500    GLU A 212       -7.86   -145.50                                   
REMARK 500    GLU A 213       18.28     59.60                                   
REMARK 500    SER A 216       35.74    -61.53                                   
REMARK 500    ILE A 227       -2.92    -58.86                                   
REMARK 500    HIS B  16      167.25    175.68                                   
REMARK 500    CYS B  60       40.09   -141.49                                   
REMARK 500    VAL B  64       40.71    -70.85                                   
REMARK 500    THR B  65      -98.43    -31.42                                   
REMARK 500    HIS B 138       50.59     39.63                                   
REMARK 500    HIS B 141      168.24    175.88                                   
REMARK 500    THR B 145      105.63   -169.92                                   
REMARK 500    PRO B 148       42.22    -74.83                                   
REMARK 500    ASP B 149      -69.93    -19.36                                   
REMARK 500    THR B 150      167.93     45.55                                   
REMARK 500    LYS B 153      132.49    156.67                                   
REMARK 500    HIS C 131       -1.27     72.33                                   
REMARK 500    ALA C 181      -30.24    -39.95                                   
REMARK 500    PRO C 194      -15.62    -47.48                                   
REMARK 500    PRO C 200      170.02    -58.21                                   
REMARK 500    SER C 211       54.72    -58.47                                   
REMARK 500    GLU C 212       -7.45   -145.64                                   
REMARK 500    GLU C 213       19.44     59.11                                   
REMARK 500    SER C 216       33.95    -61.18                                   
REMARK 500    ILE C 227       -0.25    -58.31                                   
REMARK 500    TYR C 300     -141.42    -65.13                                   
REMARK 500    ALA D  13       77.42     45.31                                   
REMARK 500    HIS D  16      148.29    169.75                                   
REMARK 500    PRO D  17      124.71    -32.19                                   
REMARK 500    ASN D  55       52.22   -118.11                                   
REMARK 500    VAL D  64       42.87    -69.46                                   
REMARK 500    THR D  65      -97.51    -32.69                                   
REMARK 500    PRO D 106      -18.50    -49.61                                   
REMARK 500    HIS D 138       49.31     39.69                                   
REMARK 500    HIS D 141      167.30    176.95                                   
REMARK 500    THR D 145      105.77   -168.80                                   
REMARK 500    PRO D 148       42.03    -75.91                                   
REMARK 500    ASP D 149      -69.28    -19.38                                   
REMARK 500    THR D 150      166.82     44.57                                   
REMARK 500    LYS D 153      132.48    155.07                                   
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 D  45         0.07    SIDE_CHAIN                              
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 IOD A 302                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 202                 
DBREF  1PVH A  101   301  UNP    P40189   IL6RB_HUMAN    123    323             
DBREF  1PVH B   12   180  UNP    P15018   LIF_HUMAN       34    202             
DBREF  1PVH C  101   301  UNP    P40189   IL6RB_HUMAN    123    323             
DBREF  1PVH D   12   180  UNP    P15018   LIF_HUMAN       34    202             
SEQRES   1 A  201  GLY LEU PRO PRO GLU LYS PRO LYS ASN LEU SER CYS ILE          
SEQRES   2 A  201  VAL ASN GLU GLY LYS LYS MET ARG CYS GLU TRP ASP GLY          
SEQRES   3 A  201  GLY ARG GLU THR HIS LEU GLU THR ASN PHE THR LEU LYS          
SEQRES   4 A  201  SER GLU TRP ALA THR HIS LYS PHE ALA ASP CYS LYS ALA          
SEQRES   5 A  201  LYS ARG ASP THR PRO THR SER CYS THR VAL ASP TYR SER          
SEQRES   6 A  201  THR VAL TYR PHE VAL ASN ILE GLU VAL TRP VAL GLU ALA          
SEQRES   7 A  201  GLU ASN ALA LEU GLY LYS VAL THR SER ASP HIS ILE ASN          
SEQRES   8 A  201  PHE ASP PRO VAL TYR LYS VAL LYS PRO ASN PRO PRO HIS          
SEQRES   9 A  201  ASN LEU SER VAL ILE ASN SER GLU GLU LEU SER SER ILE          
SEQRES  10 A  201  LEU LYS LEU THR TRP THR ASN PRO SER ILE LYS SER VAL          
SEQRES  11 A  201  ILE ILE LEU LYS TYR ASN ILE GLN TYR ARG THR LYS ASP          
SEQRES  12 A  201  ALA SER THR TRP SER GLN ILE PRO PRO GLU ASP THR ALA          
SEQRES  13 A  201  SER THR ARG SER SER PHE THR VAL GLN ASP LEU LYS PRO          
SEQRES  14 A  201  PHE THR GLU TYR VAL PHE ARG ILE ARG CYS MET LYS GLU          
SEQRES  15 A  201  ASP GLY LYS GLY TYR TRP SER ASP TRP SER GLU GLU ALA          
SEQRES  16 A  201  SER GLY ILE THR TYR GLU                                      
SEQRES   1 B  169  CYS ALA ILE ARG HIS PRO CYS HIS ASN ASN LEU MET ASN          
SEQRES   2 B  169  GLN ILE ARG SER GLN LEU ALA GLN LEU ASN GLY SER ALA          
SEQRES   3 B  169  ASN ALA LEU PHE ILE LEU TYR TYR THR ALA GLN GLY GLU          
SEQRES   4 B  169  PRO PHE PRO ASN ASN LEU ASP LYS LEU CYS GLY PRO ASN          
SEQRES   5 B  169  VAL THR ASP PHE PRO PRO PHE HIS ALA ASN GLY THR GLU          
SEQRES   6 B  169  LYS ALA LYS LEU VAL GLU LEU TYR ARG ILE VAL VAL TYR          
SEQRES   7 B  169  LEU GLY THR SER LEU GLY ASN ILE THR ARG ASP GLN LYS          
SEQRES   8 B  169  ILE LEU ASN PRO SER ALA LEU SER LEU HIS SER LYS LEU          
SEQRES   9 B  169  ASN ALA THR ALA ASP ILE LEU ARG GLY LEU LEU SER ASN          
SEQRES  10 B  169  VAL LEU CYS ARG LEU CYS SER LYS TYR HIS VAL GLY HIS          
SEQRES  11 B  169  VAL ASP VAL THR TYR GLY PRO ASP THR SER GLY LYS ASP          
SEQRES  12 B  169  VAL PHE GLN LYS LYS LYS LEU GLY CYS GLN LEU LEU GLY          
SEQRES  13 B  169  LYS TYR LYS GLN ILE ILE ALA VAL LEU ALA GLN ALA PHE          
SEQRES   1 C  201  GLY LEU PRO PRO GLU LYS PRO LYS ASN LEU SER CYS ILE          
SEQRES   2 C  201  VAL ASN GLU GLY LYS LYS MET ARG CYS GLU TRP ASP GLY          
SEQRES   3 C  201  GLY ARG GLU THR HIS LEU GLU THR ASN PHE THR LEU LYS          
SEQRES   4 C  201  SER GLU TRP ALA THR HIS LYS PHE ALA ASP CYS LYS ALA          
SEQRES   5 C  201  LYS ARG ASP THR PRO THR SER CYS THR VAL ASP TYR SER          
SEQRES   6 C  201  THR VAL TYR PHE VAL ASN ILE GLU VAL TRP VAL GLU ALA          
SEQRES   7 C  201  GLU ASN ALA LEU GLY LYS VAL THR SER ASP HIS ILE ASN          
SEQRES   8 C  201  PHE ASP PRO VAL TYR LYS VAL LYS PRO ASN PRO PRO HIS          
SEQRES   9 C  201  ASN LEU SER VAL ILE ASN SER GLU GLU LEU SER SER ILE          
SEQRES  10 C  201  LEU LYS LEU THR TRP THR ASN PRO SER ILE LYS SER VAL          
SEQRES  11 C  201  ILE ILE LEU LYS TYR ASN ILE GLN TYR ARG THR LYS ASP          
SEQRES  12 C  201  ALA SER THR TRP SER GLN ILE PRO PRO GLU ASP THR ALA          
SEQRES  13 C  201  SER THR ARG SER SER PHE THR VAL GLN ASP LEU LYS PRO          
SEQRES  14 C  201  PHE THR GLU TYR VAL PHE ARG ILE ARG CYS MET LYS GLU          
SEQRES  15 C  201  ASP GLY LYS GLY TYR TRP SER ASP TRP SER GLU GLU ALA          
SEQRES  16 C  201  SER GLY ILE THR TYR GLU                                      
SEQRES   1 D  169  CYS ALA ILE ARG HIS PRO CYS HIS ASN ASN LEU MET ASN          
SEQRES   2 D  169  GLN ILE ARG SER GLN LEU ALA GLN LEU ASN GLY SER ALA          
SEQRES   3 D  169  ASN ALA LEU PHE ILE LEU TYR TYR THR ALA GLN GLY GLU          
SEQRES   4 D  169  PRO PHE PRO ASN ASN LEU ASP LYS LEU CYS GLY PRO ASN          
SEQRES   5 D  169  VAL THR ASP PHE PRO PRO PHE HIS ALA ASN GLY THR GLU          
SEQRES   6 D  169  LYS ALA LYS LEU VAL GLU LEU TYR ARG ILE VAL VAL TYR          
SEQRES   7 D  169  LEU GLY THR SER LEU GLY ASN ILE THR ARG ASP GLN LYS          
SEQRES   8 D  169  ILE LEU ASN PRO SER ALA LEU SER LEU HIS SER LYS LEU          
SEQRES   9 D  169  ASN ALA THR ALA ASP ILE LEU ARG GLY LEU LEU SER ASN          
SEQRES  10 D  169  VAL LEU CYS ARG LEU CYS SER LYS TYR HIS VAL GLY HIS          
SEQRES  11 D  169  VAL ASP VAL THR TYR GLY PRO ASP THR SER GLY LYS ASP          
SEQRES  12 D  169  VAL PHE GLN LYS LYS LYS LEU GLY CYS GLN LEU LEU GLY          
SEQRES  13 D  169  LYS TYR LYS GLN ILE ILE ALA VAL LEU ALA GLN ALA PHE          
HET    IOD  A 302       1                                                       
HET    IOD  D 202       1                                                       
HETNAM     IOD IODIDE ION                                                       
FORMUL   5  IOD    2(I 1-)                                                      
FORMUL   7  HOH   *192(H2 O)                                                    
HELIX    1   1 ASP A  193  TYR A  196  5                                   4    
HELIX    2   2 PRO A  225  VAL A  230  5                                   6    
HELIX    3   3 PRO A  251  ALA A  256  5                                   6    
HELIX    4   4 ASN B   21  GLY B   49  1                                  29    
HELIX    5   5 ASN B   55  CYS B   60  1                                   6    
HELIX    6   6 THR B   75  ASN B  105  1                                  31    
HELIX    7   7 ALA B  108  LYS B  136  1                                  29    
HELIX    8   8 ASP B  154  GLN B  178  1                                  25    
HELIX    9   9 ASP C  193  TYR C  196  5                                   4    
HELIX   10  10 PRO C  225  VAL C  230  5                                   6    
HELIX   11  11 PRO C  251  ALA C  256  5                                   6    
HELIX   12  12 ASN D   21  GLY D   49  1                                  29    
HELIX   13  13 ASN D   55  CYS D   60  1                                   6    
HELIX   14  14 THR D   75  ASN D  105  1                                  31    
HELIX   15  15 ALA D  108  LYS D  136  1                                  29    
HELIX   16  16 ASP D  154  ALA D  179  1                                  26    
SHEET    1   A 4 SER A 159  THR A 161  0                                        
SHEET    2   A 4 ARG A 121  ASP A 125 -1  N  CYS A 122   O  CYS A 160           
SHEET    3   A 4 LYS A 108  ASN A 115 -1  N  LYS A 108   O  ASP A 125           
SHEET    4   A 4 VAL A 198  LYS A 199  1  O  LYS A 199   N  VAL A 114           
SHEET    1   B 4 CYS A 150  LYS A 151  0                                        
SHEET    2   B 4 ASN A 135  GLU A 141 -1  N  LEU A 138   O  CYS A 150           
SHEET    3   B 4 ILE A 172  ASN A 180 -1  O  GLU A 173   N  GLU A 141           
SHEET    4   B 4 GLY A 183  THR A 186 -1  O  VAL A 185   N  ALA A 178           
SHEET    1   C 4 CYS A 150  LYS A 151  0                                        
SHEET    2   C 4 ASN A 135  GLU A 141 -1  N  LEU A 138   O  CYS A 150           
SHEET    3   C 4 ILE A 172  ASN A 180 -1  O  GLU A 173   N  GLU A 141           
SHEET    4   C 4 ILE A 190  PHE A 192 -1  O  ILE A 190   N  VAL A 174           
SHEET    1   D 3 HIS A 204  ILE A 209  0                                        
SHEET    2   D 3 ILE A 217  THR A 223 -1  O  THR A 223   N  HIS A 204           
SHEET    3   D 3 SER A 261  GLN A 265 -1  O  PHE A 262   N  LEU A 220           
SHEET    1   E 4 SER A 248  GLN A 249  0                                        
SHEET    2   E 4 LEU A 233  THR A 241 -1  N  TYR A 239   O  SER A 248           
SHEET    3   E 4 GLU A 272  LYS A 281 -1  O  ARG A 276   N  GLN A 238           
SHEET    4   E 4 ALA A 295  ILE A 298 -1  O  GLY A 297   N  TYR A 273           
SHEET    1   F 4 SER C 159  THR C 161  0                                        
SHEET    2   F 4 ARG C 121  ASP C 125 -1  N  CYS C 122   O  CYS C 160           
SHEET    3   F 4 LYS C 108  ASN C 115 -1  N  LYS C 108   O  ASP C 125           
SHEET    4   F 4 VAL C 198  LYS C 199  1  O  LYS C 199   N  VAL C 114           
SHEET    1   G 4 HIS C 145  LYS C 146  0                                        
SHEET    2   G 4 ASN C 135  TRP C 142 -1  N  TRP C 142   O  HIS C 145           
SHEET    3   G 4 ILE C 172  ASN C 180 -1  O  GLU C 173   N  GLU C 141           
SHEET    4   G 4 GLY C 183  THR C 186 -1  O  VAL C 185   N  ALA C 178           
SHEET    1   H 4 CYS C 150  LYS C 151  0                                        
SHEET    2   H 4 ASN C 135  TRP C 142 -1  N  LEU C 138   O  CYS C 150           
SHEET    3   H 4 ILE C 172  ASN C 180 -1  O  GLU C 173   N  GLU C 141           
SHEET    4   H 4 ILE C 190  PHE C 192 -1  O  ILE C 190   N  VAL C 174           
SHEET    1   I 3 HIS C 204  ILE C 209  0                                        
SHEET    2   I 3 ILE C 217  THR C 223 -1  O  THR C 223   N  HIS C 204           
SHEET    3   I 3 SER C 261  GLN C 265 -1  O  PHE C 262   N  LEU C 220           
SHEET    1   J 4 SER C 248  GLN C 249  0                                        
SHEET    2   J 4 LEU C 233  THR C 241 -1  N  TYR C 239   O  SER C 248           
SHEET    3   J 4 GLU C 272  LYS C 281 -1  O  ARG C 276   N  GLN C 238           
SHEET    4   J 4 ALA C 295  ILE C 298 -1  O  GLY C 297   N  TYR C 273           
SSBOND   1 CYS A  112    CYS A  122                          1555   1555  2.05  
SSBOND   2 CYS A  150    CYS A  160                          1555   1555  2.05  
SSBOND   3 CYS B   12    CYS B  134                          1555   1555  2.03  
SSBOND   4 CYS B   18    CYS B  131                          1555   1555  2.06  
SSBOND   5 CYS B   60    CYS B  163                          1555   1555  2.05  
SSBOND   6 CYS C  112    CYS C  122                          1555   1555  2.05  
SSBOND   7 CYS C  150    CYS C  160                          1555   1555  2.05  
SSBOND   8 CYS D   12    CYS D  134                          1555   1555  2.04  
SSBOND   9 CYS D   18    CYS D  131                          1555   1555  2.05  
SSBOND  10 CYS D   60    CYS D  163                          1555   1555  2.04  
CISPEP   1 GLU B   50    PRO B   51          0         0.23                     
CISPEP   2 GLU D   50    PRO D   51          0         0.15                     
SITE     1 AC1  1 TRP A 288                                                     
SITE     1 AC2  2 TRP C 288  GLY D 140                                          
CRYST1   79.710   86.700  146.430  90.00  90.00  90.00 P 21 21 21    8          
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      0.012545  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011534  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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