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Database: PDB
Entry: 3L5I
LinkDB: 3L5I
Original site: 3L5I 
HEADER    IMMUNE SYSTEM                           22-DEC-09   3L5I              
TITLE     CRYSTAL STRUCTURE OF FNIII DOMAINS OF HUMAN GP130 (DOMAINS 4-6)       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-6 RECEPTOR SUBUNIT BETA;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 323-612;                                      
COMPND   5 SYNONYM: IL-6R-BETA, INTERLEUKIN-6 SIGNAL TRANSDUCER, MEMBRANE       
COMPND   6 GLYCOPROTEIN 130, GP130, CDW130, ONCOSTATIN-M RECEPTOR SUBUNIT ALPHA;
COMPND   7 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: GP130, IL6ST;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-DUET                                  
KEYWDS    CYTOKINE RECEPTOR, FIBRONECTIN TYPE III DOMAIN, CELL MEMBRANE,        
KEYWDS   2 DISULFIDE BOND, IMMUNOGLOBULIN DOMAIN, MEMBRANE, RECEPTOR, SECRETED, 
KEYWDS   3 TRANSMEMBRANE, IMMUNE SYSTEM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.J.KERSHAW,J.-G.ZHANG,T.P.J.GARRETT,P.E.CZABOTAR                     
REVDAT   3   01-NOV-17 3L5I    1       REMARK                                   
REVDAT   2   05-APR-17 3L5I    1       JRNL   VERSN                             
REVDAT   1   12-MAY-10 3L5I    0                                                
JRNL        AUTH   Y.XU,N.J.KERSHAW,C.S.LUO,P.SOO,M.J.POCOCK,P.E.CZABOTAR,      
JRNL        AUTH 2 D.J.HILTON,N.A.NICOLA,T.P.GARRETT,J.G.ZHANG                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE ENTIRE ECTODOMAIN OF GP130:         
JRNL        TITL 2 INSIGHTS INTO THE MOLECULAR ASSEMBLY OF THE TALL CYTOKINE    
JRNL        TITL 3 RECEPTOR COMPLEXES.                                          
JRNL        REF    J.BIOL.CHEM.                  V. 285 21214 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20489211                                                     
JRNL        DOI    10.1074/JBC.C110.129502                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 27159                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2132                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.7610 -  4.6830    1.00     1811   156  0.1850 0.2050        
REMARK   3     2  4.6830 -  3.7180    1.00     1721   148  0.1680 0.1860        
REMARK   3     3  3.7180 -  3.2490    1.00     1710   147  0.1730 0.2180        
REMARK   3     4  3.2490 -  2.9520    1.00     1676   140  0.1720 0.2190        
REMARK   3     5  2.9520 -  2.7400    1.00     1677   145  0.1830 0.2360        
REMARK   3     6  2.7400 -  2.5790    1.00     1676   147  0.1760 0.2490        
REMARK   3     7  2.5790 -  2.4500    1.00     1649   137  0.1790 0.2220        
REMARK   3     8  2.4500 -  2.3430    1.00     1667   143  0.1800 0.2300        
REMARK   3     9  2.3430 -  2.2530    1.00     1655   136  0.1800 0.2310        
REMARK   3    10  2.2530 -  2.1750    1.00     1664   146  0.1710 0.2410        
REMARK   3    11  2.1750 -  2.1070    1.00     1653   138  0.1670 0.2350        
REMARK   3    12  2.1070 -  2.0470    1.00     1647   144  0.1630 0.2320        
REMARK   3    13  2.0470 -  1.9930    1.00     1642   138  0.1790 0.2550        
REMARK   3    14  1.9930 -  1.9440    0.98     1625   143  0.1910 0.2520        
REMARK   3    15  1.9440 -  1.9000    0.95     1554   124  0.2000 0.2230        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 50.32                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.91000                                              
REMARK   3    B22 (A**2) : -6.51300                                             
REMARK   3    B33 (A**2) : -0.39700                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           2386                                  
REMARK   3   ANGLE     :  0.972           3235                                  
REMARK   3   CHIRALITY :  0.066            367                                  
REMARK   3   PLANARITY :  0.004            411                                  
REMARK   3   DIHEDRAL  : 15.901            837                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 304:395)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3755  61.8369  65.5941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0898 T22:   0.1396                                     
REMARK   3      T33:   0.1328 T12:   0.0105                                     
REMARK   3      T13:  -0.0285 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4193 L22:   2.5869                                     
REMARK   3      L33:   1.4735 L12:   0.4932                                     
REMARK   3      L13:  -0.3240 L23:  -0.1365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:   0.0601 S13:  -0.1098                       
REMARK   3      S21:  -0.0058 S22:   0.0478 S23:  -0.0571                       
REMARK   3      S31:  -0.0349 S32:  -0.0204 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 405:494)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7521  41.9320  62.0380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1368 T22:   0.1552                                     
REMARK   3      T33:   0.1393 T12:  -0.0019                                     
REMARK   3      T13:  -0.0089 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5586 L22:   2.8516                                     
REMARK   3      L33:   1.0893 L12:   1.2621                                     
REMARK   3      L13:   0.8700 L23:   1.5077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0602 S12:  -0.0612 S13:  -0.0554                       
REMARK   3      S21:   0.0884 S22:  -0.0188 S23:  -0.1083                       
REMARK   3      S31:   0.1399 S32:  -0.0527 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 497:590)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8507  16.0470  36.5243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2033 T22:   0.1646                                     
REMARK   3      T33:   0.1430 T12:   0.0030                                     
REMARK   3      T13:  -0.0254 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8602 L22:   1.0468                                     
REMARK   3      L33:   1.6560 L12:  -0.6137                                     
REMARK   3      L13:  -1.1591 L23:   0.7861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0401 S12:  -0.0792 S13:   0.0348                       
REMARK   3      S21:   0.0587 S22:   0.0848 S23:  -0.1524                       
REMARK   3      S31:   0.0363 S32:   0.1033 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3L5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000056858.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798, 0.9537                     
REMARK 200  MONOCHROMATOR                  : UNDULATOR                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27278                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 18.50                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.57200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHENIX AUTOSOL                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NACL, TRIS-HCL, PH 8.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       20.78250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.59250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.67350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.59250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.78250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.67350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     LYS A 306    CD   CE   NZ                                        
REMARK 470     LYS A 313    CG   CD   CE   NZ                                   
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     TRP A 351    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 351    CZ3  CH2                                            
REMARK 470     LYS A 352    CG   CD   CE   NZ                                   
REMARK 470     SER A 353    OG                                                  
REMARK 470     HIS A 354    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 383    CD1  CD2                                            
REMARK 470     LYS A 409    CD   CE   NZ                                        
REMARK 470     LYS A 413    NZ                                                  
REMARK 470     SER A 427    OG                                                  
REMARK 470     LYS A 429    CE   NZ                                             
REMARK 470     LYS A 441    CG   CD   CE   NZ                                   
REMARK 470     LYS A 489    NZ                                                  
REMARK 470     LYS A 506    CE   NZ                                             
REMARK 470     LYS A 507    NZ                                                  
REMARK 470     LYS A 510    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 361       69.30   -115.82                                   
REMARK 500    ALA A 362     -179.82    178.19                                   
REMARK 500    ARG A 461       53.18    -90.18                                   
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 EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 591                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 592                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 16                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 593                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 17                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L5H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L5J   RELATED DB: PDB                                   
DBREF  3L5I A  301   590  UNP    P40189   IL6RB_HUMAN    323    612             
SEQRES   1 A  290  GLU ASP ARG PRO SER LYS ALA PRO SER PHE TRP TYR LYS          
SEQRES   2 A  290  ILE ASP PRO SER HIS THR GLN GLY TYR ARG THR VAL GLN          
SEQRES   3 A  290  LEU VAL TRP LYS THR LEU PRO PRO PHE GLU ALA ASN GLY          
SEQRES   4 A  290  LYS ILE LEU ASP TYR GLU VAL THR LEU THR ARG TRP LYS          
SEQRES   5 A  290  SER HIS LEU GLN ASN TYR THR VAL ASN ALA THR LYS LEU          
SEQRES   6 A  290  THR VAL ASN LEU THR ASN ASP ARG TYR LEU ALA THR LEU          
SEQRES   7 A  290  THR VAL ARG ASN LEU VAL GLY LYS SER ASP ALA ALA VAL          
SEQRES   8 A  290  LEU THR ILE PRO ALA CYS ASP PHE GLN ALA THR HIS PRO          
SEQRES   9 A  290  VAL MSE ASP LEU LYS ALA PHE PRO LYS ASP ASN MSE LEU          
SEQRES  10 A  290  TRP VAL GLU TRP THR THR PRO ARG GLU SER VAL LYS LYS          
SEQRES  11 A  290  TYR ILE LEU GLU TRP CYS VAL LEU SER ASP LYS ALA PRO          
SEQRES  12 A  290  CYS ILE THR ASP TRP GLN GLN GLU ASP GLY THR VAL HIS          
SEQRES  13 A  290  ARG THR TYR LEU ARG GLY ASN LEU ALA GLU SER LYS CYS          
SEQRES  14 A  290  TYR LEU ILE THR VAL THR PRO VAL TYR ALA ASP GLY PRO          
SEQRES  15 A  290  GLY SER PRO GLU SER ILE LYS ALA TYR LEU LYS GLN ALA          
SEQRES  16 A  290  PRO PRO SER LYS GLY PRO THR VAL ARG THR LYS LYS VAL          
SEQRES  17 A  290  GLY LYS ASN GLU ALA VAL LEU GLU TRP ASP GLN LEU PRO          
SEQRES  18 A  290  VAL ASP VAL GLN ASN GLY PHE ILE ARG ASN TYR THR ILE          
SEQRES  19 A  290  PHE TYR ARG THR ILE ILE GLY ASN GLU THR ALA VAL ASN          
SEQRES  20 A  290  VAL ASP SER SER HIS THR GLU TYR THR LEU SER SER LEU          
SEQRES  21 A  290  THR SER ASP THR LEU TYR MSE VAL ARG MSE ALA ALA TYR          
SEQRES  22 A  290  THR ASP GLU GLY GLY LYS ASP GLY PRO GLU PHE THR PHE          
SEQRES  23 A  290  THR THR PRO LYS                                              
MODRES 3L5I MSE A  406  MET  SELENOMETHIONINE                                   
MODRES 3L5I MSE A  416  MET  SELENOMETHIONINE                                   
MODRES 3L5I MSE A  567  MET  SELENOMETHIONINE                                   
MODRES 3L5I MSE A  570  MET  SELENOMETHIONINE                                   
HET    MSE  A 406       8                                                       
HET    MSE  A 416       8                                                       
HET    MSE  A 567       8                                                       
HET    MSE  A 570       8                                                       
HET    EDO  A   1       4                                                       
HET    EDO  A   2       4                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  A   6       4                                                       
HET    EDO  A   7       4                                                       
HET    EDO  A   8       4                                                       
HET    EDO  A   9       4                                                       
HET    EDO  A  10       4                                                       
HET    EDO  A  11       4                                                       
HET    EDO  A  12       4                                                       
HET    EDO  A  13       4                                                       
HET     CL  A 591       1                                                       
HET    EDO  A  14       4                                                       
HET     CL  A 592       1                                                       
HET    EDO  A  15       4                                                       
HET    EDO  A  16       4                                                       
HET     CL  A 593       1                                                       
HET    EDO  A  17       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2  EDO    17(C2 H6 O2)                                                 
FORMUL  15   CL    3(CL 1-)                                                     
FORMUL  22  HOH   *204(H2 O)                                                    
HELIX    1   1 PRO A  333  ASN A  338  1                                   6    
HELIX    2   2 PRO A  521  ASN A  526  1                                   6    
SHEET    1   A 3 PHE A 310  PRO A 316  0                                        
SHEET    2   A 3 ARG A 323  TRP A 329 -1  O  THR A 324   N  ASP A 315           
SHEET    3   A 3 LYS A 364  LEU A 369 -1  O  VAL A 367   N  VAL A 325           
SHEET    1   B 4 GLN A 356  VAL A 360  0                                        
SHEET    2   B 4 ILE A 341  ARG A 350 -1  N  TYR A 344   O  VAL A 360           
SHEET    3   B 4 TYR A 374  ASN A 382 -1  O  ARG A 381   N  ASP A 343           
SHEET    4   B 4 ALA A 390  ILE A 394 -1  O  ILE A 394   N  TYR A 374           
SHEET    1   C 3 MSE A 406  LYS A 413  0                                        
SHEET    2   C 3 MSE A 416  THR A 422 -1  O  THR A 422   N  MSE A 406           
SHEET    3   C 3 ARG A 457  TYR A 459 -1  O  THR A 458   N  VAL A 419           
SHEET    1   D 4 ASP A 447  ASP A 452  0                                        
SHEET    2   D 4 LYS A 430  LEU A 438 -1  N  LEU A 433   O  GLN A 449           
SHEET    3   D 4 CYS A 469  TYR A 478 -1  O  CYS A 469   N  LEU A 438           
SHEET    4   D 4 GLY A 481  PRO A 482 -1  O  GLY A 481   N  TYR A 478           
SHEET    1   E 4 ASP A 447  ASP A 452  0                                        
SHEET    2   E 4 LYS A 430  LEU A 438 -1  N  LEU A 433   O  GLN A 449           
SHEET    3   E 4 CYS A 469  TYR A 478 -1  O  CYS A 469   N  LEU A 438           
SHEET    4   E 4 GLU A 486  TYR A 491 -1  O  ILE A 488   N  ILE A 472           
SHEET    1   F 3 VAL A 503  VAL A 508  0                                        
SHEET    2   F 3 ALA A 513  TRP A 517 -1  O  VAL A 514   N  LYS A 506           
SHEET    3   F 3 GLU A 554  LEU A 557 -1  O  TYR A 555   N  LEU A 515           
SHEET    1   G 4 THR A 544  ASP A 549  0                                        
SHEET    2   G 4 ASN A 531  THR A 538 -1  N  TYR A 536   O  THR A 544           
SHEET    3   G 4 LEU A 565  THR A 574 -1  O  ARG A 569   N  PHE A 535           
SHEET    4   G 4 GLY A 577  ASP A 580 -1  O  GLY A 577   N  THR A 574           
SHEET    1   H 4 THR A 544  ASP A 549  0                                        
SHEET    2   H 4 ASN A 531  THR A 538 -1  N  TYR A 536   O  THR A 544           
SHEET    3   H 4 LEU A 565  THR A 574 -1  O  ARG A 569   N  PHE A 535           
SHEET    4   H 4 PHE A 584  THR A 587 -1  O  PHE A 586   N  TYR A 566           
SSBOND   1 CYS A  436    CYS A  444                          1555   1555  2.04  
LINK         C   VAL A 405                 N   MSE A 406     1555   1555  1.33  
LINK         C   MSE A 406                 N   ASP A 407     1555   1555  1.33  
LINK         C   ASN A 415                 N   MSE A 416     1555   1555  1.33  
LINK         C   MSE A 416                 N   LEU A 417     1555   1555  1.33  
LINK         C   TYR A 566                 N   MSE A 567     1555   1555  1.33  
LINK         C   MSE A 567                 N   VAL A 568     1555   1555  1.33  
LINK         C   ARG A 569                 N   MSE A 570     1555   1555  1.33  
LINK         C   MSE A 570                 N   ALA A 571     1555   1555  1.33  
SITE     1 AC1  6 EDO A  10  HOH A  53  THR A 366  VAL A 437                    
SITE     2 AC1  6 TYR A 470  HOH A 612                                          
SITE     1 AC2  7 HOH A  55  HOH A 112  PRO A 412  ALA A 490                    
SITE     2 AC2  7 TYR A 491  GLN A 494  PHE A 528                               
SITE     1 AC3  7 PHE A 535  ARG A 537  GLU A 543  MSE A 567                    
SITE     2 AC3  7 VAL A 568  ARG A 569  GLU A 583                               
SITE     1 AC4  9 HOH A  51  HOH A 295  PHE A 399  ALA A 401                    
SITE     2 AC4  9 THR A 402  TYR A 478  ASP A 480  PRO A 482                    
SITE     3 AC4  9 GLY A 483                                                     
SITE     1 AC5  3 ARG A 569  TYR A 573  ASP A 580                               
SITE     1 AC6  3 GLU A 426  VAL A 428  GLY A 453                               
SITE     1 AC7  5 HOH A 125  HIS A 403  PRO A 404  ASN A 542                    
SITE     2 AC7  5 THR A 544                                                     
SITE     1 AC8  3 GLU A 434  LEU A 471  THR A 473                               
SITE     1 AC9  5 VAL A 328  GLU A 434  THR A 446  TRP A 448                    
SITE     2 AC9  5 HOH A 638                                                     
SITE     1 BC1  7 EDO A   1  HOH A  72  ASN A 368  TRP A 435                    
SITE     2 BC1  7 VAL A 437  ILE A 445  ASP A 447                               
SITE     1 BC2  3 HOH A  92  ILE A 341  ASN A 361                               
SITE     1 BC3  3 HOH A 292  TRP A 311  TYR A 312                               
SITE     1 BC4  4 PRO A 316  SER A 317  ALA A 362  THR A 363                    
SITE     1 BC5  3 LYS A 510  ASN A 511  GLU A 512                               
SITE     1 BC6  6 MSE A 416  LEU A 417  LEU A 460  GLY A 462                    
SITE     2 BC6  6 LEU A 464  HOH A 648                                          
SITE     1 BC7  2 ILE A 488  LYS A 489                                          
SITE     1 BC8  5 ARG A 457  GLY A 509  GLU A 512  VAL A 514                    
SITE     2 BC8  5 THR A 556                                                     
SITE     1 BC9  5 THR A 402  SER A 559  LEU A 560  THR A 561                    
SITE     2 BC9  5 TYR A 566                                                     
SITE     1 CC1  4 SER A 309  GLN A 450  ARG A 461  HOH A 606                    
SITE     1 CC2  2 TYR A 555  THR A 556                                          
CRYST1   41.565   75.347  107.185  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024059  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013272  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009330        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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