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Database: PDB
Entry: 3L5J
LinkDB: 3L5J
Original site: 3L5J 
HEADER    IMMUNE SYSTEM                           22-DEC-09   3L5J              
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, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 323-610;                                      
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;                                                         
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, 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 3L5J    1       REMARK                                   
REVDAT   2   05-APR-17 3L5J    1       JRNL   VERSN                             
REVDAT   1   12-MAY-10 3L5J    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.    3.04 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) : 3.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.070                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15678                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 791                             
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 35.1560 -  5.5220    0.99     2638   149  0.2070 0.2400        
REMARK   3     2  5.5220 -  4.3860    0.98     2545   153  0.1680 0.2160        
REMARK   3     3  4.3860 -  3.8320    0.95     2518   106  0.1920 0.2740        
REMARK   3     4  3.8320 -  3.4820    0.97     2534   144  0.2280 0.2920        
REMARK   3     5  3.4820 -  3.2330    0.94     2420   134  0.2380 0.2880        
REMARK   3     6  3.2330 -  3.0420    0.85     2232   105  0.2650 0.3100        
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              : 0.29                                          
REMARK   3   B_SOL              : 1.36                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.550            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.87500                                              
REMARK   3    B22 (A**2) : -4.76800                                             
REMARK   3    B33 (A**2) : 0.89300                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.61800                                             
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      :  0.002           4409                                  
REMARK   3   ANGLE     :  0.621           6060                                  
REMARK   3   CHIRALITY :  0.042            710                                  
REMARK   3   PLANARITY :  0.002            775                                  
REMARK   3   DIHEDRAL  : 13.620           1469                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3L5J 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_1000056859.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-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                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95443                            
REMARK 200  MONOCHROMATOR                  : DIPOLE/BENGING MAGNET              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16494                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
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: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.46800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.61050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.46800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.61050            
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     GLY A   321                                                      
REMARK 465     ASP B   315                                                      
REMARK 465     PRO B   316                                                      
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    CE   NZ                                             
REMARK 470     LYS A 313    CG   CD   CE   NZ                                   
REMARK 470     TYR A 322    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     ARG A 350    CZ   NH1  NH2                                       
REMARK 470     TRP A 351    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 351    CZ3  CH2                                            
REMARK 470     LYS A 352    CD   CE   NZ                                        
REMARK 470     SER A 353    OG                                                  
REMARK 470     HIS A 354    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 364    CE   NZ                                             
REMARK 470     GLN A 400    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 409    CD   CE   NZ                                        
REMARK 470     ARG A 425    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 426    CG   CD   OE1  OE2                                  
REMARK 470     SER A 427    OG                                                  
REMARK 470     LYS A 429    CD   CE   NZ                                        
REMARK 470     LYS A 441    CG   CD   CE   NZ                                   
REMARK 470     ARG A 457    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 468    CE   NZ                                             
REMARK 470     LYS A 489    NZ                                                  
REMARK 470     LYS A 493    CG   CD   CE   NZ                                   
REMARK 470     LYS A 499    CG   CD   CE   NZ                                   
REMARK 470     VAL A 503    CG1  CG2                                            
REMARK 470     LYS A 506    CG   CD   CE   NZ                                   
REMARK 470     LYS A 507    CG   CD   CE   NZ                                   
REMARK 470     VAL A 508    CG1  CG2                                            
REMARK 470     LYS A 510    CG   CD   CE   NZ                                   
REMARK 470     ASN A 511    CG   OD1  ND2                                       
REMARK 470     GLU A 512    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 537    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE A 539    CG1  CG2  CD1                                       
REMARK 470     ILE A 540    CG1  CG2  CD1                                       
REMARK 470     SER A 550    OG                                                  
REMARK 470     GLU A 554    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 583    CG   CD   OE1  OE2                                  
REMARK 470     THR A 588    OG1  CG2                                            
REMARK 470     GLU B 301    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 306    CG   CD   CE   NZ                                   
REMARK 470     LYS B 313    CG   CD   CE   NZ                                   
REMARK 470     SER B 317    OG                                                  
REMARK 470     THR B 319    OG1  CG2                                            
REMARK 470     GLN B 320    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 335    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 336    CD   OE1  OE2                                       
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     ARG B 350    CZ   NH1  NH2                                       
REMARK 470     SER B 353    OG                                                  
REMARK 470     HIS B 354    ND1  CD2  CE1  NE2                                  
REMARK 470     LYS B 364    CG   CD   CE   NZ                                   
REMARK 470     LEU B 383    CG   CD1  CD2                                       
REMARK 470     LYS B 386    CE   NZ                                             
REMARK 470     GLN B 400    CG   CD   OE1  NE2                                  
REMARK 470     THR B 402    OG1  CG2                                            
REMARK 470     LYS B 409    CE   NZ                                             
REMARK 470     LYS B 413    CG   CD   CE   NZ                                   
REMARK 470     ARG B 425    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 426    CG   CD   OE1  OE2                                  
REMARK 470     SER B 427    OG                                                  
REMARK 470     LYS B 429    CE   NZ                                             
REMARK 470     LYS B 441    CG   CD   CE   NZ                                   
REMARK 470     ILE B 445    CG1  CG2  CD1                                       
REMARK 470     HIS B 456    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 463    CG   OD1  ND2                                       
REMARK 470     LYS B 468    NZ                                                  
REMARK 470     LYS B 489    NZ                                                  
REMARK 470     LYS B 493    CG   CD   CE   NZ                                   
REMARK 470     LYS B 499    CG   CD   CE   NZ                                   
REMARK 470     LYS B 506    CE   NZ                                             
REMARK 470     LYS B 507    CG   CD   CE   NZ                                   
REMARK 470     VAL B 508    CG1  CG2                                            
REMARK 470     LYS B 510    CG   CD   CE   NZ                                   
REMARK 470     GLU B 512    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 540    CG1  CG2  CD1                                       
REMARK 470     ASN B 542    CG   OD1  ND2                                       
REMARK 470     ASP B 549    CG   OD1  OD2                                       
REMARK 470     SER B 550    OG                                                  
REMARK 470     SER B 551    OG                                                  
REMARK 470     SER B 559    OG                                                  
REMARK 470     LEU B 560    CG   CD1  CD2                                       
REMARK 470     SER B 562    OG                                                  
REMARK 470     ASP B 563    CG   OD1  OD2                                       
REMARK 470     THR B 564    OG1  CG2                                            
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    ASP A 315      137.80   -170.40                                   
REMARK 500    TRP A 351      125.97    -39.99                                   
REMARK 500    SER A 353     -159.21   -123.91                                   
REMARK 500    ASN A 361       48.34   -107.35                                   
REMARK 500    HIS A 456       -6.05   -141.01                                   
REMARK 500    ASP A 480      -52.48    148.50                                   
REMARK 500    ILE A 488      146.40   -172.00                                   
REMARK 500    LYS A 506      -70.07    -72.21                                   
REMARK 500    GLU A 512      141.79   -172.84                                   
REMARK 500    HIS B 318      -74.45    -77.34                                   
REMARK 500    ASN B 338       37.51     70.59                                   
REMARK 500    ASN B 361       54.28   -101.79                                   
REMARK 500    ASN B 382     -161.59   -111.96                                   
REMARK 500    HIS B 403       72.91     61.05                                   
REMARK 500    GLU B 426      143.14   -176.66                                   
REMARK 500    ALA B 442      143.85   -173.51                                   
REMARK 500    PRO B 443     -146.56    -71.79                                   
REMARK 500    TRP B 517     -168.12   -174.53                                   
REMARK 500    THR B 574     -161.08   -109.94                                   
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 CL A 589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 590                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L5H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L5I   RELATED DB: PDB                                   
DBREF  3L5J A  301   588  UNP    P40189   IL6RB_HUMAN    323    610             
DBREF  3L5J B  301   588  UNP    P40189   IL6RB_HUMAN    323    610             
SEQRES   1 A  288  GLU ASP ARG PRO SER LYS ALA PRO SER PHE TRP TYR LYS          
SEQRES   2 A  288  ILE ASP PRO SER HIS THR GLN GLY TYR ARG THR VAL GLN          
SEQRES   3 A  288  LEU VAL TRP LYS THR LEU PRO PRO PHE GLU ALA ASN GLY          
SEQRES   4 A  288  LYS ILE LEU ASP TYR GLU VAL THR LEU THR ARG TRP LYS          
SEQRES   5 A  288  SER HIS LEU GLN ASN TYR THR VAL ASN ALA THR LYS LEU          
SEQRES   6 A  288  THR VAL ASN LEU THR ASN ASP ARG TYR LEU ALA THR LEU          
SEQRES   7 A  288  THR VAL ARG ASN LEU VAL GLY LYS SER ASP ALA ALA VAL          
SEQRES   8 A  288  LEU THR ILE PRO ALA CYS ASP PHE GLN ALA THR HIS PRO          
SEQRES   9 A  288  VAL MET ASP LEU LYS ALA PHE PRO LYS ASP ASN MET LEU          
SEQRES  10 A  288  TRP VAL GLU TRP THR THR PRO ARG GLU SER VAL LYS LYS          
SEQRES  11 A  288  TYR ILE LEU GLU TRP CYS VAL LEU SER ASP LYS ALA PRO          
SEQRES  12 A  288  CYS ILE THR ASP TRP GLN GLN GLU ASP GLY THR VAL HIS          
SEQRES  13 A  288  ARG THR TYR LEU ARG GLY ASN LEU ALA GLU SER LYS CYS          
SEQRES  14 A  288  TYR LEU ILE THR VAL THR PRO VAL TYR ALA ASP GLY PRO          
SEQRES  15 A  288  GLY SER PRO GLU SER ILE LYS ALA TYR LEU LYS GLN ALA          
SEQRES  16 A  288  PRO PRO SER LYS GLY PRO THR VAL ARG THR LYS LYS VAL          
SEQRES  17 A  288  GLY LYS ASN GLU ALA VAL LEU GLU TRP ASP GLN LEU PRO          
SEQRES  18 A  288  VAL ASP VAL GLN ASN GLY PHE ILE ARG ASN TYR THR ILE          
SEQRES  19 A  288  PHE TYR ARG THR ILE ILE GLY ASN GLU THR ALA VAL ASN          
SEQRES  20 A  288  VAL ASP SER SER HIS THR GLU TYR THR LEU SER SER LEU          
SEQRES  21 A  288  THR SER ASP THR LEU TYR MET VAL ARG MET ALA ALA TYR          
SEQRES  22 A  288  THR ASP GLU GLY GLY LYS ASP GLY PRO GLU PHE THR PHE          
SEQRES  23 A  288  THR THR                                                      
SEQRES   1 B  288  GLU ASP ARG PRO SER LYS ALA PRO SER PHE TRP TYR LYS          
SEQRES   2 B  288  ILE ASP PRO SER HIS THR GLN GLY TYR ARG THR VAL GLN          
SEQRES   3 B  288  LEU VAL TRP LYS THR LEU PRO PRO PHE GLU ALA ASN GLY          
SEQRES   4 B  288  LYS ILE LEU ASP TYR GLU VAL THR LEU THR ARG TRP LYS          
SEQRES   5 B  288  SER HIS LEU GLN ASN TYR THR VAL ASN ALA THR LYS LEU          
SEQRES   6 B  288  THR VAL ASN LEU THR ASN ASP ARG TYR LEU ALA THR LEU          
SEQRES   7 B  288  THR VAL ARG ASN LEU VAL GLY LYS SER ASP ALA ALA VAL          
SEQRES   8 B  288  LEU THR ILE PRO ALA CYS ASP PHE GLN ALA THR HIS PRO          
SEQRES   9 B  288  VAL MET ASP LEU LYS ALA PHE PRO LYS ASP ASN MET LEU          
SEQRES  10 B  288  TRP VAL GLU TRP THR THR PRO ARG GLU SER VAL LYS LYS          
SEQRES  11 B  288  TYR ILE LEU GLU TRP CYS VAL LEU SER ASP LYS ALA PRO          
SEQRES  12 B  288  CYS ILE THR ASP TRP GLN GLN GLU ASP GLY THR VAL HIS          
SEQRES  13 B  288  ARG THR TYR LEU ARG GLY ASN LEU ALA GLU SER LYS CYS          
SEQRES  14 B  288  TYR LEU ILE THR VAL THR PRO VAL TYR ALA ASP GLY PRO          
SEQRES  15 B  288  GLY SER PRO GLU SER ILE LYS ALA TYR LEU LYS GLN ALA          
SEQRES  16 B  288  PRO PRO SER LYS GLY PRO THR VAL ARG THR LYS LYS VAL          
SEQRES  17 B  288  GLY LYS ASN GLU ALA VAL LEU GLU TRP ASP GLN LEU PRO          
SEQRES  18 B  288  VAL ASP VAL GLN ASN GLY PHE ILE ARG ASN TYR THR ILE          
SEQRES  19 B  288  PHE TYR ARG THR ILE ILE GLY ASN GLU THR ALA VAL ASN          
SEQRES  20 B  288  VAL ASP SER SER HIS THR GLU TYR THR LEU SER SER LEU          
SEQRES  21 B  288  THR SER ASP THR LEU TYR MET VAL ARG MET ALA ALA TYR          
SEQRES  22 B  288  THR ASP GLU GLY GLY LYS ASP GLY PRO GLU PHE THR PHE          
SEQRES  23 B  288  THR THR                                                      
HET    EDO  A   1       4                                                       
HET     CL  A 589       1                                                       
HET     CL  B   1       1                                                       
HET     CL  B 589       1                                                       
HET     CL  B 590       1                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   8  HOH   *15(H2 O)                                                     
HELIX    1   1 PRO A  333  ASN A  338  1                                   6    
HELIX    2   2 PRO A  521  ASN A  526  1                                   6    
HELIX    3   3 PRO B  333  ASN B  338  1                                   6    
HELIX    4   4 PRO B  521  ASN B  526  1                                   6    
SHEET    1   A 3 PHE A 310  ASP A 315  0                                        
SHEET    2   A 3 ARG A 323  TRP A 329 -1  O  GLN A 326   N  LYS A 313           
SHEET    3   A 3 LYS A 364  LEU A 369 -1  O  LEU A 369   N  ARG A 323           
SHEET    1   B 4 LEU A 355  VAL A 360  0                                        
SHEET    2   B 4 ASP A 343  ARG A 350 -1  N  VAL A 346   O  TYR A 358           
SHEET    3   B 4 TYR A 374  ARG A 381 -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 MET A 406  LYS A 413  0                                        
SHEET    2   C 3 MET A 416  THR A 422 -1  O  THR A 422   N  MET 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  VAL A 437 -1  N  TRP A 435   O  ASP A 447           
SHEET    3   D 4 CYS A 469  TYR A 478 -1  O  LEU A 471   N  CYS A 436           
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  VAL A 437 -1  N  TRP A 435   O  ASP A 447           
SHEET    3   E 4 CYS A 469  TYR A 478 -1  O  LEU A 471   N  CYS A 436           
SHEET    4   E 4 GLU A 486  TYR A 491 -1  O  ILE A 488   N  ILE A 472           
SHEET    1   F 3 ARG A 504  LYS A 507  0                                        
SHEET    2   F 3 ALA A 513  GLU A 516 -1  O  GLU A 516   N  ARG A 504           
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 584   N  VAL A 568           
SHEET    1   I 3 PHE B 310  LYS B 313  0                                        
SHEET    2   I 3 TYR B 322  TRP B 329 -1  O  VAL B 328   N  TRP B 311           
SHEET    3   I 3 LYS B 364  THR B 370 -1  O  LEU B 365   N  LEU B 327           
SHEET    1   J 4 LEU B 355  VAL B 360  0                                        
SHEET    2   J 4 ASP B 343  ARG B 350 -1  N  LEU B 348   O  GLN B 356           
SHEET    3   J 4 TYR B 374  ARG B 381 -1  O  ARG B 381   N  ASP B 343           
SHEET    4   J 4 ALA B 390  ILE B 394 -1  O  LEU B 392   N  ALA B 376           
SHEET    1   K 3 MET B 406  LYS B 413  0                                        
SHEET    2   K 3 MET B 416  THR B 422 -1  O  THR B 422   N  MET B 406           
SHEET    3   K 3 ARG B 457  TYR B 459 -1  O  THR B 458   N  VAL B 419           
SHEET    1   L 4 ASP B 447  ASP B 452  0                                        
SHEET    2   L 4 LYS B 430  VAL B 437 -1  N  TYR B 431   O  GLU B 451           
SHEET    3   L 4 CYS B 469  VAL B 477 -1  O  LEU B 471   N  CYS B 436           
SHEET    4   L 4 GLU B 486  TYR B 491 -1  O  ALA B 490   N  TYR B 470           
SHEET    1   M 3 ARG B 504  VAL B 508  0                                        
SHEET    2   M 3 ALA B 513  GLU B 516 -1  O  VAL B 514   N  LYS B 507           
SHEET    3   M 3 GLU B 554  LEU B 557 -1  O  LEU B 557   N  ALA B 513           
SHEET    1   N 4 THR B 544  VAL B 548  0                                        
SHEET    2   N 4 ASN B 531  ARG B 537 -1  N  ILE B 534   O  VAL B 546           
SHEET    3   N 4 LEU B 565  TYR B 573 -1  O  ARG B 569   N  PHE B 535           
SHEET    4   N 4 GLY B 578  ASP B 580 -1  O  LYS B 579   N  ALA B 572           
SHEET    1   O 4 THR B 544  VAL B 548  0                                        
SHEET    2   O 4 ASN B 531  ARG B 537 -1  N  ILE B 534   O  VAL B 546           
SHEET    3   O 4 LEU B 565  TYR B 573 -1  O  ARG B 569   N  PHE B 535           
SHEET    4   O 4 PHE B 584  THR B 587 -1  O  PHE B 584   N  VAL B 568           
SSBOND   1 CYS A  397    CYS B  397                          1555   1555  2.03  
SSBOND   2 CYS A  436    CYS A  444                          1555   1555  2.03  
SSBOND   3 CYS B  436    CYS B  444                          1555   1555  2.03  
SITE     1 AC1  7 ALA A 401  THR A 402  TYR A 478  ASP A 480                    
SITE     2 AC1  7 GLY A 481  PRO A 482  GLY A 483                               
SITE     1 AC2  3 SER A 309  GLN A 450  ARG A 461                               
SITE     1 AC3  5 SER B 309  LYS B 330  GLN B 449  GLN B 450                    
SITE     2 AC3  5 ARG B 461                                                     
SITE     1 AC4  3 LYS B 352  TYR B 491  GLN B 494                               
SITE     1 AC5  2 ARG B 537  ARG B 569                                          
CRYST1  102.936   89.221  106.877  90.00 117.72  90.00 C 1 2 1       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      0.009715  0.000000  0.005104        0.00000                         
SCALE2      0.000000  0.011208  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010569        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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