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Database: PDB
Entry: 1N6V
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Original site: 1N6V 
HEADER    IMMUNE SYSTEM                           12-NOV-02   1N6V              
TITLE     AVERAGE STRUCTURE OF THE INTERFERON-BINDING ECTODOMAIN OF             
TITLE    2 THE HUMAN TYPE I INTERFERON RECEPTOR                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERFERON-ALPHA/BETA RECEPTOR BETA CHAIN;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IFNAR2-EC, IFN-ALPHA-REC, TYPE I INTERFERON                 
COMPND   5 RECEPTOR, IFN-R, INTERFERON ALPHA/BETA RECEPTOR- 2;                  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TG1;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    IMMUNOGLOBULIN FOLD, FIBRONECTIN FOLD, TWO-DOMAIN STRUCTURE,          
KEYWDS   2 IMMUNE SYSTEM                                                        
EXPDTA    SOLUTION NMR                                                          
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    J.H.CHILL,S.R.QUADT,R.LEVY,G.SCHREIBER,J.ANGLISTER                    
REVDAT   2   24-FEB-09 1N6V    1       VERSN                                    
REVDAT   1   15-JUL-03 1N6V    0                                                
JRNL        AUTH   J.H.CHILL,S.R.QUADT,R.LEVY,G.SCHREIBER,J.ANGLISTER           
JRNL        TITL   THE HUMAN TYPE I INTERFERON RECEPTOR. NMR                    
JRNL        TITL 2 STRUCTURE REVEALS THE MOLECULAR BASIS OF LIGAND              
JRNL        TITL 3 BINDING.                                                     
JRNL        REF    STRUCTURE                     V.  11   791 2003              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12842042                                                     
JRNL        DOI    10.1016/S0969-2126(03)00120-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.H.CHILL,R.NIVASCH,R.LEVY,S.ALBECK,G.SCHREIBER,             
REMARK   1  AUTH 2 J.ANGLISTER                                                  
REMARK   1  TITL   THE HUMAN INTERFERON RECEPTOR: NMR-BASED MODELING,           
REMARK   1  TITL 2 MAPPING OF THE IFN-ALPHA2 BINDING SITE, AND                  
REMARK   1  TITL 3 OBSERVED LIGAND-INDUCED TIGHTENING                           
REMARK   1  REF    BIOCHEMISTRY                  V.  41  3575 2002              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI011778F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STRUCTURE BASED UPON 1947 NOE-            
REMARK   3  DERIVED DISTANCE RESTRAINTS (1066 OF WHICH LONG RANGE), 172         
REMARK   3  DIHEDRAL ANGLE RESTRAINTS (OF WHICH 88 EXPERIMENTAL AND 84          
REMARK   3  TALOS-DERIVED), 138 HYDROGEN-BOND RESTRAINTS AND 109 RESIDUAL       
REMARK   3  DIPOLAR COUPLING RESTRAINTS                                         
REMARK   4                                                                      
REMARK   4 1N6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017592.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 308; 308; 305                      
REMARK 210  PH                             : 8; 8; 8                            
REMARK 210  IONIC STRENGTH                 : 20MM TRIS BUFFER; 20MM TRIS        
REMARK 210                                   BUFFER; 20MM TRIS BUFFER           
REMARK 210  PRESSURE                       : AMBIENT; AMBIENT; AMBIENT          
REMARK 210  SAMPLE CONTENTS                : 0.4MM U-15N IFNAR2-EC; 20MM D      
REMARK 210                                   -TRIS PH 8, 0.02% NAN3; 0.35MM     
REMARK 210                                   U-13C,15N IFNAR2-EC; 20MM D-       
REMARK 210                                   TRIS PH 8, 0.02% NAN3; 0.3MM U     
REMARK 210                                   -13C,15N IFNAR2-EC; 20MM D-        
REMARK 210                                   TRIS PH 8, 0.02% NAN3              
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, HNHA,      
REMARK 210                                   HNCA, HNCACB, CBCACONH, 3D_13C     
REMARK 210                                   -SEPARATED_NOESY                   
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ, 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : DRX, DMX                           
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 3.0, CNS 1.1, NMRPIPE      
REMARK 210                                   2.1                                
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY, SIMULATED       
REMARK 210                                   ANNEALING                          
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: ALL EXPERIMENTS CONDUCTED IN SHIGEMI TUBES EQUIPPED          
REMARK 210  WITH INSERT                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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   3     -169.25     45.55                                   
REMARK 500    ASP A   6       95.65    -69.85                                   
REMARK 500    TYR A   7       73.55    -69.89                                   
REMARK 500    GLU A  10       63.83    174.19                                   
REMARK 500    CYS A  12       34.60     38.40                                   
REMARK 500    HIS A  32      -70.34   -120.31                                   
REMARK 500    SER A  33      -67.99   -100.75                                   
REMARK 500    ASP A  51       55.51   -111.70                                   
REMARK 500    ASN A  57       -9.29     79.95                                   
REMARK 500    ASN A  60       75.49     13.08                                   
REMARK 500    LEU A  68       88.74   -171.49                                   
REMARK 500    TYR A  79       88.47    -59.51                                   
REMARK 500    SER A  94       94.73   -160.52                                   
REMARK 500    ALA A 102      -33.11    -39.78                                   
REMARK 500    MET A 105       88.43     28.93                                   
REMARK 500    GLU A 108      -59.03   -158.53                                   
REMARK 500    PRO A 110      153.50    -33.66                                   
REMARK 500    ASP A 138       34.48   -156.83                                   
REMARK 500    GLN A 146       68.29   -110.00                                   
REMARK 500    LYS A 159       67.20    -69.81                                   
REMARK 500    MET A 162       41.48    -93.17                                   
REMARK 500    ASP A 171     -165.70   -110.69                                   
REMARK 500    PRO A 175      156.17    -38.70                                   
REMARK 500    ASN A 176       67.96     64.67                                   
REMARK 500    SER A 188       39.76    177.79                                   
REMARK 500    ALA A 192       42.71    -95.21                                   
REMARK 500    PRO A 197      107.63    -50.21                                   
REMARK 500    LEU A 198      174.84    -49.87                                   
REMARK 500    PRO A 204      103.23    -55.44                                   
REMARK 500    GLN A 207       38.02    -92.27                                   
REMARK 500    GLU A 208     -159.65    -74.65                                   
REMARK 500    SER A 209     -166.72    -56.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N6U   RELATED DB: PDB                                   
DBREF  1N6V A    1   210  UNP    P48551   INAR2_HUMAN     28    237             
SEQADV 1N6V PHE A  211  UNP  P48551              CLONING ARTIFACT               
SEQADV 1N6V SER A  212  UNP  P48551              CLONING ARTIFACT               
SEQRES   1 A  212  SER TYR ASP SER PRO ASP TYR THR ASP GLU SER CYS THR          
SEQRES   2 A  212  PHE LYS ILE SER LEU ARG ASN PHE ARG SER ILE LEU SER          
SEQRES   3 A  212  TRP GLU LEU LYS ASN HIS SER ILE VAL PRO THR HIS TYR          
SEQRES   4 A  212  THR LEU LEU TYR THR ILE MET SER LYS PRO GLU ASP LEU          
SEQRES   5 A  212  LYS VAL VAL LYS ASN CYS ALA ASN THR THR ARG SER PHE          
SEQRES   6 A  212  CYS ASP LEU THR ASP GLU TRP ARG SER THR HIS GLU ALA          
SEQRES   7 A  212  TYR VAL THR VAL LEU GLU GLY PHE SER GLY ASN THR THR          
SEQRES   8 A  212  LEU PHE SER CYS SER HIS ASN PHE TRP LEU ALA ILE ASP          
SEQRES   9 A  212  MET SER PHE GLU PRO PRO GLU PHE GLU ILE VAL GLY PHE          
SEQRES  10 A  212  THR ASN HIS ILE ASN VAL MET VAL LYS PHE PRO SER ILE          
SEQRES  11 A  212  VAL GLU GLU GLU LEU GLN PHE ASP LEU SER LEU VAL ILE          
SEQRES  12 A  212  GLU GLU GLN SER GLU GLY ILE VAL LYS LYS HIS LYS PRO          
SEQRES  13 A  212  GLU ILE LYS GLY ASN MET SER GLY ASN PHE THR TYR ILE          
SEQRES  14 A  212  ILE ASP LYS LEU ILE PRO ASN THR ASN TYR CYS VAL SER          
SEQRES  15 A  212  VAL TYR LEU GLU HIS SER ASP GLU GLN ALA VAL ILE LYS          
SEQRES  16 A  212  SER PRO LEU LYS CYS THR LEU LEU PRO PRO GLY GLN GLU          
SEQRES  17 A  212  SER GLU PHE SER                                              
HELIX    1   1 LEU A  101  MET A  105  1                                   5    
HELIX    2   2 VAL A  131  LEU A  135  5                                   5    
SHEET    1   A 3 THR A  13  LEU A  18  0                                        
SHEET    2   A 3 SER A  23  GLU A  28 -1  O  SER A  26   N  LYS A  15           
SHEET    3   A 3 CYS A  66  LEU A  68 -1  O  LEU A  68   N  SER A  23           
SHEET    1   B 4 LYS A  48  VAL A  54  0                                        
SHEET    2   B 4 TYR A  39  ILE A  45 -1  N  ILE A  45   O  LYS A  48           
SHEET    3   B 4 ALA A  78  SER A  87 -1  O  VAL A  82   N  LEU A  42           
SHEET    4   B 4 THR A  90  THR A  91 -1  O  THR A  90   N  SER A  87           
SHEET    1   C 4 LYS A  48  VAL A  54  0                                        
SHEET    2   C 4 TYR A  39  ILE A  45 -1  N  ILE A  45   O  LYS A  48           
SHEET    3   C 4 ALA A  78  SER A  87 -1  O  VAL A  82   N  LEU A  42           
SHEET    4   C 4 CYS A  95  TRP A 100 -1  O  HIS A  97   N  THR A  81           
SHEET    1   D 2 GLU A 111  PHE A 117  0                                        
SHEET    2   D 2 HIS A 120  LYS A 126 -1  O  MET A 124   N  GLU A 113           
SHEET    1   E 4 ILE A 150  HIS A 154  0                                        
SHEET    2   E 4 SER A 140  SER A 147 -1  N  SER A 147   O  ILE A 150           
SHEET    3   E 4 TYR A 179  GLU A 186 -1  O  TYR A 184   N  VAL A 142           
SHEET    4   E 4 LYS A 199  THR A 201 -1  O  LYS A 199   N  VAL A 181           
SSBOND   1 CYS A   12    CYS A   95                          1555   1555  2.03  
SSBOND   2 CYS A   58    CYS A   66                          1555   1555  2.03  
SSBOND   3 CYS A  180    CYS A  200                          1555   1555  2.04  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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