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Database: PDB
Entry: 1OSX
LinkDB: 1OSX
Original site: 1OSX 
HEADER    IMMUNE SYSTEM                           20-MAR-03   1OSX              
TITLE     SOLUTION STRUCTURE OF THE EXTRACELLULAR DOMAIN OF BLYS                
TITLE    2 RECEPTOR 3 (BR3)                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY                 
COMPND   3 MEMBER 13C;                                                          
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   6 SYNONYM: B CELL- ACTIVATING FACTOR RECEPTOR, BAFF RECEPTOR,          
COMPND   7 BAFF-R, BLYS RECEPTOR 3;                                             
COMPND   8 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: TNFRSF13C OR BAFFR OR BR3;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYSTEINE-RICH DOMAIN, EXTRACELLULAR DOMAIN, TUMOR NECROSIS            
KEYWDS   2 FACTOR RECEPTOR, IMMUNE SYSTEM                                       
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,                     
AUTHOR   2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK          
REVDAT   2   24-FEB-09 1OSX    1       VERSN                                    
REVDAT   1   27-MAY-03 1OSX    0                                                
JRNL        AUTH   N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,            
JRNL        AUTH 2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,                 
JRNL        AUTH 3 M.A.STAROVASNIK                                              
JRNL        TITL   BAFF/BLYS RECEPTOR 3 COMPRISES A MINIMAL TNF                 
JRNL        TITL 2 RECEPTOR-LIKE MODULE THAT ENCODES A HIGHLY FOCUSED           
JRNL        TITL 3 LIGAND-BINDING SITE                                          
JRNL        REF    BIOCHEMISTRY                  V.  42  5977 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12755599                                                     
JRNL        DOI    10.1021/BI034017G                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98                                            
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ONLY 19 RESIDUES, INCLUDING CYS19         
REMARK   3  THROUGH LEU37 ARE ORDERED IN SOLUTION, WHILE THE REST OF THE        
REMARK   3  EXTRACELLULAR DOMAIN IS HIGHLY FLEXIBLE (BASED ON 1H-15N            
REMARK   3  HETERONUCLEAR NOE ANALYSIS). FURTHERMORE, THE BAFF-BINDING          
REMARK   3  DOMAIN OF BR3 WAS FOUND TO RESIDE WITHIN A FRAGMENT CONSISTING      
REMARK   3  OF THR17-ARG42 DENOTED MINIBR3. THUS, THE STRUCTURE OF BR3 WAS      
REMARK   3  CALCULATED ONLY FOR THESE 26 RESIDUES, BASED ON A TOTAL OF 315      
REMARK   3  DISTANCE AND 46 DIHEDRAL ANGLE RESTRAINTS DERIVED FROM              
REMARK   3  ANALYSIS OF NMR DATA COLLEECTED ON THE ENTIRE BR3 ECD.              
REMARK   4                                                                      
REMARK   4 1OSX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018636.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 293                                
REMARK 210  PH                             : 5.0                                
REMARK 210  IONIC STRENGTH                 : 50 MM NACL, 25 MM NA2PO4           
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.5 MM BR3 U-15N,25 MM             
REMARK 210                                   NA2PO4, 50 MM NACL, 0.1 MM         
REMARK 210                                   NAN3, 0.1 MM DSS-D10; 1.5 MM       
REMARK 210                                   BR3 U-15N,13C,25 MM NA2PO4, 50     
REMARK 210                                   MM NACL, 0.1 MM NAN3, 0.1 MM       
REMARK 210                                   DSS-D10; 1.5 MM BR3 U-15N,13C,     
REMARK 210                                   25 MM NA2PO4, 50 MM NACL, 0.1      
REMARK 210                                   MM NAN3, 0.1 MM DSS-D10            
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, 3D_        
REMARK 210                                   13C-SEPARATED_NOESY, HNHA,         
REMARK 210                                   HNHB, 3D HCCH-COSY, 3D HCCH-       
REMARK 210                                   TOCSY, 3D HNCO, 3D HNCA, 3D        
REMARK 210                                   CBCA(CO)NH                         
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 800 MHZ                   
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 3.6, FELIX 98, X-PLOR      
REMARK 210                                   98                                 
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 128                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   RESTRAINT VIOLATION ENERGY         
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR      
REMARK 210  SPECTROSCOPY.                                                       
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     ARG A    54                                                      
REMARK 465     THR A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     LEU A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     GLN A    60                                                      
REMARK 465     GLU A    61                                                      
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  1 PRO A  18     -163.60    -71.04                                   
REMARK 500  1 CYS A  19     -146.78    -58.46                                   
REMARK 500  1 PRO A  21      -24.62    -37.64                                   
REMARK 500  1 HIS A  31     -177.68   -174.00                                   
REMARK 500  1 ALA A  34      101.53    -40.05                                   
REMARK 500  1 CYS A  35      115.77    -39.85                                   
REMARK 500  1 LEU A  37       17.00     56.26                                   
REMARK 500  1 THR A  40      131.11     62.52                                   
REMARK 500  1 PRO A  41      -95.13    -75.19                                   
REMARK 500  2 PRO A  18      155.31    -38.69                                   
REMARK 500  2 CYS A  19     -145.70    -69.22                                   
REMARK 500  2 PRO A  21      -22.83    -38.22                                   
REMARK 500  2 ARG A  30       46.53     80.26                                   
REMARK 500  2 HIS A  31     -158.44   -173.07                                   
REMARK 500  2 ALA A  34      103.87    -47.68                                   
REMARK 500  2 CYS A  35       99.95    -42.83                                   
REMARK 500  2 LEU A  38     -157.18   -140.00                                   
REMARK 500  2 THR A  40       68.18   -160.57                                   
REMARK 500  3 CYS A  19     -157.36    -75.85                                   
REMARK 500  3 PRO A  21      -22.78    -37.27                                   
REMARK 500  3 HIS A  31     -175.40   -173.00                                   
REMARK 500  3 ALA A  34      105.59    -55.13                                   
REMARK 500  3 CYS A  35      100.04    -40.85                                   
REMARK 500  3 LEU A  37        0.15     56.82                                   
REMARK 500  3 THR A  40       64.65     29.55                                   
REMARK 500  3 PRO A  41      100.41    -49.73                                   
REMARK 500  4 CYS A  19     -156.68    -75.81                                   
REMARK 500  4 PRO A  21      -23.69    -37.39                                   
REMARK 500  4 ARG A  30       31.30     80.05                                   
REMARK 500  4 HIS A  31     -176.79   -175.09                                   
REMARK 500  4 ALA A  34      107.87    -52.20                                   
REMARK 500  5 PRO A  18      -93.65    -72.82                                   
REMARK 500  5 CYS A  19     -158.33    -78.87                                   
REMARK 500  5 PRO A  21      -35.56    -34.78                                   
REMARK 500  5 ARG A  30       24.99     80.12                                   
REMARK 500  5 ALA A  34      107.22    -49.01                                   
REMARK 500  5 CYS A  35      122.44    -39.98                                   
REMARK 500  5 LEU A  37       19.50     54.56                                   
REMARK 500  5 ARG A  39      116.66   -171.99                                   
REMARK 500  6 PRO A  18      112.35    -38.59                                   
REMARK 500  6 CYS A  19     -146.79    -76.10                                   
REMARK 500  6 PRO A  21       -9.31    -48.58                                   
REMARK 500  6 HIS A  31     -151.72   -173.96                                   
REMARK 500  6 ALA A  34      106.57    -52.01                                   
REMARK 500  6 CYS A  35       99.84    -46.58                                   
REMARK 500  6 LEU A  38     -103.19    -99.90                                   
REMARK 500  6 ARG A  39      -34.70   -172.50                                   
REMARK 500  7 CYS A  19     -158.27   -106.67                                   
REMARK 500  7 PRO A  21      -22.48    -37.57                                   
REMARK 500  7 HIS A  31     -172.85   -173.63                                   
REMARK 500  7 ALA A  34      104.03    -54.23                                   
REMARK 500  7 CYS A  35       99.92    -42.92                                   
REMARK 500  7 PRO A  41      151.05    -40.36                                   
REMARK 500  8 PRO A  18       -6.65    -50.77                                   
REMARK 500  8 CYS A  19     -155.53    -70.60                                   
REMARK 500  8 PRO A  21      -24.51    -37.16                                   
REMARK 500  8 ARG A  30       53.72     80.02                                   
REMARK 500  8 ALA A  34      102.45    -55.40                                   
REMARK 500  8 CYS A  35       99.89    -39.98                                   
REMARK 500  8 LEU A  37       10.20     53.32                                   
REMARK 500  8 ARG A  39       41.48    -78.29                                   
REMARK 500  9 PRO A  18       98.68    -39.81                                   
REMARK 500  9 CYS A  19     -145.43    -65.76                                   
REMARK 500  9 PRO A  21      -23.08    -37.82                                   
REMARK 500  9 HIS A  31     -142.41   -168.09                                   
REMARK 500  9 ARG A  39      134.55    -39.53                                   
REMARK 500 10 PRO A  18      -91.16    -70.74                                   
REMARK 500 10 CYS A  19     -143.74    -78.11                                   
REMARK 500 10 PRO A  21      -25.71    -38.89                                   
REMARK 500 10 LEU A  28      -10.30    -49.47                                   
REMARK 500 10 ALA A  34      108.44    -46.27                                   
REMARK 500 10 LEU A  38      -67.25    -99.95                                   
REMARK 500 10 PRO A  41      -90.24    -70.42                                   
REMARK 500 11 CYS A  19     -157.57    -77.79                                   
REMARK 500 11 PRO A  21      -21.86    -37.96                                   
REMARK 500 11 ARG A  30       37.53     80.25                                   
REMARK 500 11 HIS A  31     -173.43   -174.63                                   
REMARK 500 11 ALA A  34      106.01    -54.42                                   
REMARK 500 11 LEU A  38       49.96   -140.06                                   
REMARK 500 11 PRO A  41      124.52    -37.25                                   
REMARK 500 12 CYS A  19     -152.24   -139.98                                   
REMARK 500 12 PRO A  21      -23.58    -37.59                                   
REMARK 500 12 ARG A  30       49.88     80.05                                   
REMARK 500 12 HIS A  31     -178.23   -173.39                                   
REMARK 500 12 ALA A  34      100.51    -53.42                                   
REMARK 500 12 CYS A  35       99.95    -39.77                                   
REMARK 500 12 LEU A  38       40.47   -140.07                                   
REMARK 500 12 ARG A  39      -81.26   -135.12                                   
REMARK 500 12 THR A  40       55.31   -158.84                                   
REMARK 500 12 PRO A  41      -88.48    -69.66                                   
REMARK 500 13 CYS A  19     -144.65    -67.21                                   
REMARK 500 13 PRO A  21      -36.59    -37.43                                   
REMARK 500 13 CYS A  35       99.76    -54.52                                   
REMARK 500 13 LEU A  38      -91.97   -140.05                                   
REMARK 500 13 THR A  40       70.28     28.90                                   
REMARK 500 13 PRO A  41       95.70    -60.00                                   
REMARK 500 14 PRO A  18      -94.84    -72.62                                   
REMARK 500 14 CYS A  19     -143.63   -158.44                                   
REMARK 500 14 PRO A  21      -39.45    -37.83                                   
REMARK 500 14 ALA A  34      102.97    -48.58                                   
REMARK 500 14 CYS A  35       99.81    -40.11                                   
REMARK 500 14 LEU A  37       17.16     44.19                                   
REMARK 500 14 ARG A  39       37.17    -73.71                                   
REMARK 500 15 CYS A  19     -145.91    -59.60                                   
REMARK 500 15 PRO A  21      -24.72    -37.52                                   
REMARK 500 15 HIS A  31     -150.99   -173.50                                   
REMARK 500 15 CYS A  35       99.92    -53.05                                   
REMARK 500 15 LEU A  38       50.22   -100.57                                   
REMARK 500 15 ARG A  39     -134.55   -146.02                                   
REMARK 500 16 PRO A  18       26.41    -70.40                                   
REMARK 500 16 CYS A  19     -145.98    -69.30                                   
REMARK 500 16 PRO A  21      -23.11    -37.91                                   
REMARK 500 16 VAL A  29      -30.34   -136.91                                   
REMARK 500 16 ARG A  30       46.61     80.41                                   
REMARK 500 16 HIS A  31     -156.95   -172.84                                   
REMARK 500 16 ALA A  34      104.12    -48.63                                   
REMARK 500 16 CYS A  35       99.78    -43.73                                   
REMARK 500 16 LEU A  37       -0.08     58.40                                   
REMARK 500 16 ARG A  39        5.67    -65.41                                   
REMARK 500 16 THR A  40       77.39   -160.89                                   
REMARK 500 16 PRO A  41       82.95    -46.85                                   
REMARK 500 17 CYS A  19     -147.09    -98.04                                   
REMARK 500 17 PRO A  21      -26.94    -36.93                                   
REMARK 500 17 ARG A  30       60.04     71.03                                   
REMARK 500 17 HIS A  31     -161.03   -172.33                                   
REMARK 500 17 ALA A  34       99.26    -51.99                                   
REMARK 500 17 CYS A  35       99.88    -39.98                                   
REMARK 500 17 LEU A  38     -135.27    -99.64                                   
REMARK 500 17 ARG A  39      -70.52    -40.68                                   
REMARK 500 17 THR A  40       76.02   -170.48                                   
REMARK 500 18 CYS A  19     -144.01    -75.95                                   
REMARK 500 18 PRO A  21       -8.96    -48.33                                   
REMARK 500 18 ALA A  34      107.53    -56.64                                   
REMARK 500 18 CYS A  35       99.85    -48.99                                   
REMARK 500 18 LEU A  37        9.56     51.08                                   
REMARK 500 18 THR A  40      -49.42    178.47                                   
REMARK 500 19 PRO A  18       -8.95    -48.75                                   
REMARK 500 19 CYS A  19     -153.52   -136.36                                   
REMARK 500 19 PRO A  21      -21.92    -38.07                                   
REMARK 500 19 ARG A  30       30.79     74.17                                   
REMARK 500 19 HIS A  31     -172.63   -177.52                                   
REMARK 500 19 CYS A  35       99.89    -52.01                                   
REMARK 500 19 LEU A  38     -102.48    -99.67                                   
REMARK 500 20 CYS A  19     -150.36    -71.42                                   
REMARK 500 20 PRO A  21      -22.74    -37.94                                   
REMARK 500 20 HIS A  31     -153.16   -176.23                                   
REMARK 500 20 ALA A  34      107.31    -58.33                                   
REMARK 500 20 CYS A  35       99.93    -43.63                                   
REMARK 500 20 LEU A  37        1.77     56.90                                   
REMARK 500 20 LEU A  38      -72.85   -101.19                                   
REMARK 500 20 THR A  40       64.90     34.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MPV   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF BHPBR3; BR3 RESIDUES 26-31 EMBEDDED            
REMARK 900 IN A BETA-HAIRPIN PEPTIDE                                            
REMARK 900 RELATED ID: 1OSG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BHPBR3 IN COMPLEX WITH BAFF                     
DBREF  1OSX A    1    61  UNP    Q96RJ3   TR13C_HUMAN      1     61             
SEQRES   1 A   61  MET ARG ARG GLY PRO ARG SER LEU ARG GLY ARG ASP ALA          
SEQRES   2 A   61  PRO ALA PRO THR PRO CYS VAL PRO ALA GLU CYS PHE ASP          
SEQRES   3 A   61  LEU LEU VAL ARG HIS CYS VAL ALA CYS GLY LEU LEU ARG          
SEQRES   4 A   61  THR PRO ARG PRO LYS PRO ALA GLY ALA SER SER PRO ALA          
SEQRES   5 A   61  PRO ARG THR ALA LEU GLN PRO GLN GLU                          
SHEET    1   A 2 GLU A  23  ASP A  26  0                                        
SHEET    2   A 2 HIS A  31  ALA A  34 -1  O  HIS A  31   N  ASP A  26           
SSBOND   1 CYS A   19    CYS A   32                          1555   1555  2.03  
SSBOND   2 CYS A   24    CYS A   35                          1555   1555  2.03  
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                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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