PDB entry 1ddf

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HEADER    DEATH DOMAIN                            08-NOV-96   1DDF              
TITLE     FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAS;                                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGAN: FETAL LIVER;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HMS174 (DE3);                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET30B;                                    
SOURCE   8 OTHER_DETAILS: METHIONINE RESIDUE ADDED TO N-TERMINUS, AN            
SOURCE   9 LEHHHHHH HISTIDINE TAG WAS ADDED AT THE C-TERMINUS FOR               
SOURCE  10 EASE OF PURIFICATION                                                 
KEYWDS    DEATH DOMAIN, APOPTOSIS, RECEPTOR, GLYCOPROTEIN,                      
KEYWDS   2 TRANSMEMBRANE                                                        
EXPDTA    NMR                                                                   
AUTHOR    B.HUANG,M.EBERSTADT,E.OLEJNICZAK,R.P.MEADOWS,S.FESIK                  
REVDAT   1   12-NOV-97 1DDF    0                                                
JRNL        AUTH   B.HUANG,M.EBERSTADT,E.T.OLEJNICZAK,R.P.MEADOWS,              
JRNL        AUTH 2 S.W.FESIK                                                    
JRNL        TITL   NMR STRUCTURE AND MUTAGENESIS OF THE FAS                     
JRNL        TITL 2 (APO-1/CD95) DEATH DOMAIN.                                   
JRNL        REF    NATURE                        V. 384   638 1996              
JRNL        REFN   ASTM NATUAS  UK ISSN 0028-0836                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DDF COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006                         
REMARK   4                                                                      
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.                    
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-16)                     
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : 4.0                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
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 : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 203      169.12     57.57                                   
REMARK 500    ILE A 206      161.24     66.09                                   
REMARK 500    ASN A 239      125.77     65.90                                   
REMARK 500    GLN A 316      -91.55   -179.20                                   
DBREF  1DDF A  202   319  UNP    P25445   TNR6_HUMAN     218    335             
SEQRES   1 A  127  MET GLU THR VAL ALA ILE ASN LEU SER ASP VAL ASP LEU          
SEQRES   2 A  127  SER LYS TYR ILE THR THR ILE ALA GLY VAL MET THR LEU          
SEQRES   3 A  127  SER GLN VAL LYS GLY PHE VAL ARG LYS ASN GLY VAL ASN          
SEQRES   4 A  127  GLU ALA LYS ILE ASP GLU ILE LYS ASN ASP ASN VAL GLN          
SEQRES   5 A  127  ASP THR ALA GLU GLN LYS VAL GLN LEU LEU ARG ASN TRP          
SEQRES   6 A  127  HIS GLN LEU HIS GLY LYS LYS GLU ALA TYR ASP THR LEU          
SEQRES   7 A  127  ILE LYS ASP LEU LYS LYS ALA ASN LEU CYS THR LEU ALA          
SEQRES   8 A  127  GLU LYS ILE GLN THR ILE ILE LEU LYS ASP ILE THR SER          
SEQRES   9 A  127  ASP SER GLU ASN SER ASN PHE ARG ASN GLU ILE GLN SER          
SEQRES  10 A  127  LEU VAL LEU GLU HIS HIS HIS HIS HIS HIS                      
HELIX    1   1 TYR A  216  VAL A  223  1                                   8    
HELIX    2   2 LEU A  226  ASN A  236  1                                  11    
HELIX    3   3 GLU A  240  ASN A  250  1                                  11    
HELIX    4   4 GLN A  257  LEU A  268  1                                  12    
HELIX    5   5 ALA A  274  LYS A  284  1                                  11    
HELIX    6   6 LEU A  290  ILE A  302  1                                  13    
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