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