HEADER APOPTOSIS 23-MAR-99 1FAD TITLE DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, TITLE 2 RESIDUES 89-183 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (FADD PROTEIN); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DEATH DOMAIN (RESIDUES 89-183); COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: N-TERMINAL EXTENSION OF GLY-SER-HIS-MET COMPND 8 FROM CLONING ARTIFACT. COORDINATES ARE NOT SHOWN FOR COMPND 9 ARTIFACT. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS APOPTOSIS, FADD, DEATH DOMAIN EXPDTA NMR, 21 STRUCTURES AUTHOR E.-J.JEONG,S.BANG,T.H.LEE,Y.-I.PARK,W.-S.SIM,K.-S.KIM REVDAT 2 01-APR-03 1FAD 1 JRNL REVDAT 1 06-JUL-99 1FAD 0 JRNL AUTH E.J.JEONG,S.BANG,T.H.LEE,Y.I.PARK,W.S.SIM,K.S.KIM JRNL TITL THE SOLUTION STRUCTURE OF FADD DEATH DOMAIN. JRNL TITL 2 STRUCTURAL BASIS OF DEATH DOMAIN INTERACTIONS OF JRNL TITL 3 FAS AND FADD. JRNL REF J.BIOL.CHEM. V. 274 16337 1999 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.ZHANG,A.WINOTO REMARK 1 TITL A MOUSE FAS-ASSOCIATED PROTEIN WITH HOMOLOGY TO REMARK 1 TITL 2 THE HUMAN MORT1/FADD IS ESSENTIAL FOR FAS-INDUCED REMARK 1 TITL 3 APOPTOSIS REMARK 1 REF MOL.CELL.BIOL. V. 16 2756 1996 REMARK 1 REFN ASTM MCEBD4 US ISSN 0270-7306 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FAD 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 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000704. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 2 MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-15N-HSQC-NOESY, 3D-13C, REMARK 210 15N-EDITED NOESY, 13C-HCCH- REMARK 210 TOCSY, 3D-15N-HSQC-TOCSY, 3D- REMARK 210 HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ, 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS600, INOVA500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY AND REMARK 210 SIMMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21 REMARK 210 REMARK 210 REMARK: DISTANCE CONSTRAINTS ARE DERIVED FROM THE 3D-13C, 15N- REMARK 210 EDITED NOESY. J-COUPLING CONSTANTS FROM HNHA AND 13C CHEMICAL REMARK 210 SHIFTS WERE USED AS CONTRAINTS. DURING THE REFINEMENT, REMARK 210 DATABASE POTENTIAL WAS USED. 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. (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 1 GLY A 85 REMARK 465 1 SER A 86 REMARK 465 1 HIS A 87 REMARK 465 1 MET A 88 REMARK 465 2 GLY A 85 REMARK 465 2 SER A 86 REMARK 465 2 HIS A 87 REMARK 465 2 MET A 88 REMARK 465 3 GLY A 85 REMARK 465 3 SER A 86 REMARK 465 3 HIS A 87 REMARK 465 3 MET A 88 REMARK 465 4 GLY A 85 REMARK 465 4 SER A 86 REMARK 465 4 HIS A 87 REMARK 465 4 MET A 88 REMARK 465 5 GLY A 85 REMARK 465 5 SER A 86 REMARK 465 5 HIS A 87 REMARK 465 5 MET A 88 REMARK 465 6 GLY A 85 REMARK 465 6 SER A 86 REMARK 465 6 HIS A 87 REMARK 465 6 MET A 88 REMARK 465 7 GLY A 85 REMARK 465 7 SER A 86 REMARK 465 7 HIS A 87 REMARK 465 7 MET A 88 REMARK 465 8 GLY A 85 REMARK 465 8 SER A 86 REMARK 465 8 HIS A 87 REMARK 465 8 MET A 88 REMARK 465 9 GLY A 85 REMARK 465 9 SER A 86 REMARK 465 9 HIS A 87 REMARK 465 9 MET A 88 REMARK 465 10 GLY A 85 REMARK 465 10 SER A 86 REMARK 465 10 HIS A 87 REMARK 465 10 MET A 88 REMARK 465 11 GLY A 85 REMARK 465 11 SER A 86 REMARK 465 11 HIS A 87 REMARK 465 11 MET A 88 REMARK 465 12 GLY A 85 REMARK 465 12 SER A 86 REMARK 465 12 HIS A 87 REMARK 465 12 MET A 88 REMARK 465 13 GLY A 85 REMARK 465 13 SER A 86 REMARK 465 13 HIS A 87 REMARK 465 13 MET A 88 REMARK 465 14 GLY A 85 REMARK 465 14 SER A 86 REMARK 465 14 HIS A 87 REMARK 465 14 MET A 88 REMARK 465 15 GLY A 85 REMARK 465 15 SER A 86 REMARK 465 15 HIS A 87 REMARK 465 15 MET A 88 REMARK 465 16 GLY A 85 REMARK 465 16 SER A 86 REMARK 465 16 HIS A 87 REMARK 465 16 MET A 88 REMARK 465 17 GLY A 85 REMARK 465 17 SER A 86 REMARK 465 17 HIS A 87 REMARK 465 17 MET A 88 REMARK 465 18 GLY A 85 REMARK 465 18 SER A 86 REMARK 465 18 HIS A 87 REMARK 465 18 MET A 88 REMARK 465 19 GLY A 85 REMARK 465 19 SER A 86 REMARK 465 19 HIS A 87 REMARK 465 19 MET A 88 REMARK 465 20 GLY A 85 REMARK 465 20 SER A 86 REMARK 465 20 HIS A 87 REMARK 465 20 MET A 88 REMARK 465 21 GLY A 85 REMARK 465 21 SER A 86 REMARK 465 21 HIS A 87 REMARK 465 21 MET A 88 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 1 LYS A 153 -104.15 54.89 REMARK 500 1 GLU A 182 -59.80 64.91 REMARK 500 8 GLU A 182 -58.55 66.36 REMARK 500 12 GLU A 182 -57.45 65.40 REMARK 500 14 LYS A 153 -92.11 54.69 REMARK 500 19 LYS A 153 -91.85 53.81 REMARK 500 20 LYS A 153 -114.71 52.72 DBREF 1FAD A 89 183 UNP Q61160 FADD_MOUSE 89 183 SEQADV 1FAD TYR A 96 UNP Q61160 ASP 96 ENGINEERED MUTATION SEQADV 1FAD GLY A 85 UNP Q61160 CLONING ARTIFACT SEQADV 1FAD SER A 86 UNP Q61160 CLONING ARTIFACT SEQADV 1FAD HIS A 87 UNP Q61160 CLONING ARTIFACT SEQADV 1FAD MET A 88 UNP Q61160 CLONING ARTIFACT SEQRES 1 A 99 GLY SER HIS MET ALA ALA PRO PRO GLY GLU ALA TYR LEU SEQRES 2 A 99 GLN VAL ALA PHE ASP ILE VAL CYS ASP ASN VAL GLY ARG SEQRES 3 A 99 ASP TRP LYS ARG LEU ALA ARG GLU LEU LYS VAL SER GLU SEQRES 4 A 99 ALA LYS MET ASP GLY ILE GLU GLU LYS TYR PRO ARG SER SEQRES 5 A 99 LEU SER GLU ARG VAL ARG GLU SER LEU LYS VAL TRP LYS SEQRES 6 A 99 ASN ALA GLU LYS LYS ASN ALA SER VAL ALA GLY LEU VAL SEQRES 7 A 99 LYS ALA LEU ARG THR CYS ARG LEU ASN LEU VAL ALA ASP SEQRES 8 A 99 LEU VAL GLU GLU ALA GLN GLU SER HELIX 1 1 GLU A 94 LEU A 119 1 26 HELIX 2 2 GLU A 123 LYS A 132 1 10 HELIX 3 3 LEU A 137 ALA A 156 1 20 HELIX 4 4 VAL A 158 CYS A 168 1 11 HELIX 5 5 ASN A 171 GLN A 181 1 11 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