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HEADER APOPTOSIS 27-JUN-00 1E41 TITLE DEATH DOMAIN FROM HUMAN FADD/MORT1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FADD PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DEATH DOMAIN RESIDUES 93-192; COMPND 5 SYNONYM: FAS-ASSOCIATING DEATH DOMAIN-CONTAINING PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: T7; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET14B; SOURCE 8 OTHER_DETAILS: PCR CLONING INTO N-TERMINAL 6*HIS TAG SOURCE 9 THROMBIN-CLEAVABLE FUSION PROTEIN KEYWDS DEATH DOMAIN, ADAPTER MOLECULE, FAS RECEPTOR DEATH INDUCING KEYWDS 2 SIGNALLING COMPLEX EXPDTA NMR, 25 STRUCTURES AUTHOR P.C.DRISCOLL,H.BERGLUND,D.OLERENSHAW,N.Q.MCDONALD REVDAT 2 01-APR-03 1E41 1 JRNL REVDAT 1 06-NOV-00 1E41 0 JRNL AUTH H.BERGLUND,D.OLERENSHAW,A.SANKAR,M.FEDERWISCH, JRNL AUTH 2 N.Q.MCDONALD,P.C.DRISCOLL JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE AND JRNL TITL 2 DYNAMIC PROPERTIES OF THE HUMAN FADD DEATH DOMAIN. JRNL REF J.MOL.BIOL. V. 302 171 2000 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 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: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 1E41 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 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-4758 . REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE BUFFER, 150MM REMARK 210 NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS DOUBLE, TRIPLE REMARK 210 RESONANCES EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS 600 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN NMR INC. REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG, X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING FROM REMARK 210 RANDOM CHAIN STARTING CONF REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND REMARK 210 GOOD NON-BONDED CONTAC 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 ON 13C, 15N-LABELED FADD-DD. FULL DETAILS ARE REMARK 210 GIVEN IN BERGLUND ET AL., J. MOL. BIOL. (2000), IN PRESS 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O GLU A 95 N CYS A 98 2.16 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 2 SER A 90 157.40 60.25 REMARK 500 2 ASP A 96 -54.95 64.79 REMARK 500 4 ASP A 96 -53.45 68.23 REMARK 500 5 ASP A 96 -57.56 66.59 REMARK 500 6 ASP A 96 -61.50 63.28 REMARK 500 6 LYS A 120 39.16 118.83 REMARK 500 6 SER A 190 -89.02 55.56 REMARK 500 7 ASP A 96 -63.13 65.75 REMARK 500 7 SER A 190 -69.23 63.26 REMARK 500 8 ASP A 96 -57.57 66.64 REMARK 500 9 MET A 92 147.85 64.24 REMARK 500 9 ASP A 96 -54.26 67.28 REMARK 500 10 ASP A 96 -42.29 70.48 REMARK 500 11 ASP A 96 -54.37 66.80 REMARK 500 12 ASP A 96 -61.13 64.22 REMARK 500 13 ASP A 96 -56.73 66.65 REMARK 500 14 ASP A 96 -49.42 67.92 REMARK 500 15 ASP A 96 -49.15 67.31 REMARK 500 16 SER A 90 -96.05 43.79 REMARK 500 16 ASP A 96 -59.51 64.14 REMARK 500 17 SER A 90 -97.43 51.48 REMARK 500 17 ASP A 96 -51.90 65.17 REMARK 500 18 ASP A 96 -49.70 66.81 REMARK 500 18 LYS A 120 34.68 112.93 REMARK 500 18 ARG A 189 -92.06 31.57 REMARK 500 19 ASP A 96 -53.25 64.96 REMARK 500 20 HIS A 91 140.02 61.20 REMARK 500 20 ASP A 96 -54.32 43.32 REMARK 500 20 LYS A 120 35.56 121.11 REMARK 500 21 ASP A 96 -43.62 66.83 REMARK 500 22 ASP A 96 -45.03 67.41 REMARK 500 23 ASP A 96 -46.99 67.01 REMARK 500 23 THR A 157 152.05 125.92 REMARK 500 24 MET A 92 -74.05 64.50 REMARK 500 24 ASP A 96 -56.26 67.27 REMARK 500 25 ASP A 96 -53.29 68.47 REMARK 500 25 LYS A 120 37.18 113.22 DBREF 1E41 A 89 192 UNP Q13158 FADD_HUMAN 89 192 SEQADV 1E41 SER A 90 UNP Q13158 ALA 90 CONFLICT SEQADV 1E41 HIS A 91 UNP Q13158 ALA 91 CONFLICT SEQADV 1E41 MET A 92 UNP Q13158 PRO 92 CONFLICT SEQRES 1 A 104 GLY SER HIS MET GLY GLU GLU ASP LEU CYS ALA ALA PHE SEQRES 2 A 104 ASN VAL ILE CYS ASP ASN VAL GLY LYS ASP TRP ARG ARG SEQRES 3 A 104 LEU ALA ARG GLN LEU LYS VAL SER ASP THR LYS ILE ASP SEQRES 4 A 104 SER ILE GLU ASP ARG TYR PRO ARG ASN LEU THR GLU ARG SEQRES 5 A 104 VAL ARG GLU SER LEU ARG ILE TRP LYS ASN THR GLU LYS SEQRES 6 A 104 GLU ASN ALA THR VAL ALA HIS LEU VAL GLY ALA LEU ARG SEQRES 7 A 104 SER CYS GLN MET ASN LEU VAL ALA ASP LEU VAL GLN GLU SEQRES 8 A 104 VAL GLN GLN ALA ARG ASP LEU GLN ASN ARG SER GLY ALA HELIX 1 1 ASP A 96 ASN A 107 1 12 HELIX 2 2 ASP A 111 VAL A 121 1 11 HELIX 3 3 SER A 122 TYR A 133 1 12 HELIX 4 4 ASN A 136 LYS A 153 1 18 HELIX 5 5 GLU A 154 ALA A 156 5 3 HELIX 6 6 THR A 157 CYS A 168 1 12 HELIX 7 7 MET A 170 LEU A 186 1 17 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