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HEADER APOPTOSIS 21-MAR-06 2GF5 TITLE STRUCTURE OF INTACT FADD (MORT1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FADD PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FAS-ASSOCIATING DEATH DOMAIN-CONTAINING PROTEIN, COMPND 5 MEDIATOR OF RECEPTOR INDUCED TOXICITY; 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 GENE: FADD, MORT1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE50 KEYWDS DEATH DOMAIN, DEATH EFFECTOR DOMAIN, APOPTOSIS, DEATH- KEYWDS 2 INDUCING SIGNALING COMPLEX EXPDTA NMR, 25 STRUCTURES AUTHOR P.E.CARRINGTON,C.SANDU,Y.WEI,J.M.HILL,G.MORISAWA,T.HUANG, AUTHOR 2 E.GAVATHIOTIS,Y.WEI,M.H.WERNER REVDAT 1 27-JUN-06 2GF5 0 JRNL AUTH P.E.CARRINGTON,C.SANDU,Y.WEI,J.M.HILL,G.MORISAWA, JRNL AUTH 2 T.HUANG,E.GAVATHIOTIS,Y.WEI,M.H.WERNER JRNL TITL THE STRUCTURE OF FADD AND ITS MODE OF INTERACTION JRNL TITL 2 WITH PROCASPASE-8 JRNL REF MOL. CELL V. 22 599 2006 JRNL REFN ASTM MOCEFL US ISSN 1097-2765 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 2.12.2 REMARK 3 AUTHORS : BRUNGER ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: WATER REFINEMENT REMARK 4 REMARK 4 2GF5 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 RCSB037040. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 200MM PHOSPHATE REMARK 210 PRESSURE : 1ATM REMARK 210 SAMPLE CONTENTS : 200MM PHOSPHATE BUFFER, 95% REMARK 210 H2O 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED NOESY, 13C-EDITED REMARK 210 NOESY, CBCA(CO)NH, HNCA, C(CO) REMARK 210 NH, H(CCO)NH, HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 2.12.2 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : 25 STRUCTURES FOR LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 1 ARG A 71 -42.37 86.20 REMARK 500 7 ARG A 71 -35.62 78.41 REMARK 500 14 ARG A 71 -34.95 84.06 REMARK 500 19 ARG A 71 -34.75 75.73 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ALA A 87 ALA A 88 2 147.18 REMARK 500 LYS A 120 VAL A 121 2 139.15 REMARK 500 SER A 1 ASP A 2 4 -136.54 REMARK 500 GLN A 40 SER A 41 4 -138.28 REMARK 500 GLY A 89 ALA A 90 4 149.71 REMARK 500 LYS A 110 ASP A 111 4 -144.78 REMARK 500 GLU A 152 LYS A 153 4 145.80 REMARK 500 ASP A 2 PRO A 3 5 133.74 REMARK 500 GLN A 40 SER A 41 5 -148.07 REMARK 500 LYS A 110 ASP A 111 5 -144.39 REMARK 500 SER A 1 ASP A 2 6 -142.07 REMARK 500 ALA A 88 GLY A 89 7 -149.59 REMARK 500 GLN A 40 SER A 41 8 -145.08 REMARK 500 ASN A 136 LEU A 137 8 146.22 REMARK 500 LYS A 110 ASP A 111 9 -146.51 REMARK 500 ASP A 111 TRP A 112 11 145.65 REMARK 500 ALA A 91 PRO A 92 12 -149.38 REMARK 500 SER A 1 ASP A 2 13 -149.92 REMARK 500 LYS A 120 VAL A 121 15 148.70 REMARK 500 ASP A 2 PRO A 3 16 145.93 REMARK 500 ALA A 88 GLY A 89 17 -144.75 REMARK 500 LYS A 110 ASP A 111 18 -142.21 REMARK 500 PRO A 57 GLY A 58 19 146.69 REMARK 500 ALA A 91 PRO A 92 19 -145.19 REMARK 500 ALA A 87 ALA A 88 21 147.85 REMARK 500 GLY A 85 ALA A 86 23 -149.47 REMARK 500 LYS A 110 ASP A 111 23 -136.42 REMARK 500 GLN A 40 SER A 41 24 -149.52 REMARK 500 TYR A 133 PRO A 134 24 -148.84 REMARK 500 SER A 1 ASP A 2 25 -149.68 REMARK 500 LYS A 110 ASP A 111 25 -140.18 REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED DBREF 2GF5 A 2 191 UNP Q13158 FADD_HUMAN 2 191 SEQADV 2GF5 SER A 1 UNP Q13158 CLONING ARTIFACT SEQADV 2GF5 TYR A 25 UNP Q13158 PHE 25 ENGINEERED SEQRES 1 A 191 SER ASP PRO PHE LEU VAL LEU LEU HIS SER VAL SER SER SEQRES 2 A 191 SER LEU SER SER SER GLU LEU THR GLU LEU LYS TYR LEU SEQRES 3 A 191 CYS LEU GLY ARG VAL GLY LYS ARG LYS LEU GLU ARG VAL SEQRES 4 A 191 GLN SER GLY LEU ASP LEU PHE SER MET LEU LEU GLU GLN SEQRES 5 A 191 ASN ASP LEU GLU PRO GLY HIS THR GLU LEU LEU ARG GLU SEQRES 6 A 191 LEU LEU ALA SER LEU ARG ARG HIS ASP LEU LEU ARG ARG SEQRES 7 A 191 VAL ASP ASP PHE GLU ALA GLY ALA ALA ALA GLY ALA ALA SEQRES 8 A 191 PRO GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE SEQRES 9 A 191 CYS ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG SEQRES 10 A 191 GLN LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU SEQRES 11 A 191 ASP ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SEQRES 12 A 191 SER LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA SEQRES 13 A 191 THR VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN SEQRES 14 A 191 MET ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN SEQRES 15 A 191 ALA ARG ASP LEU GLN ASN ARG SER GLY HELIX 1 1 ASP A 2 SER A 13 1 12 HELIX 2 2 SER A 16 CYS A 27 1 12 HELIX 3 3 GLY A 32 VAL A 39 1 8 HELIX 4 4 GLY A 42 GLN A 52 1 11 HELIX 5 5 THR A 60 LEU A 70 1 11 HELIX 6 6 ARG A 72 GLY A 85 1 14 HELIX 7 7 GLY A 93 ASN A 107 1 15 HELIX 8 8 ASP A 111 LEU A 119 1 9 HELIX 9 9 SER A 122 TYR A 133 1 12 HELIX 10 10 LEU A 137 GLU A 152 1 16 HELIX 11 11 THR A 157 GLN A 169 1 13 HELIX 12 12 MET A 170 GLY A 191 1 22 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