HEADER APOPTOSIS 01-APR-01 1ICH TITLE SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 TITLE 2 DEATH DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DEATH DOMAIN; COMPND 5 SYNONYM: TNF-1; 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_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE) PLYS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSET(T7) KEYWDS DEATH DOMAIN EXPDTA NMR AUTHOR S.F.SUKITS,L.-L.LIN,K.MALAKIAN,R.POWERS,G.-Y.XU REVDAT 2 01-APR-03 1ICH 1 JRNL REVDAT 1 01-APR-02 1ICH 0 JRNL AUTH S.F.SUKITS,L.L.LIN,S.HSU,K.MALAKIAN,R.POWERS,G.Y.XU JRNL TITL SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR JRNL TITL 2 RECEPTOR-1 DEATH DOMAIN. JRNL REF J.MOL.BIOL. V. 310 895 2001 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 9.8 REMARK 3 AUTHORS : BADGER, J., KUMAR, R.A., YIP, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE BASED ON A TOTAL REMARK 3 OF 1167 DISTANCE CONSTRAINTS FROM NOE AND H-BOND, 117 DIHEDRAL REMARK 3 ANGLE CONSTRAINTS FROM 3D HNHA AND TALOS PROGRAM AND 81 PAIRS REMARK 3 OF CA/CB CHEMICAL SHIFT CONTRAINTS. REMARK 4 REMARK 4 1ICH 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 RCSB013155. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : 10 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM SAMPLE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_ REMARK 210 13C-SEPARATED_NOESY, 4D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 9.8, NMRPIPE 1.8, REMARK 210 2000, PIPP 4.2.2, 1998 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS 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: THE STRUCTURE WAS DETERMININED USING 3D TRIPLE- REMARK 210 RESONANCE EXPERIMENTS WITH THE ENHANCED-SENSITIVITY PULSE REMARK 210 FIELD GRADIENT APPROACH. 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 MET A 315 REMARK 465 ALA A 316 REMARK 465 HIS A 317 REMARK 465 LYS A 318 REMARK 465 PRO A 319 REMARK 465 GLN A 320 REMARK 465 SER A 321 REMARK 465 LEU A 322 REMARK 465 ASP A 323 REMARK 465 THR A 324 REMARK 465 ASP A 325 REMARK 465 ASP A 326 REMARK 465 GLY A 414 REMARK 465 PRO A 415 REMARK 465 ALA A 416 REMARK 465 ALA A 417 REMARK 465 LEU A 418 REMARK 465 PRO A 419 REMARK 465 PRO A 420 REMARK 465 ALA A 421 REMARK 465 PRO A 422 REMARK 465 SER A 423 REMARK 465 LEU A 424 REMARK 465 LEU A 425 REMARK 465 ARG A 426 DBREF 1ICH A 316 426 UNP P19438 TNR1A_HUMAN 345 455 SEQADV 1ICH MET A 315 UNP P19438 INITIATING METHIONINE SEQADV 1ICH LYS A 347 UNP P19438 ARG 376 ENGINEERED SEQRES 1 A 112 MET ALA HIS LYS PRO GLN SER LEU ASP THR ASP ASP PRO SEQRES 2 A 112 ALA THR LEU TYR ALA VAL VAL GLU ASN VAL PRO PRO LEU SEQRES 3 A 112 ARG TRP LYS GLU PHE VAL LYS ARG LEU GLY LEU SER ASP SEQRES 4 A 112 HIS GLU ILE ASP ARG LEU GLU LEU GLN ASN GLY ARG CYS SEQRES 5 A 112 LEU ARG GLU ALA GLN TYR SER MET LEU ALA THR TRP ARG SEQRES 6 A 112 ARG ARG THR PRO ARG ARG GLU ALA THR LEU GLU LEU LEU SEQRES 7 A 112 GLY ARG VAL LEU ARG ASP MET ASP LEU LEU GLY CYS LEU SEQRES 8 A 112 GLU ASP ILE GLU GLU ALA LEU CYS GLY PRO ALA ALA LEU SEQRES 9 A 112 PRO PRO ALA PRO SER LEU LEU ARG HELIX 1 1 PRO A 327 VAL A 337 1 11 HELIX 2 2 ARG A 341 GLY A 350 1 10 HELIX 3 3 SER A 352 ASN A 363 1 12 HELIX 4 4 CYS A 366 THR A 382 1 17 HELIX 5 5 ALA A 387 MET A 399 1 13 HELIX 6 6 LEU A 401 CYS A 413 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