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HEADER APOPTOSIS 16-APR-03 1UCP TITLE NMR STRUCTURE OF THE PYRIN DOMAIN OF HUMAN ASC COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOPTOSIS-ASSOCIATED SPECK-LIKE PROTEIN COMPND 3 CONTAINING A CARD; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: PYRIN DOMAIN; COMPND 6 SYNONYM: PYCARD, ASC; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 TISSUE: LYMPHOCYTES; SOURCE 5 GENE: ASC; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30 KEYWDS DEATH DOMAIN FOLD EXPDTA NMR, 20 STRUCTURES AUTHOR E.LIEPINSH,R.BARBALS,E.DAHL,A.SHARIPO,E.STAUB,G.OTTING REVDAT 1 04-NOV-03 1UCP 0 JRNL AUTH E.LIEPINSH,R.BARBALS,E.DAHL,A.SHARIPO,E.STAUB, JRNL AUTH 2 G.OTTING JRNL TITL THE DEATH-DOMAIN FOLD OF THE ASC PYRIN DOMAIN, JRNL TITL 2 PRESENTING A BASIS FOR PYRIN/PYRIN RECOGNITION JRNL REF J.MOL.BIOL. V. 332 1155 2003 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 : OPAL 2.6 REMARK 3 AUTHORS : JONES,ZOU,COWAN,KJELDGAARD REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1118 NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS, 206 COUPLING CONSTANTS REMARK 4 REMARK 4 1UCP 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005681. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 301 REMARK 210 PH : 3.7 REMARK 210 IONIC STRENGTH : 50MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PYRIN DOMAIN; 1MM PYRIN REMARK 210 DOMAIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 2D TOCSY, W1- REMARK 210 DECOUPLED NOESY, DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,TARGET REMARK 210 FUNCTION 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: 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 MET A 1 GLY A 2 6 142.12 REMARK 500 MET A 1 GLY A 2 10 -145.41 REMARK 500 MET A 1 GLY A 2 20 149.60 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5780 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFTS DBREF 1UCP A 1 91 UNP Q9ULZ3 ASC_HUMAN 1 91 SEQRES 1 A 91 MET GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU SEQRES 2 A 91 ASN LEU THR ALA GLU GLU LEU LYS LYS PHE LYS LEU LYS SEQRES 3 A 91 LEU LEU SER VAL PRO LEU ARG GLU GLY TYR GLY ARG ILE SEQRES 4 A 91 PRO ARG GLY ALA LEU LEU SER MET ASP ALA LEU ASP LEU SEQRES 5 A 91 THR ASP LYS LEU VAL SER PHE TYR LEU GLU THR TYR GLY SEQRES 6 A 91 ALA GLU LEU THR ALA ASN VAL LEU ARG ASP MET GLY LEU SEQRES 7 A 91 GLN GLU MET ALA GLY GLN LEU GLN ALA ALA THR HIS GLN HELIX 1 1 GLY A 2 LEU A 15 1 14 HELIX 2 2 THR A 16 LEU A 27 1 12 HELIX 3 3 PRO A 40 MET A 47 1 8 HELIX 4 4 ASP A 48 PHE A 59 1 12 HELIX 5 5 LEU A 61 MET A 76 1 16 HELIX 6 6 GLN A 79 GLN A 91 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 MODEL 1