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HEADER APOPTOSIS 26-AUG-99 1CWW TITLE SOLUTION STRUCTURE OF THE CASPASE RECRUITMENT DOMAIN (CARD) TITLE 2 FROM APAF-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOPTOTIC PROTEASE ACTIVATING FACTOR 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CASPASE RECRUITMENT DOMAIN; COMPND 5 SYNONYM: CARD OF APAF-1; COMPND 6 ENGINEERED: 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_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX 6P-3 KEYWDS HELICAL BUNDLE EXPDTA NMR, 20 STRUCTURES AUTHOR C.L.DAY,C.DUPONT,M.LACKMANN,D.L.VAUX,M.G.HINDS REVDAT 1 21-JAN-00 1CWW 0 JRNL AUTH C.L.DAY,C.DUPONT,M.LACKMANN,D.L.VAUX,M.G.HINDS JRNL TITL SOLUTION STRUCTURE AND MUTAGENESIS OF THE CASPASE JRNL TITL 2 RECRUITMENT DOMAIN (CARD) FROM APAF-1. JRNL REF CELL DEATH DIFFER. V. 6 1125 1999 JRNL REFN UK ISSN 1350-9047 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: THE STRUCTURES ARE BASED ON A TOTAL REMARK 3 OF 2314 NOE-DERIVED DISTANCE CONSTRAINTS, 31 HYDROGEN BOND REMARK 3 CONSTRAINTS AND 173 DIHEDRAL ANGLE CONSTRAINTS. REMARK 4 REMARK 4 1CWW 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 (2007-03-16) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB009593. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 30; 30; 30 REMARK 210 PH : 6.7; 6.7; 6.7 REMARK 210 IONIC STRENGTH : NULL; NULL; NULL REMARK 210 PRESSURE : NULL; NULL; NULL REMARK 210 SAMPLE CONTENTS : UNLABELLED 1.5MM APAF-1 CARD REMARK 210 20MM SODIUM PHOSPHATE PH 6.7 REMARK 210 75MM NACL 2MM DITHIOTHREITOL; REMARK 210 U-15N 1.5MM APAF-1 CARD 20MM REMARK 210 SODIUM PHOSPHATE PH 6.7 75MM REMARK 210 NACL 2MM DITHIOTHREITOL; U- REMARK 210 15N; U-13C 1.5MM APAF-1 CARD REMARK 210 20MM SODIUM PHOSPHATE PH 6.7 REMARK 210 75MM NACL 2MM DITHIOTHREITOL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 3D_15N-SEPARATED_ REMARK 210 NOESY, HNHA, 3D_13C-SEPARATED_ REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ, 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX, DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13, REMARK 210 DYANA 1.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY TORSION REMARK 210 ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 250 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, REMARK 210 STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 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: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 4 GLY A -5 N GLY A -5 CA 0.035 REMARK 500 8 GLY A -5 N GLY A -5 CA 0.037 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 PRO A 47 N - CA - C ANGL. DEV. = 5.4 DEGREES REMARK 500 10 PRO A 47 N - CA - C ANGL. DEV. = 6.4 DEGREES REMARK 500 20 LEU A 83 N - CA - C ANGL. DEV. = -5.7 DEGREES 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 SER A 95 -70.68 77.35 REMARK 500 2 SER A 23 -101.94 29.09 REMARK 500 2 SER A 95 -62.79 74.56 REMARK 500 3 SER A 23 -111.86 49.21 REMARK 500 5 SER A 23 -101.36 30.45 REMARK 500 6 SER A 23 -107.57 44.48 REMARK 500 9 SER A 23 -106.92 40.13 REMARK 500 11 SER A 23 -100.55 26.41 REMARK 500 17 SER A 23 -91.94 31.78 REMARK 500 19 SER A 23 -109.16 39.56 DBREF 1CWW A 1 97 UNP O14727 APAF_HUMAN 1 97 SEQADV 1CWW GLY A -5 UNP O14727 EXPRESSION ARTIFACT SEQADV 1CWW PRO A -4 UNP O14727 EXPRESSION ARTIFACT SEQADV 1CWW LEU A -3 UNP O14727 EXPRESSION ARTIFACT SEQADV 1CWW GLY A -2 UNP O14727 EXPRESSION ARTIFACT SEQADV 1CWW SER A -1 UNP O14727 EXPRESSION ARTIFACT SEQRES 1 A 102 GLY PRO LEU GLY SER MET ASP ALA LYS ALA ARG ASN CYS SEQRES 2 A 102 LEU LEU GLN HIS ARG GLU ALA LEU GLU LYS ASP ILE LYS SEQRES 3 A 102 THR SER TYR ILE MET ASP HIS MET ILE SER ASP GLY PHE SEQRES 4 A 102 LEU THR ILE SER GLU GLU GLU LYS VAL ARG ASN GLU PRO SEQRES 5 A 102 THR GLN GLN GLN ARG ALA ALA MET LEU ILE LYS MET ILE SEQRES 6 A 102 LEU LYS LYS ASP ASN ASP SER TYR VAL SER PHE TYR ASN SEQRES 7 A 102 ALA LEU LEU HIS GLU GLY TYR LYS ASP LEU ALA ALA LEU SEQRES 8 A 102 LEU HIS ASP GLY ILE PRO VAL VAL SER SER SER HELIX 1 1 ASP A 2 GLN A 11 1 10 HELIX 2 2 ALA A 15 ILE A 20 1 6 HELIX 3 3 THR A 22 ASP A 32 1 11 HELIX 4 4 THR A 36 GLU A 46 1 11 HELIX 5 5 THR A 48 LEU A 61 1 14 HELIX 6 6 ASP A 64 GLU A 78 1 15 HELIX 7 7 TYR A 80 ASP A 89 1 10 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