HEADER CASPASE RECRUITMENT DOMAIN 24-JUL-98 3CRD TITLE NMR STRUCTURE OF THE RAIDD CARD DOMAIN, 15 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAIDD; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CARD DOMAIN; COMPND 5 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_VECTOR: PET23B; SOURCE 6 OTHER_DETAILS: HHHHHH HISTIDINE TAG WAS ADDED AT THE C- SOURCE 7 TERMINUS FOR EASE OF PURIFICATION KEYWDS CASPASE RECRUITMENT DOMAIN, APOPTOSIS, HOMOPHILIC KEYWDS 2 INTERACTION EXPDTA NMR, 15 STRUCTURES AUTHOR J.J.CHOU,H.MATSUO,H.DUAN,G.WAGNER REVDAT 2 16-FEB-99 3CRD 3 ATOM REMARK TITLE JRNL REVDAT 1 02-FEB-99 3CRD 0 JRNL AUTH J.J.CHOU,H.MATSUO,H.DUAN,G.WAGNER JRNL TITL SOLUTION STRUCTURE OF THE RAIDD CARD AND MODEL FOR JRNL TITL 2 CARD/CARD INTERACTION IN CASPASE-2 AND CASPASE-9 JRNL TITL 3 RECRUITMENT. JRNL REF CELL V. 94 171 1998 JRNL REFN ASTM CELLB5 US ISSN 0092-8674 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 3CRD 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 (2007-03-18) REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 8.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : TRIS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H, 13C, 15N), 15N REMARK 210 TOCSY-HSQC, 2D TOCSY, REMARK 210 HCCHTOCSY, HNCA, HN(CO)CA, REMARK 210 HNCACB, HN(CO)CACB, HNCO, REMARK 210 HN(CA)CO REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ, 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS750, UNITY500, REMARK 210 UNITYPLUS500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND REMARK 210 LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 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: 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 5 LYS A 88 N LYS A 88 CA -0.031 REMARK 500 6 LYS A 88 N LYS A 88 CA -0.032 REMARK 500 8 LYS A 88 N LYS A 88 CA -0.032 REMARK 500 14 LYS A 88 N LYS A 88 CA -0.031 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 5 ARG A 90 N - CA - C ANGL. DEV. = -4.3 DEGREES REMARK 500 6 ARG A 90 N - CA - C ANGL. DEV. = -4.4 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 2 LEU A 21 161.41 72.14 REMARK 500 2 THR A 48 -58.55 67.52 REMARK 500 3 VAL A 20 152.71 66.47 REMARK 500 4 ARG A 4 -59.03 73.51 REMARK 500 4 THR A 48 -67.98 60.62 REMARK 500 5 THR A 48 -61.49 67.31 REMARK 500 6 VAL A 20 139.28 70.40 REMARK 500 6 THR A 48 -72.59 65.54 REMARK 500 7 THR A 48 -60.24 67.42 REMARK 500 8 VAL A 20 161.82 52.38 REMARK 500 8 THR A 48 -75.03 56.65 REMARK 500 9 THR A 48 -73.61 58.10 REMARK 500 10 THR A 48 -59.11 72.04 REMARK 500 11 THR A 48 -64.48 63.03 REMARK 500 12 GLU A 23 131.70 72.10 REMARK 500 12 THR A 48 -64.78 61.22 REMARK 500 12 THR A 95 136.50 72.23 REMARK 500 12 ALA A 99 -67.01 65.99 REMARK 500 13 ARG A 4 -64.88 74.03 REMARK 500 13 THR A 48 -66.58 64.59 REMARK 500 14 VAL A 22 120.15 85.16 REMARK 500 15 ARG A 4 -66.43 66.94 REMARK 500 15 THR A 48 -79.41 63.37 DBREF 3CRD A 1 100 UNP P78560 CRADD_HUMAN 1 100 SEQRES 1 A 100 MET GLU ALA ARG ASP LYS GLN VAL LEU ARG SER LEU ARG SEQRES 2 A 100 LEU GLU LEU GLY ALA GLU VAL LEU VAL GLU GLY LEU VAL SEQRES 3 A 100 LEU GLN TYR LEU TYR GLN GLU GLY ILE LEU THR GLU ASN SEQRES 4 A 100 HIS ILE GLN GLU ILE ASN ALA GLN THR THR GLY LEU ARG SEQRES 5 A 100 LYS THR MET LEU LEU LEU ASP ILE LEU PRO SER ARG GLY SEQRES 6 A 100 PRO LYS ALA PHE ASP THR PHE LEU ASP SER LEU GLN GLU SEQRES 7 A 100 PHE PRO TRP VAL ARG GLU LYS LEU LYS LYS ALA ARG GLU SEQRES 8 A 100 GLU ALA MET THR ASP LEU PRO ALA GLY HELIX 1 1 ASP A 5 ALA A 18 1 14 HELIX 2 2 LEU A 27 GLU A 33 1 7 HELIX 3 3 GLU A 38 ILE A 44 1 7 HELIX 4 4 LEU A 51 ILE A 60 1 10 HELIX 5 5 PHE A 69 SER A 75 1 7 HELIX 6 6 PHE A 79 GLU A 92 1 14 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