HEADER APOPTOSIS 11-JUL-06 2HM2
TITLE SOLUTION STRUCTURE OF ASC2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIN-ONLY PROTEIN 1;
COMPND 3 CHAIN: Q;
COMPND 4 FRAGMENT: PYRIN DOMAIN;
COMPND 5 SYNONYM: ASC2; PYRIN DOMAIN CONTAINING 1; PAAD-ONLY
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POP1, PYDC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-30
KEYWDS PYRIN DOMAIN, SIX HELIX BUNDLE, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.NATARAJAN,R.GHOSE,J.M.HILL
REVDAT 4 24-FEB-09 2HM2 1 VERSN
REVDAT 3 12-DEC-06 2HM2 1 JRNL
REVDAT 2 28-NOV-06 2HM2 1 JRNL
REVDAT 1 25-JUL-06 2HM2 0
JRNL AUTH A.NATARAJAN,R.GHOSE,J.M.HILL
JRNL TITL STRUCTURE AND DYNAMICS OF ASC2, A PYRIN
JRNL TITL 2 DOMAIN-ONLY PROTEIN THAT REGULATES INFLAMMATORY
JRNL TITL 3 SIGNALING
JRNL REF J.BIOL.CHEM. V. 281 31863 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16905547
JRNL DOI 10.1074/JBC.M605458200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.11.2
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 1778 NMR-DERIVED RESTRAINTS, INCLUDING 1338 NOES, 197
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 73 3J(NH-HA) COUPLING CONSTANTS AND
REMARK 3 170 13CA/CB SECONDARY SHIFT RESTRAINTS
REMARK 4
REMARK 4 2HM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038502.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE AND
REMARK 210 140 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM ASC2 U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS DOUBLE AND TRIPLE
REMARK 210 RESONANCE EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
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,
REMARK 210 STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO Q 17 -37.29 -32.20
REMARK 500 1 GLU Q 34 -95.24 -32.86
REMARK 500 1 PRO Q 40 146.08 -39.95
REMARK 500 1 TYR Q 61 152.37 77.56
REMARK 500 1 ALA Q 88 48.26 -73.53
REMARK 500 2 THR Q 29 -50.76 -125.67
REMARK 500 2 PRO Q 31 147.52 -39.34
REMARK 500 2 ARG Q 33 -178.37 -69.36
REMARK 500 2 GLU Q 34 -94.10 25.29
REMARK 500 2 PRO Q 40 116.61 -37.77
REMARK 500 2 LEU Q 44 4.50 -68.34
REMARK 500 2 GLN Q 46 7.04 -49.70
REMARK 500 2 ILE Q 49 -16.63 -48.35
REMARK 500 2 TYR Q 61 147.77 80.54
REMARK 500 2 MET Q 78 64.33 -113.81
REMARK 500 2 GLN Q 86 -9.41 -58.18
REMARK 500 2 ALA Q 88 40.80 -73.93
REMARK 500 3 LEU Q 44 6.48 -69.30
REMARK 500 3 GLN Q 46 5.51 -45.55
REMARK 500 3 ILE Q 49 -19.13 -47.83
REMARK 500 3 TYR Q 61 152.63 76.90
REMARK 500 3 ALA Q 88 41.01 -73.32
REMARK 500 4 PRO Q 17 -39.21 -33.99
REMARK 500 4 GLU Q 34 92.68 -65.61
REMARK 500 4 PRO Q 40 125.36 -37.82
REMARK 500 4 LEU Q 44 6.81 -69.37
REMARK 500 4 GLN Q 46 12.20 -51.16
REMARK 500 4 TYR Q 61 152.90 77.73
REMARK 500 4 ALA Q 88 -81.66 -71.28
REMARK 500 5 ARG Q 33 -172.70 -69.27
REMARK 500 5 PRO Q 40 113.12 -38.52
REMARK 500 5 LEU Q 44 1.33 -64.81
REMARK 500 5 GLN Q 46 2.30 -47.99
REMARK 500 5 TYR Q 61 155.23 75.05
REMARK 500 5 MET Q 76 32.25 -86.37
REMARK 500 5 ALA Q 88 47.61 -72.28
REMARK 500 6 GLU Q 34 -88.92 -39.00
REMARK 500 6 PRO Q 40 112.65 -39.67
REMARK 500 6 GLN Q 46 11.34 -50.88
REMARK 500 6 ILE Q 49 -18.97 -48.69
REMARK 500 6 TYR Q 61 153.44 50.72
REMARK 500 6 ARG Q 77 40.85 70.64
REMARK 500 6 ALA Q 88 46.79 -73.53
REMARK 500 7 ARG Q 33 -179.43 -67.81
REMARK 500 7 GLU Q 34 -92.17 20.22
REMARK 500 7 ARG Q 38 170.62 -59.69
REMARK 500 7 PRO Q 40 108.87 -40.89
REMARK 500 7 GLN Q 46 8.19 -50.67
REMARK 500 7 ILE Q 49 -18.09 -47.91
REMARK 500 7 TYR Q 61 150.07 78.80
REMARK 500 7 MET Q 76 -133.24 -84.78
REMARK 500 7 MET Q 78 50.55 -112.68
REMARK 500 8 PRO Q 40 110.05 -37.71
REMARK 500 8 TYR Q 61 152.22 78.54
REMARK 500 8 MET Q 76 32.61 -84.77
REMARK 500 8 ARG Q 77 29.01 49.04
REMARK 500 8 MET Q 78 68.47 -114.38
REMARK 500 8 GLN Q 86 -7.17 -58.44
REMARK 500 8 ALA Q 88 111.09 -160.23
REMARK 500 9 PRO Q 40 117.71 -39.05
REMARK 500 9 LEU Q 44 3.67 -66.79
REMARK 500 9 GLN Q 46 13.13 -62.01
REMARK 500 9 TYR Q 61 154.42 78.51
REMARK 500 9 MET Q 76 -134.31 -85.66
REMARK 500 9 MET Q 78 51.93 -113.39
REMARK 500 9 ALA Q 88 -80.96 -66.22
REMARK 500 10 THR Q 29 -55.01 -121.04
REMARK 500 10 ARG Q 33 -175.53 -66.21
REMARK 500 10 PRO Q 40 112.15 -36.62
REMARK 500 10 LEU Q 44 2.46 -65.62
REMARK 500 10 GLN Q 46 -1.01 -42.90
REMARK 500 10 ILE Q 49 -17.73 -48.62
REMARK 500 10 TYR Q 61 150.26 76.57
REMARK 500 10 MET Q 78 68.40 -113.89
REMARK 500 10 ALA Q 88 109.76 -162.34
REMARK 500 11 PRO Q 17 -36.40 -33.71
REMARK 500 11 ARG Q 38 -179.72 -61.90
REMARK 500 11 PRO Q 40 111.79 -39.51
REMARK 500 11 TYR Q 61 153.34 75.33
REMARK 500 11 ALA Q 88 -93.02 -70.22
REMARK 500 12 ARG Q 33 -175.36 -69.31
REMARK 500 12 TYR Q 61 150.00 79.14
REMARK 500 12 MET Q 78 68.93 -118.29
REMARK 500 13 GLU Q 34 13.72 -66.07
REMARK 500 13 PRO Q 40 118.52 -38.25
REMARK 500 13 TYR Q 61 151.49 76.77
REMARK 500 13 MET Q 78 67.42 -114.80
REMARK 500 14 LYS Q 26 -8.87 -59.73
REMARK 500 14 GLU Q 34 97.19 -63.32
REMARK 500 14 PRO Q 40 123.87 -38.80
REMARK 500 14 GLN Q 46 -3.04 -41.08
REMARK 500 14 ILE Q 49 -17.36 -48.88
REMARK 500 14 TYR Q 61 153.76 74.74
REMARK 500 14 ASP Q 75 -32.08 -37.20
REMARK 500 14 MET Q 76 -132.53 -86.21
REMARK 500 14 MET Q 78 58.67 -117.78
REMARK 500 14 ALA Q 88 -78.74 -64.90
REMARK 500 15 ARG Q 33 -168.81 -69.17
REMARK 500 15 GLU Q 34 -98.51 17.14
REMARK 500 15 ARG Q 38 -173.85 -60.34
REMARK 500 15 PRO Q 40 122.37 -39.41
REMARK 500 15 GLN Q 46 6.89 -50.83
REMARK 500 15 TYR Q 61 148.30 82.57
REMARK 500 15 MET Q 76 -134.48 -86.80
REMARK 500 15 ALA Q 88 -78.43 -66.41
REMARK 500 16 THR Q 29 -50.18 -120.85
REMARK 500 16 PRO Q 31 150.52 -38.59
REMARK 500 16 PRO Q 40 126.45 -38.57
REMARK 500 16 GLN Q 46 3.85 -45.86
REMARK 500 16 ILE Q 49 -18.67 -47.66
REMARK 500 16 TYR Q 61 150.79 73.52
REMARK 500 16 ALA Q 88 -88.98 -70.53
REMARK 500 17 PRO Q 17 -39.97 -32.23
REMARK 500 17 GLU Q 34 -95.20 31.50
REMARK 500 17 ARG Q 38 -146.50 -64.61
REMARK 500 17 PRO Q 40 123.02 -37.24
REMARK 500 17 TYR Q 61 152.50 75.62
REMARK 500 17 MET Q 76 30.09 -84.59
REMARK 500 17 MET Q 78 68.85 -110.37
REMARK 500 17 ALA Q 88 -82.76 -72.44
REMARK 500 18 ARG Q 33 -173.85 -67.76
REMARK 500 18 GLU Q 34 -91.62 14.67
REMARK 500 18 ARG Q 38 -168.16 -60.80
REMARK 500 18 LEU Q 44 -73.87 -77.85
REMARK 500 18 TYR Q 61 153.18 80.38
REMARK 500 18 MET Q 76 -136.42 -86.06
REMARK 500 18 ALA Q 88 -81.24 -66.14
REMARK 500 19 THR Q 29 -51.79 -120.08
REMARK 500 19 ARG Q 33 -177.61 -66.82
REMARK 500 19 PRO Q 40 116.16 -37.62
REMARK 500 19 LEU Q 44 4.21 -66.27
REMARK 500 19 GLN Q 46 6.98 -47.55
REMARK 500 19 ILE Q 49 -18.57 -47.64
REMARK 500 19 TYR Q 61 151.74 77.73
REMARK 500 19 MET Q 78 69.07 -116.95
REMARK 500 19 GLN Q 86 -8.46 -58.48
REMARK 500 19 ALA Q 88 39.22 -72.82
REMARK 500 20 PRO Q 17 -38.54 -35.11
REMARK 500 20 PRO Q 40 128.01 -39.96
REMARK 500 20 GLN Q 46 7.08 -50.25
REMARK 500 20 ILE Q 49 -17.51 -49.53
REMARK 500 20 TYR Q 61 151.85 77.55
REMARK 500 20 MET Q 78 64.94 -116.74
REMARK 500 20 ALA Q 88 38.60 -70.69
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HM2 Q 1 89 UNP Q8WXC3 Q8WXC3_HUMAN 1 89
SEQRES 1 Q 89 MET GLY THR LYS ARG GLU ALA ILE LEU LYS VAL LEU GLU
SEQRES 2 Q 89 ASN LEU THR PRO GLU GLU LEU LYS LYS PHE LYS MET LYS
SEQRES 3 Q 89 LEU GLY THR VAL PRO LEU ARG GLU GLY PHE GLU ARG ILE
SEQRES 4 Q 89 PRO ARG GLY ALA LEU GLY GLN LEU ASP ILE VAL ASP LEU
SEQRES 5 Q 89 THR ASP LYS LEU VAL ALA SER TYR TYR GLU ASP TYR ALA
SEQRES 6 Q 89 ALA GLU LEU VAL VAL ALA VAL LEU ARG ASP MET ARG MET
SEQRES 7 Q 89 LEU GLU GLU ALA ALA ARG LEU GLN ARG ALA ALA
HELIX 1 1 THR Q 3 GLU Q 13 1 11
HELIX 2 2 THR Q 16 LEU Q 27 1 12
HELIX 3 3 PRO Q 40 LEU Q 44 5 5
HELIX 4 4 ASP Q 48 MET Q 76 1 29
HELIX 5 5 MET Q 78 ARG Q 87 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
(ATOM LINES ARE NOT SHOWN.)
END
