BMRB Entry 18608

Title:
Backbone resonance assignment of ASC pyrin domain
Deposition date:
2012-07-23
Original release date:
2012-10-18
Authors:
Vajjhala, Parimala; Mirams, Ruth; Hill, Justine
Citation:

Citation: Vajjhala, Parimala; Mirams, Ruth; Hill, Justine. "Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein."  J. Biol. Chem. 287, 41732-41743 (2012).
PubMed: 23066025

Assembly members:

Assembly members:
ASC_PYD, polymer, 108 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE-30

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts89
1H chemical shifts88

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ASC PYD1

Entities:

Entity 1, ASC PYD 108 residues - Formula weight is not available

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERMETGLYARGALAARGASPALAILE
3   LEUASPALALEUGLUASNLEUTHRALAGLU
4   GLULEULYSLYSPHELYSLEULYSLEULEU
5   SERVALPROLEUARGGLUGLYTYRGLYARG
6   ILEPROARGGLYALALEULEUSERMETASP
7   SERLEUASPLEUTHRASPLYSLEUVALSER
8   PHETYRLEUGLUTHRTYRGLYALAGLULEU
9   THRALAASNVALLEUARGASPMETGLYLEU
10   GLNGLUMETALAGLYGLNLEUGLNALAALA
11   THRHISGLNGLYSERGLYALAALA

Samples:

sample_1: ASC PYD, [U-99% 15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_2: ASC PYD, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis, CCPN - processing

HADDOCK, Alexandre Bonvin - structure solution

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

PDB
DBJ BAA87339 BAG37041 BAG73625
GB AAF99665 AAG01187 AAG01188 AAG30286 AAH13569
REF NP_037390 NP_660183 XP_001158625 XP_001158687 XP_003280507
SP Q9ULZ3
AlphaFold Q9ULZ3

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks