BMRB Entry 19875

Title:
Backbone resonance assignments of the pyrin domain of human Pyrin
Deposition date:
2014-03-26
Original release date:
2014-07-14
Authors:
Soh, Stephanie; Smith, Sarah; Hill, Justine
Citation:

Citation: Vajjhala, Parimala; Kaiser, Sebastian; Smith, Sarah; Ong, Qi-Rui; Soh, Stephanie; Stacey, Katryn; Hill, Justine. "Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly"  J. Biol. Chem. 289, 23504-23519 (2014).
PubMed: 25006247

Assembly members:

Assembly members:
Pyrin, polymer, 100 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: pET-28b

Data sets:
Data typeCount
13C chemical shifts297
15N chemical shifts93
1H chemical shifts194

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pyrin1

Entities:

Entity 1, Pyrin 100 residues - Formula weight is not available

1   METALALYSTHRPROSERASPHISLEULEU
2   SERTHRLEUGLUGLULEUVALPROTYRASP
3   PHEGLULYSPHELYSPHELYSLEUGLNASN
4   THRSERVALGLNLYSGLUHISSERARGILE
5   PROARGSERGLNILEGLNARGALAARGPRO
6   VALLYSMETALATHRLEULEUVALTHRTYR
7   TYRGLYGLUGLUTYRALAVALGLNLEUTHR
8   LEUGLNVALLEUARGALAILEASNGLNARG
9   LEULEUALAGLUGLULEUHISARGALAALA
10   ILEGLNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Pyrin, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 4.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin, CCPN, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

NCBI AF018080

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