BMRB Entry 18608

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18608

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASC_PYD: MRGSHHHHHHGSMGRARDAI LDALENLTAEELKKFKLKLL SVPLREGYGRIPRGALLSMD SLDLTDKLVSFYLETYGAEL TANVLRDMGLQEMAGQLQAA THQGSGAA

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 1UCP 3J63
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