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 PubMed: 23066025
Deposition date: 2012-07-23 Original release date: 2012-10-18
Authors: Vajjhala, Parimala; Mirams, Ruth; Hill, Justine
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).
Assembly members:
ASC_PYD, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ASC_PYD: MRGSHHHHHHGSMGRARDAI
LDALENLTAEELKKFKLKLL
SVPLREGYGRIPRGALLSMD
SLDLTDKLVSFYLETYGAEL
TANVLRDMGLQEMAGQLQAA
THQGSGAA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 266 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 88 |
Additional metadata:
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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts