BMRB Entry 25561
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25561
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structure and assembly of the mouse ASC filament by combined NMR spectroscopy and cryo-electron microscopy PubMed: 26464513
Deposition date: 2015-04-01 Original release date: 2016-06-30
Authors: Sborgi, Lorenzo
Citation: Sborgi, Lorenzo; Ravotti, Francesco; Dandey, Venkata; Dick, Mathias; Mazur, Adam; Reckel, Sina; Chami, Mohamed; Scherer, Sebastian; Huber, Matthias; Bockmann, Anja; Egelman, Edward; Stahlberg, Henning; Broz, Petr; Meier, Beat; Hiller, Sebastian. "Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy" Proc. Natl. Acad. Sci. U. S. A. 112, 13237-13242 (2015).
Assembly members:
ASC_PYD, polymer, 103 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ASC_PYD: MGRARDAILDALENLSGDEL
KKFKMKLLTVQLREGYGRIP
RGALLQMDAIDLTDKLVSYY
LESYGLELTMTVLRDMGLQE
LAEQLQTTKEEGSGSLEHHH
HHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 192 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ASC Pyrin domain | 1 |
Entities:
Entity 1, ASC Pyrin domain 103 residues - Formula weight is not available
| 1 | MET | GLY | ARG | ALA | ARG | ASP | ALA | ILE | LEU | ASP | ||||
| 2 | ALA | LEU | GLU | ASN | LEU | SER | GLY | ASP | GLU | LEU | ||||
| 3 | LYS | LYS | PHE | LYS | MET | LYS | LEU | LEU | THR | VAL | ||||
| 4 | GLN | LEU | ARG | GLU | GLY | TYR | GLY | ARG | ILE | PRO | ||||
| 5 | ARG | GLY | ALA | LEU | LEU | GLN | MET | ASP | ALA | ILE | ||||
| 6 | ASP | LEU | THR | ASP | LYS | LEU | VAL | SER | TYR | TYR | ||||
| 7 | LEU | GLU | SER | TYR | GLY | LEU | GLU | LEU | THR | MET | ||||
| 8 | THR | VAL | LEU | ARG | ASP | MET | GLY | LEU | GLN | GLU | ||||
| 9 | LEU | ALA | GLU | GLN | LEU | GLN | THR | THR | LYS | GLU | ||||
| 10 | GLU | GLY | SER | GLY | SER | LEU | GLU | HIS | HIS | HIS | ||||
| 11 | HIS | HIS | HIS |
Samples:
sample_1: ASC PYD, [U-100% 13C; U-100% 15N], 0.3 mM
sample_conditions_1: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Ascend II 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts