BMRB Entry 51509
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51509
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Diaz-parga, Pedro; Gould, Andrea; de Alba Bastarrechea, Eva. "Natural and engineered inflammasome adaptor proteins reveal optimum linker length for self-assembly" J. Biol. Chem. 298, 102501-102501 (2022).
PubMed: 36116550
Assembly members:
entity_1, polymer, 261 residues, Formula weight is not available
entity_2, polymer, 215 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 Vector: PET-15b
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
MGRARDAILDALENLTAEEL
KKFKLKLLSVPLREGYGRIP
RGALLSMDALDLTDKLVSFY
LETYGAELTANVLRDMGLQE
MAGQLQAATHQGSGAAPAGI
QAPPQSAAKPGLHQGSGAAP
AGIQAPPQSAAKPGLHQGSG
AAPAGIQAPPQSAAKPGLHF
IDQHRAALIARVTNVEWLLD
ALYGKVLTDEQYQAVRAEPT
NPSKMRKLFSFTPAWNWTCK
DLLLQALRESQSYLVEDLER
S
entity_2: MGSSHHHHHHSSGLVPRGSH
MGRARDAILDALENLTAEEL
KKFKLKLLSVPLREGYGRIP
RGALLSMDALDLTDKLVSFY
LETYGAELTANVLRDMGLQE
MAGQLQAATHQGSGAAPAGI
QAPPQSAAKPGLHFIDQHRA
ALIARVTNVEWLLDALYGKV
LTDEQYQAVRAEPTNPSKMR
KLFSFTPAWNWTCKDLLLQA
LRESQSYLVEDLERS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 321 |
| 15N chemical shifts | 171 |
| 1H chemical shifts | 171 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ASC3X | 1 |
| 2 | ASC | 2 |
Entities:
Entity 1, ASC3X 261 residues - Formula weight is not available
Residues 1-20 contain a His-tag and a thrombin cleavage site. ASC3X starts at residue 21 (M) it id designated M1 in the NMR file.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLY | ARG | ALA | ARG | ASP | ALA | ILE | LEU | ASP | ||||
| 4 | ALA | LEU | GLU | ASN | LEU | THR | ALA | GLU | GLU | LEU | ||||
| 5 | LYS | LYS | PHE | LYS | LEU | LYS | LEU | LEU | SER | VAL | ||||
| 6 | PRO | LEU | ARG | GLU | GLY | TYR | GLY | ARG | ILE | PRO | ||||
| 7 | ARG | GLY | ALA | LEU | LEU | SER | MET | ASP | ALA | LEU | ||||
| 8 | ASP | LEU | THR | ASP | LYS | LEU | VAL | SER | PHE | TYR | ||||
| 9 | LEU | GLU | THR | TYR | GLY | ALA | GLU | LEU | THR | ALA | ||||
| 10 | ASN | VAL | LEU | ARG | ASP | MET | GLY | LEU | GLN | GLU | ||||
| 11 | MET | ALA | GLY | GLN | LEU | GLN | ALA | ALA | THR | HIS | ||||
| 12 | GLN | GLY | SER | GLY | ALA | ALA | PRO | ALA | GLY | ILE | ||||
| 13 | GLN | ALA | PRO | PRO | GLN | SER | ALA | ALA | LYS | PRO | ||||
| 14 | GLY | LEU | HIS | GLN | GLY | SER | GLY | ALA | ALA | PRO | ||||
| 15 | ALA | GLY | ILE | GLN | ALA | PRO | PRO | GLN | SER | ALA | ||||
| 16 | ALA | LYS | PRO | GLY | LEU | HIS | GLN | GLY | SER | GLY | ||||
| 17 | ALA | ALA | PRO | ALA | GLY | ILE | GLN | ALA | PRO | PRO | ||||
| 18 | GLN | SER | ALA | ALA | LYS | PRO | GLY | LEU | HIS | PHE | ||||
| 19 | ILE | ASP | GLN | HIS | ARG | ALA | ALA | LEU | ILE | ALA | ||||
| 20 | ARG | VAL | THR | ASN | VAL | GLU | TRP | LEU | LEU | ASP | ||||
| 21 | ALA | LEU | TYR | GLY | LYS | VAL | LEU | THR | ASP | GLU | ||||
| 22 | GLN | TYR | GLN | ALA | VAL | ARG | ALA | GLU | PRO | THR | ||||
| 23 | ASN | PRO | SER | LYS | MET | ARG | LYS | LEU | PHE | SER | ||||
| 24 | PHE | THR | PRO | ALA | TRP | ASN | TRP | THR | CYS | LYS | ||||
| 25 | ASP | LEU | LEU | LEU | GLN | ALA | LEU | ARG | GLU | SER | ||||
| 26 | GLN | SER | TYR | LEU | VAL | GLU | ASP | LEU | GLU | ARG | ||||
| 27 | SER |
Entity 2, ASC 215 residues - Formula weight is not available
Residues 1-20 contain a His-tag and a thrombin cleavage site. ASC starts at residue 21 (M) it id designated M1 in the NMR file.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLY | ARG | ALA | ARG | ASP | ALA | ILE | LEU | ASP | ||||
| 4 | ALA | LEU | GLU | ASN | LEU | THR | ALA | GLU | GLU | LEU | ||||
| 5 | LYS | LYS | PHE | LYS | LEU | LYS | LEU | LEU | SER | VAL | ||||
| 6 | PRO | LEU | ARG | GLU | GLY | TYR | GLY | ARG | ILE | PRO | ||||
| 7 | ARG | GLY | ALA | LEU | LEU | SER | MET | ASP | ALA | LEU | ||||
| 8 | ASP | LEU | THR | ASP | LYS | LEU | VAL | SER | PHE | TYR | ||||
| 9 | LEU | GLU | THR | TYR | GLY | ALA | GLU | LEU | THR | ALA | ||||
| 10 | ASN | VAL | LEU | ARG | ASP | MET | GLY | LEU | GLN | GLU | ||||
| 11 | MET | ALA | GLY | GLN | LEU | GLN | ALA | ALA | THR | HIS | ||||
| 12 | GLN | GLY | SER | GLY | ALA | ALA | PRO | ALA | GLY | ILE | ||||
| 13 | GLN | ALA | PRO | PRO | GLN | SER | ALA | ALA | LYS | PRO | ||||
| 14 | GLY | LEU | HIS | PHE | ILE | ASP | GLN | HIS | ARG | ALA | ||||
| 15 | ALA | LEU | ILE | ALA | ARG | VAL | THR | ASN | VAL | GLU | ||||
| 16 | TRP | LEU | LEU | ASP | ALA | LEU | TYR | GLY | LYS | VAL | ||||
| 17 | LEU | THR | ASP | GLU | GLN | TYR | GLN | ALA | VAL | ARG | ||||
| 18 | ALA | GLU | PRO | THR | ASN | PRO | SER | LYS | MET | ARG | ||||
| 19 | LYS | LEU | PHE | SER | PHE | THR | PRO | ALA | TRP | ASN | ||||
| 20 | TRP | THR | CYS | LYS | ASP | LEU | LEU | LEU | GLN | ALA | ||||
| 21 | LEU | ARG | GLU | SER | GLN | SER | TYR | LEU | VAL | GLU | ||||
| 22 | ASP | LEU | GLU | ARG | SER |
Samples:
sample_1: ASC3X, [U-99% 13C; U-99% 15N], 0.2 mM; glycine 20 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 0 M; pH: 3.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks