BMRB Entry 19875
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19875
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Title: Backbone resonance assignments of the pyrin domain of human Pyrin PubMed: 25006247
Deposition date: 2014-03-26 Original release date: 2014-07-14
Authors: Soh, Stephanie; Smith, Sarah; Hill, Justine
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).
Assembly members:
Pyrin, polymer, 100 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):
Pyrin: MAKTPSDHLLSTLEELVPYD
FEKFKFKLQNTSVQKEHSRI
PRSQIQRARPVKMATLLVTY
YGEEYAVQLTLQVLRAINQR
LLAEELHRAAIQLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 297 |
15N chemical shifts | 93 |
1H chemical shifts | 194 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Pyrin | 1 |
Entities:
Entity 1, Pyrin 100 residues - Formula weight is not available
1 | MET | ALA | LYS | THR | PRO | SER | ASP | HIS | LEU | LEU | |
2 | SER | THR | LEU | GLU | GLU | LEU | VAL | PRO | TYR | ASP | |
3 | PHE | GLU | LYS | PHE | LYS | PHE | LYS | LEU | GLN | ASN | |
4 | THR | SER | VAL | GLN | LYS | GLU | HIS | SER | ARG | ILE | |
5 | PRO | ARG | SER | GLN | ILE | GLN | ARG | ALA | ARG | PRO | |
6 | VAL | LYS | MET | ALA | THR | LEU | LEU | VAL | THR | TYR | |
7 | TYR | GLY | GLU | GLU | TYR | ALA | VAL | GLN | LEU | THR | |
8 | LEU | GLN | VAL | LEU | ARG | ALA | ILE | ASN | GLN | ARG | |
9 | LEU | LEU | ALA | GLU | GLU | LEU | HIS | ARG | ALA | ALA | |
10 | ILE | GLN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts