BMRB Entry 25943
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25943
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Title: 3D NMR solution structure of NLRP3 PYD PubMed: 27432880
Deposition date: 2016-01-07 Original release date: 2016-07-25
Authors: de Alba, Eva; Oroz, Javier
Citation: Oroz, Javier; Barrera-Vilarmau, Susana; Alfonso, Carlos; Rivas, German; de Alba, Eva. "Asc pyrin domain self-associates and binds nlrp3 using Equivalent binding interfaces" J. Biol. Chem. 291, 19487-19501 (2016).
Assembly members:
entity, polymer, 91 residues, 10643.387 Da.
Natural source: Common Name: humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MASTRCKLARYLEDLEDVDL
KKFKMHLEDYPPQKGCIPLP
RGQTEKADHVDLATLMIDFN
GEEKAWAMAVWIFAAINRRD
LYEKAKRDEPK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 289 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 614 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 91 residues - 10643.387 Da.
| 1 | MET | ALA | SER | THR | ARG | CYS | LYS | LEU | ALA | ARG | ||||
| 2 | TYR | LEU | GLU | ASP | LEU | GLU | ASP | VAL | ASP | LEU | ||||
| 3 | LYS | LYS | PHE | LYS | MET | HIS | LEU | GLU | ASP | TYR | ||||
| 4 | PRO | PRO | GLN | LYS | GLY | CYS | ILE | PRO | LEU | PRO | ||||
| 5 | ARG | GLY | GLN | THR | GLU | LYS | ALA | ASP | HIS | VAL | ||||
| 6 | ASP | LEU | ALA | THR | LEU | MET | ILE | ASP | PHE | ASN | ||||
| 7 | GLY | GLU | GLU | LYS | ALA | TRP | ALA | MET | ALA | VAL | ||||
| 8 | TRP | ILE | PHE | ALA | ALA | ILE | ASN | ARG | ARG | ASP | ||||
| 9 | LEU | TYR | GLU | LYS | ALA | LYS | ARG | ASP | GLU | PRO | ||||
| 10 | LYS |
Samples:
sample_1: entity, [U-13C; U-15N], 100 – 200 uM; TCEP, [U-2H], 5 mM; sodium azide 100 uM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.0051 M; pH: 3.6; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
PIPP, Garrett - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
Molmol, Koradi, Billeter and Wuthrich - data analysis
ProcheckNMR, Laskowski and MacArthur - geometry optimization
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts