BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25943

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

Data sets:
Data typeCount
13C chemical shifts289
15N chemical shifts84
1H chemical shifts614

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 91 residues - 10643.387 Da.

1   METALASERTHRARGCYSLYSLEUALAARG
2   TYRLEUGLUASPLEUGLUASPVALASPLEU
3   LYSLYSPHELYSMETHISLEUGLUASPTYR
4   PROPROGLNLYSGLYCYSILEPROLEUPRO
5   ARGGLYGLNTHRGLULYSALAASPHISVAL
6   ASPLEUALATHRLEUMETILEASPPHEASN
7   GLYGLUGLULYSALATRPALAMETALAVAL
8   TRPILEPHEALAALAILEASNARGARGASP
9   LEUTYRGLULYSALALYSARGASPGLUPRO
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_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