BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26021

Title: Sr33 Coiled-coil domain   PubMed: 27791121

Deposition date: 2016-03-30 Original release date: 2016-10-13

Authors: Lavrencic, Peter; Mobli, Mehdi

Citation: Casey, Lachlan; Lavrencic, Peter; Bentham, Adam; Cesari, Stella; Ericsson, Daniel; Croll, Tristan; Turk, Dusan; Anderson, Peter; Mark, Alan; Dodds, Peter; Mobli, Mehdi; Kobe, Bostjan; Williams, Simon. "The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins"  Proc. Natl. Acad. Sci. U.S.A. ., .-. (2016).

Assembly members:
entity, polymer, 118 residues, 13138.456 Da.

Natural source:   Common Name: bread wheat   Taxonomy ID: 4565   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Triticum aestivum

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: SNAGAIAKLIPKLGELLVGE YKLHKGVKKNIEDLLKELKT MNAALIKIGEVPPDQLDSQD KLWADEVRELSYVIEDAVDK FLVRVHGVEPDDNTNGFKGL MKRTTKLLKKVVDKHGIA

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts120
1H chemical shifts865

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 118 residues - 13138.456 Da.

1   SERASNALAGLYALAILEALALYSLEUILE
2   PROLYSLEUGLYGLULEULEUVALGLYGLU
3   TYRLYSLEUHISLYSGLYVALLYSLYSASN
4   ILEGLUASPLEULEULYSGLULEULYSTHR
5   METASNALAALALEUILELYSILEGLYGLU
6   VALPROPROASPGLNLEUASPSERGLNASP
7   LYSLEUTRPALAASPGLUVALARGGLULEU
8   SERTYRVALILEGLUASPALAVALASPLYS
9   PHELEUVALARGVALHISGLYVALGLUPRO
10   ASPASPASNTHRASNGLYPHELYSGLYLEU
11   METLYSARGTHRTHRLYSLEULEULYSLYS
12   VALVALASPLYSHISGLYILEALA

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 450 uM; HEPES 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, refinement, structure solution

TALOS vTALOS+, Cornilescu, Delaglio and Bax - geometry optimization

CCPNMR v2.4.1, Vranken WF et al. - data analysis, peak picking

Rowland_NMR_toolkit v3, JC Hoch et al. - processing

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts