BMRB Entry 51102

Title:
TIA-1 prion-like domain, backbone chemical shifts
Deposition date:
2021-09-26
Original release date:
2022-08-17
Authors:
Sekiyama, Naotaka; Akagi, Ken-ichi; Kodama, Takashi; Tochio, Hidehito
Citation:

Citation: Sekiyama, Naotaka; Takaba, Kiyofumi; Maki-Yonekura, Saori; Akagi, Ken-Ichi; Ohtani, Yasuko; Imamura, Kayo; Terakawa, Tsuyoshi; Yamashita, Keitaro; Inaoka, Daigo; Yonekura, Koji; Kodama, Takashi; Tochio, Hidehito. "ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures"  Proc. Natl. Acad. Sci. U. S. A. 119, e2122523119-e2122523119 (2022).
PubMed: 36112647

Assembly members:

Assembly members:
entity_1, polymer, 91 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts64
1H chemical shifts64

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TIA-1 prion-like domain1

Entities:

Entity 1, TIA-1 prion-like domain 91 residues - Formula weight is not available

His-TEV-TIA1 320-386

1   METGLYSERSERHISHISHISHISHISHIS
2   HISHISHISHISHISHISSERGLUASNLEU
3   TYRPHEGLNGLYGLYGLNTYRVALPROASN
4   GLYTRPGLNVALPROALATYRGLYVALTYR
5   GLYGLNPROTRPSERGLNGLNGLYPHEASN
6   GLNTHRGLNSERSERALAPROTRPMETGLY
7   PROASNTYRSERVALPROPROPROGLNGLY
8   GLNASNGLYSERMETLEUPROSERGLNPRO
9   ALAGLYTYRARGVALALAGLYTYRGLUTHR
10   GLN

Samples:

sample_1: TIA-1 prion-like domain, [U-99% 13C; U-99% 15N], 200 uM; MES 50 mM; sodium chloride 150 mM; DTT 1 mM; 1,6-hexanediol 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - data analysis

NMR spectrometers:

  • Bruker AVANCE II 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks