BMRB Entry 27788

Title:
G335N TDP-43_267-414
Deposition date:
2019-02-15
Original release date:
2019-10-30
Authors:
Fawzi, Nicolas; Conicella, Alexander; D'Ordine, Alexandra
Citation:

Citation: Conicella, Alexander; Dignon, Gregory; Zerze, Gul; Schmidt, Hermann Broder; D'Ordine, Alexandra; Kim, Young; Rohatgi, Rajat; Ayala, Yuna; Mittal, Jeetain; Fawzi, Nicolas. "TDP-43 alpha-helical structure tunes liquid-liquid phase separation and function"  Proc. Natl. Acad. Sci. U.S.A. 117, 5883-5894 (2020).
PubMed: 32132204

Assembly members:

Assembly members:
G335N_TDP-43_267-414, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJ411

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1G335N TDP-43_267-414 Monomer1

Entities:

Entity 1, G335N TDP-43_267-414 Monomer 151 residues - Formula weight is not available

1   GLYHISMETASNARGGLNLEUGLUARGSER
2   GLYARGPHEGLYGLYASNPROGLYGLYPHE
3   GLYASNGLNGLYGLYPHEGLYASNSERARG
4   GLYGLYGLYALAGLYLEUGLYASNASNGLN
5   GLYSERASNMETGLYGLYGLYMETASNPHE
6   GLYALAPHESERILEASNPROALAMETMET
7   ALAALAALAGLNALAALALEUGLNSERSER
8   TRPASNMETMETGLYMETLEUALASERGLN
9   GLNASNGLNSERGLYPROSERGLYASNASN
10   GLNASNGLNGLYASNMETGLNARGGLUPRO
11   ASNGLNALAPHEGLYSERGLYASNASNSER
12   TYRSERGLYSERASNSERGLYALAALAILE
13   GLYTRPGLYSERALASERASNALAGLYSER
14   GLYSERGLYPHEASNGLYGLYPHEGLYSER
15   SERMETASPSERLYSSERSERGLYTRPGLY
16   MET

Samples:

sample_1: G335N TDP-43_267-414, [U-99% 13C; U-99% 15N], 20 uM; MES 20 mM

sample_conditions_1: pH: 6.1; 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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz

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