BMRB Entry 26823

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments, HNHA scalar coupling, and 15N backbone relaxation data for TDP-43 C-terminal domain wild type
Deposition date:
2016-06-20
Original release date:
2016-08-19
Authors:
Conicella, Alexander; Fawzi, Nicolas
Citation:

Citation: Conicella, Alexander; Zerze, Gul; Mittal, Jeetain; Fawzi, Nicolas. "ALS Mutations Disrupt Phase Separation Mediated by alpha-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain"  Structure (Cambridge, MA, U.S.) 24, 1537-1549 (2016).
PubMed: 27545621

Assembly members:

Assembly members:
WT_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 typeCount
13C chemical shifts660
15N chemical shifts286
1H chemical shifts292
T1 relaxation values222
T2 relaxation values259
coupling constants101
heteronuclear NOE values196

Additional metadata:

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

Assembly:

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

Entities:

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

Residues 1-3 comprise the cloning artifact left after removal of the N-terminal affinity tag by cleavage with TEV protease.

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

Samples:

sample-1: WT TDP-43_267-414, [U-99% 13C; U-99% 15N], 20 uM; MES 20 mM

sample-2: WT TDP-43_267-414, [U-99% 15N], 20 uM; MES 20 mM

283_K: pH: 6.1; pressure: 1 atm; temperature: 283 K

298_K: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample-1isotropic298_K
3D HNCACBsample-1isotropic298_K
3D CBCA(CO)NHsample-1isotropic298_K
3D HNCOsample-1isotropic298_K
3D HN(CA)COsample-1isotropic298_K
2D 1H-15N HSQCsample-1isotropic283_K
3D HNCACBsample-1isotropic283_K
3D CBCA(CO)NHsample-1isotropic283_K
hnhagp3dsample-2isotropic283_K
hsqct1etf3gpsitc3d.nlfsample-2isotropic283_K
hsqct2etf3gpsitc3d.acsample-2isotropic283_K
hsqcnoef3gpsisample-2isotropic283_K
hsqct1etf3gpsitc3d.nlfsample-2isotropic283_K
hsqct2etf3gpsitc3d.acsample-2isotropic283_K
hsqcnoef3gpsisample-2isotropic283_K

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 500 MHz

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