BMRB Entry 26728

Title:
An NMR chemical shift assignment strategy for prone-to-aggregate intrinsically disordered proteins: a case study of the C-terminal domain of TDP-43
Deposition date:
2016-01-11
Original release date:
2016-11-16
Authors:
Huang, Jie-rong; Chen, Tsai-Chen; Hsiao, Chih-Lun; Huang, Shing-Jong
Citation:

Citation: Chen, Tsai-Chen; Hsiao, Chih-Lun; Huang, Shing-Jong; Huang, Jie-rong. "The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence"  Protein Pept. Lett. 23, 967-975 (2016).
PubMed: 27653629

Assembly members:

Assembly members:
TDP-43-C, polymer, 160 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: pET21

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts145
1H chemical shifts145

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TDP-43-C1

Entities:

Entity 1, TDP-43-C 160 residues - Formula weight is not available

1   METALASERHISHISHISHISHISHISGLY
2   SERSERASNARGGLNLEUGLUARGSERGLY
3   ARGPHEGLYGLYASNPROGLYGLYPHEGLY
4   ASNGLNGLYGLYPHEGLYASNSERARGGLY
5   GLYGLYALAGLYLEUGLYASNASNGLNGLY
6   SERASNMETGLYGLYGLYMETASNPHEGLY
7   ALAPHESERILEASNPROALAMETMETALA
8   ALAALAGLNALAALALEUGLNSERSERTRP
9   GLYMETMETGLYMETLEUALASERGLNGLN
10   ASNGLNSERGLYPROSERGLYASNASNGLN
11   ASNGLNGLYASNMETGLNARGGLUPROASN
12   GLNALAPHEGLYSERGLYASNASNSERTYR
13   SERGLYSERASNSERGLYALAALAILEGLY
14   TRPGLYSERALASERASNALAGLYSERGLY
15   SERGLYPHEASNGLYGLYPHEGLYSERSER
16   METASPSERLYSSERSERGLYTRPGLYMET

Samples:

sample_1: TDP-43-C, [U-100% 13C; U-100% 15N], 100 uM

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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