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 34081

Title: Solution structure of TDP-43 (residues 1-102)   PubMed: 28566288

Deposition date: 2016-12-22 Original release date: 2017-06-02

Authors: Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Laurents, D.

Citation: Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Buratti, E.; Laurents, D.. "Point mutations in transactive response DNA-binding protein 43 (TDP-43)'s N-terminal domain compromise its stability, dimerization and functions"  J. Biol. Chem. 292, 11992-12006 (2017).

Assembly members:
entity_1, polymer, 114 residues, 12674.207 Da.

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

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

Entity Sequences (FASTA):
entity_1: MAGSHHHHHHGSMSEYIRVT EDENDEPIEIPSEDDGTVLL STVTAQFPGACGLRYRNPVS QCMRGVRLVEGILHAPDAGW GNLVYVVNYPKDNKRKMDET DASSAVKVKRAVQK

Data sets:
Data typeCount
15N chemical shifts1
1H chemical shifts584

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 114 residues - 12674.207 Da.

1   METALAGLYSERHISHISHISHISHISHIS
2   GLYSERMETSERGLUTYRILEARGVALTHR
3   GLUASPGLUASNASPGLUPROILEGLUILE
4   PROSERGLUASPASPGLYTHRVALLEULEU
5   SERTHRVALTHRALAGLNPHEPROGLYALA
6   CYSGLYLEUARGTYRARGASNPROVALSER
7   GLNCYSMETARGGLYVALARGLEUVALGLU
8   GLYILELEUHISALAPROASPALAGLYTRP
9   GLYASNLEUVALTYRVALVALASNTYRPRO
10   LYSASPASNLYSARGLYSMETASPGLUTHR
11   ASPALASERSERALAVALLYSVALLYSARG
12   ALAVALGLNLYS

Samples:

sample_1: TDP-43(1-102), [U-13C; U-15N], 0.35 mM

sample_conditions_1: pH: 3.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AvanceII 800 MHz

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