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 25675

Title: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF TDP-43   PubMed: 26756435

Deposition date: 2015-06-26 Original release date: 2016-01-11

Authors: Mompean, Miguel; Romano, Valentina; Pantoja-Uceda, David; Stuani, Cristiana; Baralle, Francisco; Buratti, Emanuele; Laurents, Douglas

Citation: Mompean, Miguel; Romano, Valentina; Pantoja-Uceda, David; Stuani, Cristiana; Baralle, Francisco; Buratti, Emanuele; Laurents, Douglas. "The TDP-43 N-terminal domain structure at high resolution"  FEBS J. 283, 1242-1260 (2016).

Assembly members:
entity, polymer, 89 residues, 9854.009 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30-6xHis

Entity Sequences (FASTA):
entity: MAGSHHHHHHGSMSEYIRVT EDENDEPIEIPSEDDGTVLL STVTAQFPGACGLRYRNPVS QCMRGVRLVEGILHAPDAGW GNLVYVVNY

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts93
1H chemical shifts569

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 89 residues - 9854.009 Da.

1   METALAGLYSERHISHISHISHISHISHIS
2   GLYSERMETSERGLUTYRILEARGVALTHR
3   GLUASPGLUASNASPGLUPROILEGLUILE
4   PROSERGLUASPASPGLYTHRVALLEULEU
5   SERTHRVALTHRALAGLNPHEPROGLYALA
6   CYSGLYLEUARGTYRARGASNPROVALSER
7   GLNCYSMETARGGLYVALARGLEUVALGLU
8   GLYILELEUHISALAPROASPALAGLYTRP
9   GLYASNLEUVALTYRVALVALASNTYR

Samples:

sample_1: NTD, [U-13C; U-15N], 0.6 mM; TCEP mM; CD3COOD/CD3COO-Na+ mM; NaN3 mM; H20 90%; D20 10%

sample_conditions_1: pH: 3.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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