BMRB Entry 27538

Title:
Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0
Deposition date:
2018-07-06
Original release date:
2018-11-16
Authors:
Jimenez, M. Angeles; Pantoja-Uceda, David; Chaves-Arquero, Belen
Citation:

Citation: Chaves-Arquero, Belen; Pantoja-Uceda, David; Roque, Alicia; Ponte, Inmaculada; Suau, Pedro; Jimenez, M. Angeles. "A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study"  J. Biomol. NMR 72, 139-148 (2018).
PubMed: 30414042

Assembly members:

Assembly members:
pT-C-H1.0, polymer, 105 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCTH1.0

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts98
1H chemical shifts56
heteronuclear NOE values56

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pT-C-H1.01

Entities:

Entity 1, pT-C-H1.0 105 residues - Formula weight is not available

Residues 2-97 correspond to residues 98-193 of histone H1.0 from mouse. Residues 98-105 are the cloning-tag. Thr residues at positions 22, 44 and 56 are phosphorylated.

1   METASPGLUPROLYSARGSERVALALAPHE
2   LYSLYSTHRLYSLYSGLUVALLYSLYSVAL
3   ALATPOPROLYSLYSALAALALYSPROLYS
4   LYSALAALASERLYSALAPROSERLYSLYS
5   PROLYSALATPOPROVALLYSLYSALALYS
6   LYSLYSPROALAALATPOPROLYSLYSALA
7   LYSLYSPROLYSVALVALLYSVALLYSPRO
8   VALLYSALASERLYSPROLYSLYSALALYS
9   THRVALLYSPROLYSALALYSSERSERALA
10   LYSARGALASERLYSLYSLYSARGSERHIS
11   HISHISHISHISHIS

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