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 27538

Title: Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0   PubMed: 30414042

Authors: Jimenez, M. Angeles; Pantoja-Uceda, David; Chaves-Arquero, Belen

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).

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

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

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

Entity Sequences (FASTA):
pT-C-H1.0: MDEPKRSVAFKKTKKEVKKV AXPKKAAKPKKAASKAPSKK PKAXPVKKAKKKPAAXPKKA KKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSH HHHHH

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

Samples:

sample_1: pT-C-H1.0, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: pT-C-H1.0, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%; sodium phosphate 10 mM; sodium chloride 10 mM

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D hacacoNcaNCOsample_1isotropicsample_conditions_1
3D hacaCOncaNCOsample_1isotropicsample_conditions_1
3D CBCANCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N-HETNOEsample_2isotropicsample_conditions_1
3D HncacoNHsample_2isotropicsample_conditions_1
3D hNcacoNHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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