BMRB Entry 27537

Title:
Chemical Shift Assignments for the 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:
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 shifts284
15N chemical shifts95
1H chemical shifts55
heteronuclear NOE values55

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-H1.01

Entities:

Entity 1, 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.

1   METASPGLUPROLYSARGSERVALALAPHE
2   LYSLYSTHRLYSLYSGLUVALLYSLYSVAL
3   ALATHRPROLYSLYSALAALALYSPROLYS
4   LYSALAALASERLYSALAPROSERLYSLYS
5   PROLYSALATHRPROVALLYSLYSALALYS
6   LYSLYSPROALAALATHRPROLYSLYSALA
7   LYSLYSPROLYSVALVALLYSVALLYSPRO
8   VALLYSALASERLYSPROLYSLYSALALYS
9   THRVALLYSPROLYSALALYSSERSERALA
10   LYSARGALASERLYSLYSLYSARGSERHIS
11   HISHISHISHISHIS

Samples:

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

sample_2: 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

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

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