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 27700

Title: Human linker histone NGH1x in low ionic strength conditions   PubMed: 30868366

Deposition date: 2018-11-21 Original release date: 2019-01-02

Authors: De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit

Citation: De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit; De Wit, Herna; Vallet, Alicia; Brutscher, Bernhard; Koorsen, Gerrit. "NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate"  Biomol. NMR Assign. 13, 249-254 (2019).

Assembly members:
NGH1x_no_salt, polymer, 119 residues, 13101.1949 Da.

Natural source:   Common Name: NGH1x   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b+

Entity Sequences (FASTA):
NGH1x_no_salt: MSVELEEALPVTTAEGMAKK VTKAGGSAALSPSKKRKNSK KKNQPGKYSQLVVETIRRLG ERNGSSLAKIYTEAKKVPWF DQQNGRTYLKYSIKALVQND TLLQVKGTGANGSFKLNRK

Data typeCount
13C chemical shifts307
15N chemical shifts107
1H chemical shifts107

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NGH1x no salt1

Entities:

Entity 1, NGH1x no salt 119 residues - 13101.1949 Da.

1   METSERVALGLULEUGLUGLUALALEUPRO
2   VALTHRTHRALAGLUGLYMETALALYSLYS
3   VALTHRLYSALAGLYGLYSERALAALALEU
4   SERPROSERLYSLYSARGLYSASNSERLYS
5   LYSLYSASNGLNPROGLYLYSTYRSERGLN
6   LEUVALVALGLUTHRILEARGARGLEUGLY
7   GLUARGASNGLYSERSERLEUALALYSILE
8   TYRTHRGLUALALYSLYSVALPROTRPPHE
9   ASPGLNGLNASNGLYARGTHRTYRLEULYS
10   TYRSERILELYSALALEUVALGLNASNASP
11   THRLEULEUGLNVALLYSGLYTHRGLYALA
12   ASNGLYSERPHELYSLEUASNARGLYS

Samples:

NGH1x_low_ionic_strength: NGH1x_no_salt, [U-99% 13C; U-99% 15N], 0.5 mM

CondSet1: ionic strength: 20 mM; pH: 7.000; temperature: 278.000 K

CondSet4: pH: 7.0; temperature: 278 K

CondSet13: pH: 7.0; temperature: 278 K

CondSet14: pH: 7.0; temperature: 278 K

CondSet15: pH: 7.0; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCNGH1x_low_ionic_strengthisotropicCondSet1
3D HNCONGH1x_low_ionic_strengthisotropicCondSet4
3D HNCACBNGH1x_low_ionic_strengthisotropicCondSet13
HNCOCACB (H[N[co[{CA|ca[C]}]]])NGH1x_low_ionic_strengthisotropicCondSet14
HNCACO (H[N[ca[CO]]])NGH1x_low_ionic_strengthisotropicCondSet15

Software:

CcpNmr_Analysis v2.4, CCPN - Spectral analysis

NMR spectrometers:

  • Bruker Avance 950 MHz

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