BMRB Entry 34318

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34318
MolProbity Validation Chart

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Title:
Solution structure of the globular domain from human histone H1.0
Deposition date:
2018-09-23
Original release date:
2019-10-08
Authors:
Martinsen, J.; Bugge, K.; Kragelund, B.
Citation:

Citation: Martinsen, Jacob; Saar, Daniel; Fernandes, Catarina; Schuler, Benjamin; Bugge, Katrine; Kragelund, Birthe. "Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges"  Protein Sci. 31, 918-932 (2022).
PubMed: 35066947

Assembly members:

Assembly members:
entity_1, polymer, 75 residues, 8163.378 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDHPKYSDMIVAAIQAEKNR AGSSRQSIQKYIKSHYKVGE NADSQIKLSIKRLVTTGVLK QTKGVGASGSFRLAK

Data sets:
Data typeCount
13C chemical shifts311
15N chemical shifts78
1H chemical shifts463

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 75 residues - 8163.378 Da.

1   GLYASPHISPROLYSTYRSERASPMETILE
2   VALALAALAILEGLNALAGLULYSASNARG
3   ALAGLYSERSERARGGLNSERILEGLNLYS
4   TYRILELYSSERHISTYRLYSVALGLYGLU
5   ASNALAASPSERGLNILELYSLEUSERILE
6   LYSARGLEUVALTHRTHRGLYVALLEULYS
7   GLNTHRLYSGLYVALGLYALASERGLYSER
8   PHEARGLEUALALYS

Samples:

sample_1: H1-GD, [U-99% 13C; U-99% 15N], 0.925 mM; Tris 10 mM; KCl 157 mM; EDTA 0.1 mM; DSS 0.125 mM

sample_2: H1-GD, [U-99% 13C; U-99% 15N], 0.25 mM; Tris 10 mM; KCl 157 mM; EDTA 0.1 mM; DSS 0.125 mM

sample_conditions_1: ionic strength: 165 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

TopSpin, Bruker Biospin - collection

CcpNmr Analysis, CCPN - chemical shift assignment, data analysis, peak picking

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker AVANCE III 750 MHz

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