BMRB Entry 34318

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):

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

Additional metadata:

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

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

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