BMRB Entry 27633
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27633
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Chemical shift assignments of the C-terminal domain of chicken H1.11L PubMed: 30301810
Deposition date: 2018-09-27 Original release date: 2019-02-06
Authors: Turner, Abigail; Watson, Matthew; Wilkins, Oscar; Cato, Laura; Travers, Andrew; Thomas, Jean; Stott, Katherine
Citation: Turner, Abigail; Watson, Matthew; Wilkins, Oscar; Cato, Laura; Travers, Andrew; Thomas, Jean; Stott, Katherine. "Highly disordered histone H1-DNA model complexes and their condensates" Proc. Natl. Acad. Sci. U.S.A. 115, 11964-11969 (2018).
Assembly members:
H1, polymer, 111 residues, Formula weight is not available
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET13a
Entity Sequences (FASTA):
H1: KPGEVKEKAPKKKASAAKPK
KPAAKKPAAAAKKPKKAVAV
KKSPKKAKKPAASATKKSAK
SPKKVTKAVKPKKAVAAKSP
AKAKAVKPKAAKPKAAKPKA
AKAKKAAAKKK
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 71 |
1H chemical shifts | 71 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | H1 C-terminal domain | 1 |
Entities:
Entity 1, H1 C-terminal domain 111 residues - Formula weight is not available
1 | LYS | PRO | GLY | GLU | VAL | LYS | GLU | LYS | ALA | PRO | ||||
2 | LYS | LYS | LYS | ALA | SER | ALA | ALA | LYS | PRO | LYS | ||||
3 | LYS | PRO | ALA | ALA | LYS | LYS | PRO | ALA | ALA | ALA | ||||
4 | ALA | LYS | LYS | PRO | LYS | LYS | ALA | VAL | ALA | VAL | ||||
5 | LYS | LYS | SER | PRO | LYS | LYS | ALA | LYS | LYS | PRO | ||||
6 | ALA | ALA | SER | ALA | THR | LYS | LYS | SER | ALA | LYS | ||||
7 | SER | PRO | LYS | LYS | VAL | THR | LYS | ALA | VAL | LYS | ||||
8 | PRO | LYS | LYS | ALA | VAL | ALA | ALA | LYS | SER | PRO | ||||
9 | ALA | LYS | ALA | LYS | ALA | VAL | LYS | PRO | LYS | ALA | ||||
10 | ALA | LYS | PRO | LYS | ALA | ALA | LYS | PRO | LYS | ALA | ||||
11 | ALA | LYS | ALA | LYS | LYS | ALA | ALA | ALA | LYS | LYS | ||||
12 | LYS |
Samples:
sample_1: H1, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 0.5 mM; NaCl 0.5 mM
sample_conditions_1: ionic strength: 0.16 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
AZARA, Boucher - processing
Analysis vv2.4, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts