BMRB Entry 52586

Name: Histone H4 Tail with Uniform Lysine Acetylation
Published: 2024-11-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52586

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Histone H4 Tail with Uniform Lysine Acetylation

Deposition date:

2024-08-19

Original release date:

2024-11-15

Authors:

Dewing, Sophia; Showalter, Scott

Citation:

Citation: Dewing, Sophia; Phan, Tien; Kraft, Emma; Mittal, Jeetain; Showalter, Scott. "Acetylation-Dependent Compaction of the Histone H4 Tail Ensemble" J. Phys. Chem. B 128, 10636-10649 (2024).
PubMed: 39437158

Assembly members:

Assembly members:
entity_1, polymer, 26 residues, Formula weight is not available

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 Vector: pET 6His TEV LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGRGKGGKGLGKGGAKRHRK VLRDNW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	98
15N chemical shifts	25

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H4 tail 5-Acetyl	1

Entities:

Entity 1, H4 tail 5-Acetyl 26 residues - Formula weight is not available

K5ac, K8ac, K12ac, K16ac, K20ac

1

SER

GLY

ARG

GLY

ALY

GLY

ALY

GLY

LEU

2

GLY

ALY

GLY

ALA

ALY

ARG

HIS

ARG

ALY

3

VAL

LEU

ARG

ASP

ASN

TRP

Samples:

sample_1: Histone H4 tail 5-acetyl, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; potassium chloride 150 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-13C CON	sample_1	isotropic	sample_conditions_1
15N-13C CCCON	sample_1	isotropic	sample_conditions_1
15N-13C HACANCACON	sample_1	isotropic	sample_conditions_1
15N-13C HACANCANCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.2.0 - collection, processing

NMRFAM-SPARKY v1.470 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 500 MHz