Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53182

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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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Name: H3 N-tail in H4ac chromatosome
Published: 2026-02-25

Title:

H3 N-tail in H4ac chromatosome

Deposition date:

2025-05-15

Original release date:

2026-02-25

Authors:

Furukawa, Ayako; Echigoya, Kenta; Wakamori, Masatoshi; Ohtomo, Hideaki; Tsunaka, Yasuo; Umehara, Takashi; Takizawa, Yoshimasa; Kurumizaka, Hitoshi; Nishimura, Yoshifumi

Citation:

Citation: Furukawa, Ayako; Echigoya, Kenta; Wakamori, Masatoshi; Ohtomo, Hideaki; Tsunaka, Yasuo; Umehara, Takashi; Takizawa, Yoshimasa; Kurumizaka, Hitoshi; Nishimura, Yoshifumi. "Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation, altering their dynamics" Commun. Biol. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 136 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: pET22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MARTKQTARKSTGGKAPRKQ LATKAARKSAPATGGVKKPH RYRPGTVALREIRRYQKSTE LLIRKLPFQRLVREIAQDFK TDLRFQSSAVMALQEACEAY LVGLFEDTNLCAIHAKRVTI MPKDIQLARRIRGERA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	33
1H chemical shifts	33

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H3.1	1

Entities:

Entity 1, H3.1 136 residues - Formula weight is not available

1

MET

ALA

ARG

THR

LYS

GLN

THR

ALA

ARG

LYS

2

SER

THR

GLY

LYS

ALA

PRO

ARG

LYS

GLN

3

LEU

ALA

THR

LYS

ALA

ARG

LYS

SER

ALA

4

PRO

ALA

THR

GLY

VAL

LYS

PRO

HIS

5

ARG

TYR

ARG

PRO

GLY

THR

VAL

ALA

LEU

ARG

6

GLU

ILE

ARG

TYR

GLN

LYS

SER

THR

GLU

7

LEU

ILE

ARG

LYS

LEU

PRO

PHE

GLN

ARG

8

LEU

VAL

ARG

GLU

ILE

ALA

GLN

ASP

PHE

LYS

9

THR

ASP

LEU

ARG

PHE

GLN

SER

ALA

VAL

10

MET

ALA

LEU

GLN

GLU

ALA

CYS

GLU

ALA

TYR

11

LEU

VAL

GLY

LEU

PHE

GLU

ASP

THR

ASN

LEU

12

CYS

ALA

ILE

HIS

ALA

LYS

ARG

VAL

THR

ILE

13

MET

PRO

LYS

ASP

ILE

GLN

LEU

ALA

ARG

14

ILE

ARG

GLY

GLU

ARG

ALA

Samples:

sample_1: H3 N-tail, [U-100% 15N], 42 uM

sample_conditions_1: ionic strength: 25 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRView - chemical shift calculation

NMR spectrometers:

Bruker AVANCE III 950 MHz

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

BMRB Entry 53182