BMRB Entry 51262
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51262
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: histone H3 H4 N-tail in nucleosome
Deposition date: 2022-01-06 Original release date: 2022-02-07
Authors: Furukawa, Ayako; Nishimura, Yoshihumi
Citation: Furukawa, Ayako; Wakamori, Masatoshi; Arimura, Yasuhiro; Ohtomo, Hideaki; Tsunaka, Yasuo; Kurumizaka, Hitoshi; Umehara, Takashi; Nishimura, Yoshihumi. "Acetylated histone H4 tail enhances histone H3 tail acetylation by altering their mutual dynamics in the nucleosome" Proc. Natl. Acad. Sci. U. S. A. ., .-..
Assembly members:
entity_1, polymer, 112 residues, Formula weight is not available
entity_2, polymer, 102 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b
Entity Sequences (FASTA):
entity_1: ARTKQTARKSTGGKAPRKQL
ATKAARKSAPATGGVKKPHR
YRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKT
DLRFQSAAIHAKRVTIMPKD
IQLARRIRGERA
entity_2: SGRGKGGKGLGKGGAKRHRK
VLRDNIQGITKPAIRRLARR
GGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKT
VTAMDVVYALKRQGRTLYGF
GG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 127 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 46 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H3 | 1 |
| 2 | H4 | 2 |
Entities:
Entity 1, H3 112 residues - Formula weight is not available
| 1 | ALA | ARG | THR | LYS | GLN | THR | ALA | ARG | LYS | SER | ||||
| 2 | THR | GLY | GLY | LYS | ALA | PRO | ARG | LYS | GLN | LEU | ||||
| 3 | ALA | THR | LYS | ALA | ALA | ARG | LYS | SER | ALA | PRO | ||||
| 4 | ALA | THR | GLY | GLY | VAL | LYS | LYS | PRO | HIS | ARG | ||||
| 5 | TYR | ARG | PRO | GLY | THR | VAL | ALA | LEU | ARG | GLU | ||||
| 6 | ILE | ARG | ARG | TYR | GLN | LYS | SER | THR | GLU | LEU | ||||
| 7 | LEU | ILE | ARG | LYS | LEU | PRO | PHE | GLN | ARG | LEU | ||||
| 8 | VAL | ARG | GLU | ILE | ALA | GLN | ASP | PHE | LYS | THR | ||||
| 9 | ASP | LEU | ARG | PHE | GLN | SER | ALA | ALA | ILE | HIS | ||||
| 10 | ALA | LYS | ARG | VAL | THR | ILE | MET | PRO | LYS | ASP | ||||
| 11 | ILE | GLN | LEU | ALA | ARG | ARG | ILE | ARG | GLY | GLU | ||||
| 12 | ARG | ALA |
Entity 2, H4 102 residues - Formula weight is not available
| 1 | SER | GLY | ARG | GLY | LYS | GLY | GLY | LYS | GLY | LEU | ||||
| 2 | GLY | LYS | GLY | GLY | ALA | LYS | ARG | HIS | ARG | LYS | ||||
| 3 | VAL | LEU | ARG | ASP | ASN | ILE | GLN | GLY | ILE | THR | ||||
| 4 | LYS | PRO | ALA | ILE | ARG | ARG | LEU | ALA | ARG | ARG | ||||
| 5 | GLY | GLY | VAL | LYS | ARG | ILE | SER | GLY | LEU | ILE | ||||
| 6 | TYR | GLU | GLU | THR | ARG | GLY | VAL | LEU | LYS | VAL | ||||
| 7 | PHE | LEU | GLU | ASN | VAL | ILE | ARG | ASP | ALA | VAL | ||||
| 8 | THR | TYR | THR | GLU | HIS | ALA | LYS | ARG | LYS | THR | ||||
| 9 | VAL | THR | ALA | MET | ASP | VAL | VAL | TYR | ALA | LEU | ||||
| 10 | LYS | ARG | GLN | GLY | ARG | THR | LEU | TYR | GLY | PHE | ||||
| 11 | GLY | GLY |
Samples:
sample_1: H3 histone tail, [U-13C; U-15N; U-2H], 70 uM; H4 histone tail, [U-100% 13C; U-100% 15N], 70 uM; DTT 2 mM
sample_2: H3 histone tail, [U-13C; U-15N; U-2H], 70 uM; H4 histone tail, [U-100% 13C; U-100% 15N], 70 uM; DTT 2 mM
sample_conditions_1: ionic strength: 25 mM; pH: 6; temperature: 298 K
sample_conditions_2: ionic strength: 25 mM; pH: 6; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3DHN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
MagRO-NMRView - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts