BMRB Entry 27792
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27792
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Horn, Velten; Uckelmann, Michael; Zhang, Heyi; Eerland, Jelmer; Aarsman, Ivette; Le Paige, Ulric; Davidovich, Chen; Sixma, Titia; van Ingen, Hugo. "Structural basis of specific H2A K13/K15 ubiquitination by RNF168." Nat. Commun. 10, 1751-1751 (2019).
PubMed: 30988309
Assembly members:
RNF168_RING, polymer, 113 residues, Formula weight is not available
Histone_H2A, polymer, 123 residues, Formula weight is not available
Histone_H2B, polymer, 122 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
Entity Sequences (FASTA):
RNF168_RING: MALPKDAIPSLSECQCGICM
EILVEPVTLPCNHTLCKPCF
QSTVEKASLCCPFCRRRVSS
WTRYHTRRNSLVNVELWTII
QKHYPRECKLRASGQESEEV
ADDYQPVRLLSKP
Histone_H2A: SGRGKGGKVKGKAKSRSNRA
GLQFPVGRIHRLLRKGNYAE
RVGAGAPVYLAAVMEYLAAE
VLELAGNAARDNKKTRIIPR
HLQLAIRNDEELNKLLSGVT
IAQGGVLPNIQAVLLPKKTE
KKA
Histone_H2B: PPKTSGKAAKKAGKAQKNIT
KTDKKKKRKRKESYAIYIYK
VLKQVHPDTGISSKAMSIMN
SFVNDIFERIAAEASRLAHY
NKRSTITSREIQTAVRLLLP
GELAKHAVSEGTKAVTKYTS
SK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 160 |
| 1H chemical shifts | 160 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RNF168 | 1 |
| 2 | Histone H2A | 2 |
| 3 | Histone H2B | 3 |
Entities:
Entity 1, RNF168 113 residues - Formula weight is not available
| 1 | MET | ALA | LEU | PRO | LYS | ASP | ALA | ILE | PRO | SER | ||||
| 2 | LEU | SER | GLU | CYS | GLN | CYS | GLY | ILE | CYS | MET | ||||
| 3 | GLU | ILE | LEU | VAL | GLU | PRO | VAL | THR | LEU | PRO | ||||
| 4 | CYS | ASN | HIS | THR | LEU | CYS | LYS | PRO | CYS | PHE | ||||
| 5 | GLN | SER | THR | VAL | GLU | LYS | ALA | SER | LEU | CYS | ||||
| 6 | CYS | PRO | PHE | CYS | ARG | ARG | ARG | VAL | SER | SER | ||||
| 7 | TRP | THR | ARG | TYR | HIS | THR | ARG | ARG | ASN | SER | ||||
| 8 | LEU | VAL | ASN | VAL | GLU | LEU | TRP | THR | ILE | ILE | ||||
| 9 | GLN | LYS | HIS | TYR | PRO | ARG | GLU | CYS | LYS | LEU | ||||
| 10 | ARG | ALA | SER | GLY | GLN | GLU | SER | GLU | GLU | VAL | ||||
| 11 | ALA | ASP | ASP | TYR | GLN | PRO | VAL | ARG | LEU | LEU | ||||
| 12 | SER | LYS | PRO |
Entity 2, Histone H2A 123 residues - Formula weight is not available
| 1 | SER | GLY | ARG | GLY | LYS | GLY | GLY | LYS | VAL | LYS | ||||
| 2 | GLY | LYS | ALA | LYS | SER | ARG | SER | ASN | ARG | ALA | ||||
| 3 | GLY | LEU | GLN | PHE | PRO | VAL | GLY | ARG | ILE | HIS | ||||
| 4 | ARG | LEU | LEU | ARG | LYS | GLY | ASN | TYR | ALA | GLU | ||||
| 5 | ARG | VAL | GLY | ALA | GLY | ALA | PRO | VAL | TYR | LEU | ||||
| 6 | ALA | ALA | VAL | MET | GLU | TYR | LEU | ALA | ALA | GLU | ||||
| 7 | VAL | LEU | GLU | LEU | ALA | GLY | ASN | ALA | ALA | ARG | ||||
| 8 | ASP | ASN | LYS | LYS | THR | ARG | ILE | ILE | PRO | ARG | ||||
| 9 | HIS | LEU | GLN | LEU | ALA | ILE | ARG | ASN | ASP | GLU | ||||
| 10 | GLU | LEU | ASN | LYS | LEU | LEU | SER | GLY | VAL | THR | ||||
| 11 | ILE | ALA | GLN | GLY | GLY | VAL | LEU | PRO | ASN | ILE | ||||
| 12 | GLN | ALA | VAL | LEU | LEU | PRO | LYS | LYS | THR | GLU | ||||
| 13 | LYS | LYS | ALA |
Entity 3, Histone H2B 122 residues - Formula weight is not available
| 1 | PRO | PRO | LYS | THR | SER | GLY | LYS | ALA | ALA | LYS | ||||
| 2 | LYS | ALA | GLY | LYS | ALA | GLN | LYS | ASN | ILE | THR | ||||
| 3 | LYS | THR | ASP | LYS | LYS | LYS | LYS | ARG | LYS | ARG | ||||
| 4 | LYS | GLU | SER | TYR | ALA | ILE | TYR | ILE | TYR | LYS | ||||
| 5 | VAL | LEU | LYS | GLN | VAL | HIS | PRO | ASP | THR | GLY | ||||
| 6 | ILE | SER | SER | LYS | ALA | MET | SER | ILE | MET | ASN | ||||
| 7 | SER | PHE | VAL | ASN | ASP | ILE | PHE | GLU | ARG | ILE | ||||
| 8 | ALA | ALA | GLU | ALA | SER | ARG | LEU | ALA | HIS | TYR | ||||
| 9 | ASN | LYS | ARG | SER | THR | ILE | THR | SER | ARG | GLU | ||||
| 10 | ILE | GLN | THR | ALA | VAL | ARG | LEU | LEU | LEU | PRO | ||||
| 11 | GLY | GLU | LEU | ALA | LYS | HIS | ALA | VAL | SER | GLU | ||||
| 12 | GLY | THR | LYS | ALA | VAL | THR | LYS | TYR | THR | SER | ||||
| 13 | SER | LYS |
Samples:
sample_1: Histone H2A, [U-2H], 200 uM; Histone H2B, [U-2H; U-15N], 200 uM; Tris 25 mM; NaCl 100 mM; ZnCl2 10 mM; DTT 3 mM
sample_2: Histone H2A, [U-2H], 200 uM; Histone H2B, [U-2H; U-15N], 200 uM; RNF168 RING 32 uM; Tris 25 mM; NaCl 100 mM; ZnCl2 10 mM; DTT 3 mM
sample_conditions_1: ionic strength: 100 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_2 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance III HD 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks