BMRB Entry 27250
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27250
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Citation: Dobrovolska, Olena; Brilkov, Maxim; Odegard, Oyvind; Aasland, Rein; Halskau, Oyvind. "1H, 13C, and 15N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides" Biomol. NMR Assign. 12, 215-220 (2018).
PubMed: 29453713
Assembly members:
CW42, polymer, 79 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSXG
Entity Sequences (FASTA):
CW42: GSRRASVGSEFTESAWVRCD
DCFKWRRIPASVVGSIDESS
RWICMNNSDKRFADCSKSQE
MSNEEINEELGIGQDEADA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 144 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 74 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CW domain of ASHH2 methyltransferase | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, CW domain of ASHH2 methyltransferase 79 residues - Formula weight is not available
| 1 | GLY | SER | ARG | ARG | ALA | SER | VAL | GLY | SER | GLU | ||||
| 2 | PHE | THR | GLU | SER | ALA | TRP | VAL | ARG | CYS | ASP | ||||
| 3 | ASP | CYS | PHE | LYS | TRP | ARG | ARG | ILE | PRO | ALA | ||||
| 4 | SER | VAL | VAL | GLY | SER | ILE | ASP | GLU | SER | SER | ||||
| 5 | ARG | TRP | ILE | CYS | MET | ASN | ASN | SER | ASP | LYS | ||||
| 6 | ARG | PHE | ALA | ASP | CYS | SER | LYS | SER | GLN | GLU | ||||
| 7 | MET | SER | ASN | GLU | GLU | ILE | ASN | GLU | GLU | LEU | ||||
| 8 | GLY | ILE | GLY | GLN | ASP | GLU | ALA | ASP | ALA |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
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