BMRB Entry 18951
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PDB ID: 2m3a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18951
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: De Rop, Valerie; Dorn, Jonas; Osborne, Michael; Boisvert, Jacques; Ryan, Joel; Padeganeh, Abbas; Moevus, Corentin; Borden, Katherine; Maddox, Amy; Maddox, Paul. "Centromere epigenome stability is mediated by structural recognition by the Centromere Licensing Complex" Science ., .-..
Assembly members:
KNL2, polymer, 134 residues, 15216.123 Da.
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P1
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 170 |
| 15N chemical shifts | 47 |
| 1H chemical shifts | 351 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MYB-like DNA binding domain of KNL-2 from C. Elegans | 1 |
Entities:
Entity 1, MYB-like DNA binding domain of KNL-2 from C. Elegans 134 residues - 15216.123 Da.
Residues 1-5 (GPLGS) are a cloning artefact
| 1 | GLY | PRO | LEU | GLY | SER | VAL | ALA | LYS | LYS | ILE | ||||
| 2 | THR | TRP | ARG | LYS | GLN | ASP | LEU | ASP | ARG | LEU | ||||
| 3 | LYS | ARG | VAL | ILE | ALA | LEU | LYS | LYS | PRO | SER | ||||
| 4 | ALA | SER | ASP | ALA | ASP | TRP | THR | GLU | VAL | LEU | ||||
| 5 | ARG | LEU | LEU | ALA | LYS | GLU | GLY | VAL | VAL | GLU | ||||
| 6 | PRO | GLU | VAL | VAL | ARG | GLN | ILE | ALA | ILE | THR | ||||
| 7 | ARG | LEU | LYS | TRP | VAL | GLU | PRO | GLY | PRO | LEU | ||||
| 8 | GLY | SER | VAL | ALA | LYS | LYS | ILE | THR | TRP | ARG | ||||
| 9 | LYS | GLN | ASP | LEU | ASP | ARG | LEU | LYS | ARG | VAL | ||||
| 10 | ILE | ALA | LEU | LYS | LYS | PRO | SER | ALA | SER | ASP | ||||
| 11 | ALA | ASP | TRP | THR | GLU | VAL | LEU | ARG | LEU | LEU | ||||
| 12 | ALA | LYS | GLU | GLY | VAL | VAL | GLU | PRO | GLU | VAL | ||||
| 13 | VAL | ARG | GLN | ILE | ALA | ILE | THR | ARG | LEU | LYS | ||||
| 14 | TRP | VAL | GLU | PRO |
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