BMRB Entry 30340
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30340
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Title: Structures of REV1 UBM2 domain complex with ubiquitin and with the first small-molecule that inhibits the REV1 UBM2-ubiquitin interaction PubMed: 29864443
Deposition date: 2017-09-06 Original release date: 2018-06-21
Authors: Fujii, N.; Vanarotti, M.
Citation: Vanarotti, Murugendra; Grace, Christy; Miller, Darcie; Actis, Marcelo; Inoue, Akira; Evison, Benjamin; Vaithiyalingam, Sivaraja; Singh, Aman; McDonald, Ezelle; Fujii, Naoaki. "Structures of REV1 UBM2 Domain Complex with Ubiquitin and with a Small-Molecule that Inhibits the REV1 UBM2-Ubiquitin Interaction" J. Mol. Biol. 430, 2857-2872 (2018).
Assembly members:
entity_1, polymer, 72 residues, 7813.632 Da.
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-Pichia pastoris shuttle vector pPpARG4
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHHHLNGSSLVP
RGSIKSSGLESNSDAGINLI
ALPAFSQVDPEVFAALPAEL
QRELKAAYDQRQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 58 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 72 residues - 7813.632 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | HIS | LEU | ASN | GLY | SER | SER | LEU | VAL | PRO | ||||
| 3 | ARG | GLY | SER | ILE | LYS | SER | SER | GLY | LEU | GLU | ||||
| 4 | SER | ASN | SER | ASP | ALA | GLY | ILE | ASN | LEU | ILE | ||||
| 5 | ALA | LEU | PRO | ALA | PHE | SER | GLN | VAL | ASP | PRO | ||||
| 6 | GLU | VAL | PHE | ALA | ALA | LEU | PRO | ALA | GLU | LEU | ||||
| 7 | GLN | ARG | GLU | LEU | LYS | ALA | ALA | TYR | ASP | GLN | ||||
| 8 | ARG | GLN |
Samples:
sample_1: REV1 UBM2, [U-13C; U-15N], 0.5 mM
sample_2: REV1 UBM2, [U-99% 15N], 0.5 mM
sample_conditions_1: ionic strength: 0.5 mM; pH: 7.0; pressure: 1 mbar; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | anisotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - peak picking, refinement
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
TOPSPIN, Bruker Biospin - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts