BMRB Entry 34617
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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/BMR34617
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Title: Solution NMR Structure of the Neh1 Domain of Human Nuclear factor erythroid 2-related factor 2 (NRF2) PubMed: 34524728
Deposition date: 2021-04-13 Original release date: 2021-09-24
Authors: Brueschweiler, S.
Citation: Bruschweiler, Sven; Fuchs, Julian; Bader, Gerd; McConnell, Darryl; Konrat, Robert; Mayer, Moriz. "A Step toward NRF2-DNA Interaction Inhibitors by Fragment-Based NMR Methods" ChemMedChem 16, 3576-3587 (2021).
Assembly members:
entity_1, polymer, 81 residues, 9422.029 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
Entity Sequences (FASTA):
entity_1: GAKHSSRLEAHLTRDELRAK
ALHIPFPVEKIINLPVVDFN
EMMSKEQFNEAQLALIRDIR
RRGKNKVAAQNCRKRKLENI
V
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 209 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 258 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 81 residues - 9422.029 Da.
| 1 | GLY | ALA | LYS | HIS | SER | SER | ARG | LEU | GLU | ALA | ||||
| 2 | HIS | LEU | THR | ARG | ASP | GLU | LEU | ARG | ALA | LYS | ||||
| 3 | ALA | LEU | HIS | ILE | PRO | PHE | PRO | VAL | GLU | LYS | ||||
| 4 | ILE | ILE | ASN | LEU | PRO | VAL | VAL | ASP | PHE | ASN | ||||
| 5 | GLU | MET | MET | SER | LYS | GLU | GLN | PHE | ASN | GLU | ||||
| 6 | ALA | GLN | LEU | ALA | LEU | ILE | ARG | ASP | ILE | ARG | ||||
| 7 | ARG | ARG | GLY | LYS | ASN | LYS | VAL | ALA | ALA | GLN | ||||
| 8 | ASN | CYS | ARG | LYS | ARG | LYS | LEU | GLU | ASN | ILE | ||||
| 9 | VAL |
Samples:
sample_1: neh1, [U-100% 13C; U-100% 15N], 0.5 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCONNH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CCNMR, Skinner, Fogh, Boucher, Ragan, Mureddu, and Vuister - data analysis
ARIA, Linge, O'Donoghue and Nilges - structure calculation
NMR spectrometers:
- Bruker AVANCE III HD 800 MHz
- Bruker Avance NOE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts