BMRB Entry 51282
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51282
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Title: NMR Backbone Assignment of Nup358-Min PubMed: 35229716
Deposition date: 2022-01-14 Original release date: 2022-01-25
Authors: Gibson, James; Wang, Chunyu; Zhao, Jing
Citation: Gibson, James; Cui, Heying; Ali, M Yusuf; Zhao, Xiaoxin; Debler, Erik; Zhao, Jing; Trybus, Kathleen; Solmaz, Sozanne; Wang, Chunyu. "Coil-to-alpha-helix transition at the Nup358-BicD2 interface activates BicD2 for dynein recruitment" eLife 11, e74714-e74714 (2022).
Assembly members:
entity_1, polymer, 98 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 Vector: pGEX6p1
Entity Sequences (FASTA):
entity_1: GPLGSDIPLQTPHKLVDTGR
AAKLIQRAEEMKSGLKDFKT
FLTNDQTKVTEEENKGSGTG
AAGASDTTIKPNPENTGPTL
EWDNYDLREDALDDSVSS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 257 |
15N chemical shifts | 78 |
1H chemical shifts | 78 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Nup358-Min | 1 |
Entities:
Entity 1, Nup358-Min 98 residues - Formula weight is not available
1 | GLY | PRO | LEU | GLY | SER | ASP | ILE | PRO | LEU | GLN | ||||
2 | THR | PRO | HIS | LYS | LEU | VAL | ASP | THR | GLY | ARG | ||||
3 | ALA | ALA | LYS | LEU | ILE | GLN | ARG | ALA | GLU | GLU | ||||
4 | MET | LYS | SER | GLY | LEU | LYS | ASP | PHE | LYS | THR | ||||
5 | PHE | LEU | THR | ASN | ASP | GLN | THR | LYS | VAL | THR | ||||
6 | GLU | GLU | GLU | ASN | LYS | GLY | SER | GLY | THR | GLY | ||||
7 | ALA | ALA | GLY | ALA | SER | ASP | THR | THR | ILE | LYS | ||||
8 | PRO | ASN | PRO | GLU | ASN | THR | GLY | PRO | THR | LEU | ||||
9 | GLU | TRP | ASP | ASN | TYR | ASP | LEU | ARG | GLU | ASP | ||||
10 | ALA | LEU | ASP | ASP | SER | VAL | SER | SER |
Samples:
sample_1: Nup358-min, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 20 mM; TCEP 0.5 mM
sample_conditions_1: pH: 7.5; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
SMILE - Reconstruction of NUS
NMRFAM-SPARKY - data analysis
PINE - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts