BMRB Entry 27143
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27143
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Title: Backbone and side chain chemical shift assignments of human PACT-D3 L273R PubMed: 29045748
Deposition date: 2017-06-16 Original release date: 2019-04-15
Authors: Heyam, Alex
Citation: Heyam, Alex; Coupland, Claire; Degut, Clement; Haley, Ruth; Baxter, Nicola; Jakob, Leonhard; Aguiar, Pedro; Meister, Gunter; Williamson, Michael; Lagos, Dimitris; Plevin, Michael. "Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins." Nucleic Acids Res. 45, 12577-12584 (2017).
Assembly members:
P3a_L273R, polymer, 79 residues, 8545.5222 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 Vector: pETFPP_2
Entity Sequences (FASTA):
P3a_L273R: GPAMTDYIQLLSEIAKEQGF
NITYLDIDELSANGQYQCRA
ELSTSPITVCHGSGISCGNA
QSDAAHNALQYLKIIAERK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 332 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P3a L273R | 1 |
Entities:
Entity 1, P3a L273R 79 residues - 8545.5222 Da.
The first four residues are non-native, and are left after cleavage of a solubility tag. This is followed by native residues 239-313.
| 1 | GLY | PRO | ALA | MET | THR | ASP | TYR | ILE | GLN | LEU | ||||
| 2 | LEU | SER | GLU | ILE | ALA | LYS | GLU | GLN | GLY | PHE | ||||
| 3 | ASN | ILE | THR | TYR | LEU | ASP | ILE | ASP | GLU | LEU | ||||
| 4 | SER | ALA | ASN | GLY | GLN | TYR | GLN | CYS | ARG | ALA | ||||
| 5 | GLU | LEU | SER | THR | SER | PRO | ILE | THR | VAL | CYS | ||||
| 6 | HIS | GLY | SER | GLY | ILE | SER | CYS | GLY | ASN | ALA | ||||
| 7 | GLN | SER | ASP | ALA | ALA | HIS | ASN | ALA | LEU | GLN | ||||
| 8 | TYR | LEU | LYS | ILE | ILE | ALA | GLU | ARG | LYS |
Samples:
sidechain_sample: P3a_L273R, [U-13C; U-15N], 0.7 mM; sodium phosphate 10 mM; sodium chloride 50 mM; beta-mercaptoethanol 4 mM; DSS 5 uM
backbone_sample: P3a_L273R, [U-13C; U-15N], 1.1 mM; sodium chloride 50 mM; MES 20 mM; TCEP 5 mM; DSS 50 uM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | backbone_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | backbone_sample | isotropic | sample_conditions_1 |
| CBCA(CO)NH | backbone_sample | isotropic | sample_conditions_1 |
| 3D HNCO | backbone_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sidechain_sample | isotropic | sample_conditions_1 |
| Aliphatic 1H-13C HSQC | sidechain_sample | isotropic | sample_conditions_1 |
| Aromatic 1H-13C HSQC | sidechain_sample | isotropic | sample_conditions_1 |
Software:
CcpNmr_Analysis v2.4, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts