BMRB Entry 27148
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27148
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Title: Backbone and side chain chemical shift assignments of wild-type PACT-D3. PubMed: 29045748
Deposition date: 2017-06-19 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:
PACT-D3_wt, polymer, 79 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: pETFPP_2
Entity Sequences (FASTA):
PACT-D3_wt: GPAMTDYIQLLSEIAKEQGF
NITYLDIDELSANGQYQCLA
ELSTSPITVCHGSGISCGNA
QSDAAHNALQYLKIIAERK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 584 |
| 15N chemical shifts | 155 |
| 1H chemical shifts | 893 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PACT-D3 state_A | 1 |
| 2 | PACT-D3 state_B | 1 |
Entities:
Entity 1, PACT-D3 state_A 79 residues - Formula weight is not available
The first four residues (GPAM) are non-native, and remain after cleavage of an affinity tag. This is followed by PACT 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 | LEU | 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:
backbone_assignment: PACT-D3_wt, [U-13C; U-15N], 1.3 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 mM; DSS 50 uM
sidechain_assignment: PACT-D3_wt, [U-13C; U-15N], 2.4 mM; sodium chloride 50 mM; MES 20 mM; TCEP 10 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 SOFAST-HMQC | backbone_assignment | isotropic | sample_conditions_1 |
| HNCACB | backbone_assignment | isotropic | sample_conditions_1 |
| CBCACONH | backbone_assignment | isotropic | sample_conditions_1 |
| HNCO | sidechain_assignment | isotropic | sample_conditions_1 |
| CC(CO)NH-TOCSY | sidechain_assignment | isotropic | sample_conditions_1 |
| HCCH-TOCSY | sidechain_assignment | isotropic | sample_conditions_1 |
| 1H-13C HSQC | sidechain_assignment | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0-3.5, Bruker Biospin - collection, processing
CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts