BMRB Entry 50680
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50680
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Title: Red1 backbone chemical shift assignments for residues 288-322 PubMed: 36774373
Deposition date: 2020-12-22 Original release date: 2022-11-30
Authors: Soni, Komal; Sinning, Irmgard
Citation: Soni, Komal; Sivadas, Anusree; Horvath, Attila; Dobrev, Nikolay; Hayashi, Rippei; Kiss, Leo; Simon, Bernd; Wild, Klemens; Sinning, Irmgard; Fischer, Tamas. "Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex" Nat. Commun. 14, 772-772 (2023).
Assembly members:
entity_1, polymer, 115 residues, Formula weight is not available
Natural source: Common Name: fission yeast Taxonomy ID: 1893 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet21d
Entity Sequences (FASTA):
entity_1: MKQYKLILNGKTLKGETTTE
AVDAATAEKVFKQYANDNGV
DGEWTYDDATKTFTVTEGSG
SGSENLYFQGAMGISLPLLK
QDDWLSSSKPFGSSTPNVVI
EFDSDDDGSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 305 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 105 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GB1-TEV-Red1 | 1 |
Entities:
Entity 1, GB1-TEV-Red1 115 residues - Formula weight is not available
The sequence contains GB1-tag and TEV protease cleavage site at the N-terminus followed by Red1 residues 288-322 and a C-terminal 6xHis-tag.
| 1 | MET | LYS | GLN | TYR | LYS | LEU | ILE | LEU | ASN | GLY | ||||
| 2 | LYS | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ||||
| 3 | ALA | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | VAL | ||||
| 4 | PHE | LYS | GLN | TYR | ALA | ASN | ASP | ASN | GLY | VAL | ||||
| 5 | ASP | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | ||||
| 6 | LYS | THR | PHE | THR | VAL | THR | GLU | GLY | SER | GLY | ||||
| 7 | SER | GLY | SER | GLU | ASN | LEU | TYR | PHE | GLN | GLY | ||||
| 8 | ALA | MET | GLY | ILE | SER | LEU | PRO | LEU | LEU | LYS | ||||
| 9 | GLN | ASP | ASP | TRP | LEU | SER | SER | SER | LYS | PRO | ||||
| 10 | PHE | GLY | SER | SER | THR | PRO | ASN | VAL | VAL | ILE | ||||
| 11 | GLU | PHE | ASP | SER | ASP | ASP | ASP | GLY | SER | HIS | ||||
| 12 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: GB1-TEV-Red1, [U-100% 13C; U-100% 15N], 1 mM; Sodium phosphate 20 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
ANALYSIS - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts