BMRB Entry 51376
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51376
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone chemical shifts of Spd1 PubMed: 35974206
Deposition date: 2022-03-21 Original release date: 2022-09-13
Authors: Broendum, Sebastian; Prestel, Andreas; Kragelund, Birthe
Citation: Dreier, Jesper; Prestel, Andreas; Martins, Joao; Brondum, Sebastian; Nielsen, Olaf; Garbers, Anna; Suga, Hiroaki; Boomsma, Wouter; Rogers, Joseph; Hartmann-Petersen, Rasmus; Kragelund, Birthe. "A context-dependent and disordered ubiquitin-binding motif" Cell. Mol. Life Sci. 79, 484-484 (2022).
Assembly members:
Spd1, polymer, 124 residues, Formula weight is not available
Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24b
Entity Sequences (FASTA):
Spd1: MHSSKRVMTTKTHVEQPESS
MRPQLPESIQGSLMDVGMRV
RKSISTGYKSKQTTFPAYNP
PLYNTVSENIALKNTAFSYE
PNGTKRPFEQAIPNYNWANP
PQDFEEPEWLKPFDVVMEGT
NERL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 344 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 103 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Spd1 | 1 |
Entities:
Entity 1, Spd1 124 residues - Formula weight is not available
| 1 | MET | HIS | SER | SER | LYS | ARG | VAL | MET | THR | THR | ||||
| 2 | LYS | THR | HIS | VAL | GLU | GLN | PRO | GLU | SER | SER | ||||
| 3 | MET | ARG | PRO | GLN | LEU | PRO | GLU | SER | ILE | GLN | ||||
| 4 | GLY | SER | LEU | MET | ASP | VAL | GLY | MET | ARG | VAL | ||||
| 5 | ARG | LYS | SER | ILE | SER | THR | GLY | TYR | LYS | SER | ||||
| 6 | LYS | GLN | THR | THR | PHE | PRO | ALA | TYR | ASN | PRO | ||||
| 7 | PRO | LEU | TYR | ASN | THR | VAL | SER | GLU | ASN | ILE | ||||
| 8 | ALA | LEU | LYS | ASN | THR | ALA | PHE | SER | TYR | GLU | ||||
| 9 | PRO | ASN | GLY | THR | LYS | ARG | PRO | PHE | GLU | GLN | ||||
| 10 | ALA | ILE | PRO | ASN | TYR | ASN | TRP | ALA | ASN | PRO | ||||
| 11 | PRO | GLN | ASP | PHE | GLU | GLU | PRO | GLU | TRP | LEU | ||||
| 12 | LYS | PRO | PHE | ASP | VAL | VAL | MET | GLU | GLY | THR | ||||
| 13 | ASN | GLU | ARG | LEU |
Samples:
sample_1: Spd1, [U-99% 13C; U-99% 15N], 50 ± 1 uM; DSS 250 uM; sodium chloride 100 mM; sodium phosphate 10 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 277.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.5 - chemical shift assignment
NMRDraw v9.9 - processing
NMR spectrometers:
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts