BMRB Entry 27475
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27475
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Title: NMR assignments of the mammalian proteasome subunit DSS1.
Deposition date: 2018-05-09 Original release date: 2019-05-10
Authors: Yu, Liping; Hengel, Sarah; Spies, Maria
Citation: Hengel, Sarah; Yu, Liping; Spies, Maria. "NMR assignments of the mammalian proteasome subunit DSS1." Nat. Commun. ., .-..
Assembly members:
DSS1, polymer, 87 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: pGEX-KG
Entity Sequences (FASTA):
DSS1: GSPGISGGGGGILDSMGMSE
KKQPVDLGLLEEDDEFEEFP
AEDWAGLDEDEDAHVWEDNW
DDDNVEDDFSNQLRAELEKH
GYKMETS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 244 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 81 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DSS1 monomer | 1 |
Entities:
Entity 1, DSS1 monomer 87 residues - Formula weight is not available
| 1 | GLY | SER | PRO | GLY | ILE | SER | GLY | GLY | GLY | GLY | ||||
| 2 | GLY | ILE | LEU | ASP | SER | MET | GLY | MET | SER | GLU | ||||
| 3 | LYS | LYS | GLN | PRO | VAL | ASP | LEU | GLY | LEU | LEU | ||||
| 4 | GLU | GLU | ASP | ASP | GLU | PHE | GLU | GLU | PHE | PRO | ||||
| 5 | ALA | GLU | ASP | TRP | ALA | GLY | LEU | ASP | GLU | ASP | ||||
| 6 | GLU | ASP | ALA | HIS | VAL | TRP | GLU | ASP | ASN | TRP | ||||
| 7 | ASP | ASP | ASP | ASN | VAL | GLU | ASP | ASP | PHE | SER | ||||
| 8 | ASN | GLN | LEU | ARG | ALA | GLU | LEU | GLU | LYS | HIS | ||||
| 9 | GLY | TYR | LYS | MET | GLU | THR | SER |
Samples:
sample_1: DSS1, [U-100% 13C; U-100% 15N], 0.22 mM; TRIS 25 mM; sodium chloride 50 mM; EDTA 25 uM; DTT 2 mM
sample_conditions_1: ionic strength: 75 mM; pH: 7.5; pressure: 1 atm; temperature: 278 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 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts