BMRB Entry 51038
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51038
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Title: Hsp104_NTD PubMed: 35305079
Deposition date: 2021-07-29 Original release date: 2022-04-13
Authors: Harari, Anna; Zoltsman, Guy; Rosenzweig, Rina
Citation: Harari, Anna; Zoltsman, Guy; Levin, Tal; Rosenzweig, Rina. "Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation" FEBS J. 289, 5359-5377 (2022).
Assembly members:
entity_1, polymer, 151 residues, Formula weight is not available
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pProEX
Entity Sequences (FASTA):
entity_1: MNDQTQFTERALTILTLAQK
LASDHQHPQLQPIHILAAFI
ETPEDGSVPYLQNLIEKGRY
DYDLFKKVVNRNLVRIPQQQ
PAPAEITPSYALGKVLQDAA
KIQKQQKDSFIAQDHILFAL
FNDSSIQQIFKEAQVDIEAI
KQQALELRGNT
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 357 |
15N chemical shifts | 132 |
1H chemical shifts | 132 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Hsp104_NTD | 1 |
Entities:
Entity 1, Hsp104_NTD 151 residues - Formula weight is not available
1 | MET | ASN | ASP | GLN | THR | GLN | PHE | THR | GLU | ARG | ||||
2 | ALA | LEU | THR | ILE | LEU | THR | LEU | ALA | GLN | LYS | ||||
3 | LEU | ALA | SER | ASP | HIS | GLN | HIS | PRO | GLN | LEU | ||||
4 | GLN | PRO | ILE | HIS | ILE | LEU | ALA | ALA | PHE | ILE | ||||
5 | GLU | THR | PRO | GLU | ASP | GLY | SER | VAL | PRO | TYR | ||||
6 | LEU | GLN | ASN | LEU | ILE | GLU | LYS | GLY | ARG | TYR | ||||
7 | ASP | TYR | ASP | LEU | PHE | LYS | LYS | VAL | VAL | ASN | ||||
8 | ARG | ASN | LEU | VAL | ARG | ILE | PRO | GLN | GLN | GLN | ||||
9 | PRO | ALA | PRO | ALA | GLU | ILE | THR | PRO | SER | TYR | ||||
10 | ALA | LEU | GLY | LYS | VAL | LEU | GLN | ASP | ALA | ALA | ||||
11 | LYS | ILE | GLN | LYS | GLN | GLN | LYS | ASP | SER | PHE | ||||
12 | ILE | ALA | GLN | ASP | HIS | ILE | LEU | PHE | ALA | LEU | ||||
13 | PHE | ASN | ASP | SER | SER | ILE | GLN | GLN | ILE | PHE | ||||
14 | LYS | GLU | ALA | GLN | VAL | ASP | ILE | GLU | ALA | ILE | ||||
15 | LYS | GLN | GLN | ALA | LEU | GLU | LEU | ARG | GLY | ASN | ||||
16 | THR |
Samples:
sample_1: Hsp104_NTD, [U-99% 13C; U-99% 15N], 3.6 mM; sodium azide 0.03%; HEPES 50 mM; potassium chloride 50 mM; DTT 2 mM
sample_conditions_1: pH: 7.5; temperature: 298.15 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.4.2 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts