BMRB Entry 50134
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50134
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Title: Backbone 1H and 15N chemical shift assignments of chimeric SC Sup35NM, 4MT-A PubMed: 32284601
Deposition date: 2019-12-15 Original release date: 2020-03-30
Authors: Shida, Toshinobu; Kamatari, Yuji; Yamaguchi, Yoshiki; Kuwata, Kazuo; Tanaka, Motomasa
Citation: Shida, Toshinobu; Kamatari, Yuji; Yoda, Takao; Yamaguchi, Yoshiki; Feig, Michael; Ohhashi, Yumiko; Sugita, Yuji; Kuwata, Kazuo; Tanaka, Motomasa. "Short Disordered Protein Segment Regulates Cross-Species Transmission of a Yeast Prion" Nat. Chem. Biol. 16, 756-765 (2020).
Assembly members:
entity_1, polymer, 260 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: pET29b
Entity Sequences (FASTA):
entity_1: MSDSNQGNNQQNYQQYNQYG
NQNQYNNRYQGYQAYNAQAQ
PAGGYYQNYQGYSGYQQGGY
QQYNPDAGYQQQYNPQGGYQ
QYNPQGGYQQQFNPQGGRGN
YKNFNYNNNLQGYQAGFQPQ
SQGMSLNDFQKQQKQAAPKP
KKTLKLVSSSGIKLANATKK
VGTKPAESDKKEEEKSAETK
EPTKEPTKVEEPVKKEEKPV
QTEEKTEEKSELPKVEDLKI
SESTHNTNNANVTSADALIK
EQEEEVDDEVVNDHHHHHHH
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 244 |
1H chemical shifts | 244 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | 4MT-A | 1 |
Entities:
Entity 1, 4MT-A 260 residues - Formula weight is not available
1 | MET | SER | ASP | SER | ASN | GLN | GLY | ASN | ASN | GLN | |
2 | GLN | ASN | TYR | GLN | GLN | TYR | ASN | GLN | TYR | GLY | |
3 | ASN | GLN | ASN | GLN | TYR | ASN | ASN | ARG | TYR | GLN | |
4 | GLY | TYR | GLN | ALA | TYR | ASN | ALA | GLN | ALA | GLN | |
5 | PRO | ALA | GLY | GLY | TYR | TYR | GLN | ASN | TYR | GLN | |
6 | GLY | TYR | SER | GLY | TYR | GLN | GLN | GLY | GLY | TYR | |
7 | GLN | GLN | TYR | ASN | PRO | ASP | ALA | GLY | TYR | GLN | |
8 | GLN | GLN | TYR | ASN | PRO | GLN | GLY | GLY | TYR | GLN | |
9 | GLN | TYR | ASN | PRO | GLN | GLY | GLY | TYR | GLN | GLN | |
10 | GLN | PHE | ASN | PRO | GLN | GLY | GLY | ARG | GLY | ASN | |
11 | TYR | LYS | ASN | PHE | ASN | TYR | ASN | ASN | ASN | LEU | |
12 | GLN | GLY | TYR | GLN | ALA | GLY | PHE | GLN | PRO | GLN | |
13 | SER | GLN | GLY | MET | SER | LEU | ASN | ASP | PHE | GLN | |
14 | LYS | GLN | GLN | LYS | GLN | ALA | ALA | PRO | LYS | PRO | |
15 | LYS | LYS | THR | LEU | LYS | LEU | VAL | SER | SER | SER | |
16 | GLY | ILE | LYS | LEU | ALA | ASN | ALA | THR | LYS | LYS | |
17 | VAL | GLY | THR | LYS | PRO | ALA | GLU | SER | ASP | LYS | |
18 | LYS | GLU | GLU | GLU | LYS | SER | ALA | GLU | THR | LYS | |
19 | GLU | PRO | THR | LYS | GLU | PRO | THR | LYS | VAL | GLU | |
20 | GLU | PRO | VAL | LYS | LYS | GLU | GLU | LYS | PRO | VAL | |
21 | GLN | THR | GLU | GLU | LYS | THR | GLU | GLU | LYS | SER | |
22 | GLU | LEU | PRO | LYS | VAL | GLU | ASP | LEU | LYS | ILE | |
23 | SER | GLU | SER | THR | HIS | ASN | THR | ASN | ASN | ALA | |
24 | ASN | VAL | THR | SER | ALA | ASP | ALA | LEU | ILE | LYS | |
25 | GLU | GLN | GLU | GLU | GLU | VAL | ASP | ASP | GLU | VAL | |
26 | VAL | ASN | ASP | HIS | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: 4MT-A, [U-99% 15N], 60 uM; MES 50 mM; H2O 90%; D2O, [U-99% 2H], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 4.0; pressure: 1 atm; temperature: 310.15 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.114, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts