BMRB Entry 50910
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50910
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Title: Rules for designing protein fold switches and their implications for the folding code PubMed: 36702827
Deposition date: 2021-04-22 Original release date: 2023-01-03
Authors: He, Yanan; Chen, Yingwei; Ruan, Biao; Choi, Eun; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D,Travis; Bryan, Philip; Orban, John
Citation: He, Yanan; Chen, Yingwei; Ruan, Biao; Choi, Eun; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D,Travis; Bryan, Philip; Orban, John. "Design and characterization of a protein fold switching network" Nat. Commun. 14, 431-431 (2023).
Assembly members:
entity_1, polymer, 56 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pA-YRGL
Entity Sequences (FASTA):
entity_1: ATFKLVLNGKTLKGETTTEA
VDAATALKNFGAYAQDVGVD
GAWTYDDATKTFTVGE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 161 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 116 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | B1 | 1 |
Entities:
Entity 1, B1 56 residues - Formula weight is not available
| 1 | ALA | THR | PHE | LYS | LEU | VAL | LEU | ASN | GLY | LYS | ||||
| 2 | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | ALA | THR | ALA | LEU | LYS | ASN | PHE | ||||
| 4 | GLY | ALA | TYR | ALA | GLN | ASP | VAL | GLY | VAL | ASP | ||||
| 5 | GLY | ALA | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
| 6 | THR | PHE | THR | VAL | GLY | GLU |
Samples:
sample_1: B1, [U-13C; U-15N], 0.3 mM; D2O 5 V/V%; potassium phosphate 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3DHNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3DCBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3DHNHA | sample_1 | isotropic | sample_conditions_1 |
| 3DHNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.61 - collection
NMRFAM-SPARKY - 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