BMRB Entry 30904
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30904
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Title: Rules for designing protein fold switches and their implications for the folding code PubMed: 36702827
Deposition date: 2021-05-04 Original release date: 2022-05-09
Authors: He, Y.; Chen, Y.; Ruan, B.; Choi, J.; Chen, Y.; Motabar, D.; Solomon, T.; Simmerman, R.; Kauffman, T.; Gallagher, T.; Bryan, P.; Orban, J.
Citation: Ruan, Biao; He, Yanan; Chen, Yingwei; Choi, Eun Jung; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D. Travis; Orban, John; Bryan, Philip N.. "Design and characterization of a protein fold switching network" Nat. Commun. 14, 431-431 (2023).
Assembly members:
entity_1, polymer, 87 residues, 10073.049 Da.
Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: TTYKYILNLKFAFGDTNSEA
VDAAEAEKKFKQYANDHGVD
GEWTYDDATKTFTVTAKDSH
ADRVRELAQRLRQRPRVERV
EITEVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 287 |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 333 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 87 residues - 10073.049 Da.
| 1 | THR | THR | TYR | LYS | TYR | ILE | LEU | ASN | LEU | LYS | ||||
| 2 | PHE | ALA | PHE | GLY | ASP | THR | ASN | SER | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | ALA | GLU | ALA | GLU | LYS | LYS | PHE | ||||
| 4 | LYS | GLN | TYR | ALA | ASN | ASP | HIS | GLY | VAL | ASP | ||||
| 5 | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | ALA | LYS | ASP | SER | HIS | ||||
| 7 | ALA | ASP | ARG | VAL | ARG | GLU | LEU | ALA | GLN | ARG | ||||
| 8 | LEU | ARG | GLN | ARG | PRO | ARG | VAL | GLU | ARG | VAL | ||||
| 9 | GLU | ILE | THR | GLU | VAL | THR | GLU |
Samples:
sample_1: Sb3, [U-13C; U-15N], 0.3 mM; 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 HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15NNOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13CNOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al., Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation
NMRFAM-SPARKY, NMRFAM - chemical shift assignment, peak picking
TopSpin, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AVANCE DMX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts