BMRB Entry 30905
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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/BMR30905
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Rules for designing protein fold switches and their implications for the folding code PubMed: 36702827
Deposition date: 2021-05-05 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, 95 residues, 10560.923 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: SAGIATFKLVLNGKTLKGET
TTEAVDAATALKNFGAYAQD
VGVDGAWTYDDATKTFTVGE
RLIFKVKMPEDRMNDLARQL
RQRDNVSRVEVTRYK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 208 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 128 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 95 residues - 10560.923 Da.
| 1 | SER | ALA | GLY | ILE | ALA | THR | PHE | LYS | LEU | VAL | ||||
| 2 | LEU | ASN | GLY | LYS | THR | LEU | LYS | GLY | GLU | THR | ||||
| 3 | THR | THR | GLU | ALA | VAL | ASP | ALA | ALA | THR | ALA | ||||
| 4 | LEU | LYS | ASN | PHE | GLY | ALA | TYR | ALA | GLN | ASP | ||||
| 5 | VAL | GLY | VAL | ASP | GLY | ALA | TRP | THR | TYR | ASP | ||||
| 6 | ASP | ALA | THR | LYS | THR | PHE | THR | VAL | GLY | GLU | ||||
| 7 | ARG | LEU | ILE | PHE | LYS | VAL | LYS | MET | PRO | GLU | ||||
| 8 | ASP | ARG | MET | ASN | ASP | LEU | ALA | ARG | GLN | LEU | ||||
| 9 | ARG | GLN | ARG | ASP | ASN | VAL | SER | ARG | VAL | GLU | ||||
| 10 | VAL | THR | ARG | TYR | LYS |
Samples:
sample_1: Sb1, [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: 283 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation
NMRFAM-SPARKY, NMRFAM - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TopSpin, Bruker Biospin - collection
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