BMRB Entry 34295
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34295
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Title: Stabilising and Understanding a Miniprotein by Rational Design. PubMed: 31251570
Deposition date: 2018-06-26 Original release date: 2019-07-02
Authors: Porter Goff, K.; Williams, C.; Baker, E.; Nicol, D.; Samphire, J.; Zieleniewski, F.; Crump, M.; Woolfson, D.
Citation: Porter Goff, K.; Nicol, D.; Williams, C.; Crump, M.; Zieleniewski, F.; Samphire, J.; Baker, E.; Woolfson, D.. "Stabilizing and Understanding a Miniprotein by Rational Redesign." Biochemistry 58, 3060-3064 (2019).
Assembly members:
entity_1, polymer, 36 residues, 3791.348 Da.
Natural source: Common Name: Streptococcus mutans Taxonomy ID: 1309 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus mutans
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: XPPKKPKKPGDNATPEKLAA
YEKELAAYEKELAAYX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 35 |
| 15N chemical shifts | 30 |
| 1H chemical shifts | 241 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 36 residues - 3791.348 Da.
| 1 | ACE | PRO | PRO | LYS | LYS | PRO | LYS | LYS | PRO | GLY | ||||
| 2 | ASP | ASN | ALA | THR | PRO | GLU | LYS | LEU | ALA | ALA | ||||
| 3 | TYR | GLU | LYS | GLU | LEU | ALA | ALA | TYR | GLU | LYS | ||||
| 4 | GLU | LEU | ALA | ALA | TYR | NH2 |
Samples:
sample_1: Optimised PPa-TYR 1 ± 0.1 mM; Na2HPO4 8.2 ± 0.1 mM; KH2PO4 1.8 ± 0.1 mM; KCL 2.7 ± 0.1 mM; NaCl 137 ± 0.1 mM; D2O, [U-99% 2H], 10 ± 0.1 %
sample_conditions_1: ionic strength: 0.1698 M; pH: 7.4; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 100ms NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 100ms NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H 250ms NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H 250ms NOESY | sample_1 | isotropic | sample_conditions_1 |
| 1H-13N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure calculation
CcpNmr Analysis v2.4.1, CCPN - chemical shift assignment, peak picking
TopSpin v3.5, Bruker Biospin - collection
VNMR v4, Varian - collection
NMRDraw v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AvanceIII 700 MHz
- Varian VNMRS 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts