BMRB Entry 34032
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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/BMR34032
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Title: Engineering protein stability with atomic precision in a monomeric miniprotein PubMed: 28530710
Deposition date: 2016-08-08 Original release date: 2017-05-12
Authors: Baker, E.; Hudson, K.; Williams, C.; Bartlett, G.; Heal, J.; Sessions, R.; Crump, M.; Woolfson, D.
Citation: Baker, E.; Williams, C.; Hudson, K.; Bartlett, G.; Heal, J.; Porter Goff, K.; Sessions, R.; Crump, M.; Woolfson, D.. "Engineering protein stability with atomic precision in a monomeric miniprotein" Nat. Chem. Biol. 13, 764-770 (2017).
Assembly members:
entity_1, polymer, 36 residues, 3849.365 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: XPPTKPTKPGDNATPEKLAK
XQADLAKXQKDLADXX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 39 |
| 15N chemical shifts | 32 |
| 1H chemical shifts | 227 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 36 residues - 3849.365 Da.
| 1 | ACE | PRO | PRO | THR | LYS | PRO | THR | LYS | PRO | GLY | ||||
| 2 | ASP | ASN | ALA | THR | PRO | GLU | LYS | LEU | ALA | LYS | ||||
| 3 | 0A1 | GLN | ALA | ASP | LEU | ALA | LYS | 0A1 | GLN | LYS | ||||
| 4 | ASP | LEU | ALA | ASP | 0A1 | NH2 |
Samples:
sample_1: KH2PO4 1.8 mM; Na2HPO4 8.2 mM; NaCl 137 mM; NaOH 13.7 mM; PPalpha_OMe 1 mM
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 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - refinement
Analysis, CCPN - chemical shift assignment, peak picking
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AvanceIII 700 MHz
- Bruker AvanceIII 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts