BMRB Entry 30067
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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/BMR30067
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Title: Solution structure of the de novo miniprotein EHE_06 PubMed: 27626386
Deposition date: 2016-04-21 Original release date: 2016-09-22
Authors: Buchko, G.; Gilmore, J.; Bahl, C.
Citation: Bhardwaj, G.; Mulligan, V.; Bahl, C.; Gilmore, J.; Harvey, P.; Cheneval, O.; Buchko, G.; Pulavarti, S.; Kaas, Q.; Eletsky, A.; Huang, P.; Johnsen, W.; Greisen, P.; Rocklin, G.; Song, Y.; Linsky, T.; Watkins, A.; Rettie, S.; Xu, X.; Carter, L.; Bonneau, R.; Olson, J.; Coutsias, E.; Correnti, C.; Szyperski, T.; Craik, D.; Baker, D.. "Accurate de novo design of hyperstable constrained peptides." Nature 538, 329-335 (2016).
Assembly members:
W35, polymer, 35 residues, 4278.767 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
W35: CKQRRRYRGSEEECRKYAEE
LSRRTGCEVEVECET
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 76 |
| 15N chemical shifts | 41 |
| 1H chemical shifts | 218 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 35 residues - 4278.767 Da.
| 1 | CYS | LYS | GLN | ARG | ARG | ARG | TYR | ARG | GLY | SER | ||||
| 2 | GLU | GLU | GLU | CYS | ARG | LYS | TYR | ALA | GLU | GLU | ||||
| 3 | LEU | SER | ARG | ARG | THR | GLY | CYS | GLU | VAL | GLU | ||||
| 4 | VAL | GLU | CYS | GLU | THR |
Samples:
sample_1: W35, [U-99% 15N], 1 ± 0.2 mM; sodium acetate 25 ± 1 mM; sodium chloride 50 ± 2 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 75 mM; pH: 4.8; pressure: 1 atm; temperature: 293 K
sample_conditions_2: ionic strength: 75 mM; pH: 4.8 pD; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| Deuterium Exchange | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
Felix v2007, Accelrys Software Inc. - processing
SPARKY, Goddard - peak picking
SPARKY v3.115, Goddard - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts