BMRB Entry 26046
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26046
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Title: Solution structure of the de novo mini protein EEH_04 PubMed: 27626386
Deposition date: 2016-04-22 Original release date: 2016-09-13
Authors: Eletsky, Alexander; Bahl, Christopher; Gilmore, Jason; Buchko, Garry; Baker, David
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:
entity, polymer, 38 residues, 4527.0 Da.
Natural source: Common Name: not available Taxonomy ID: not available 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):
entity: QCYTFRSECTNKEFTVCRPN
PEEVEKEARRTKEEECRK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 109 |
| 15N chemical shifts | 43 |
| 1H chemical shifts | 247 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EEH_04 | 1 |
Entities:
Entity 1, EEH_04 38 residues - 4527.0 Da.
| 1 | GLN | CYS | TYR | THR | PHE | ARG | SER | GLU | CYS | THR | ||||
| 2 | ASN | LYS | GLU | PHE | THR | VAL | CYS | ARG | PRO | ASN | ||||
| 3 | PRO | GLU | GLU | VAL | GLU | LYS | GLU | ALA | ARG | ARG | ||||
| 4 | THR | LYS | GLU | GLU | GLU | CYS | ARG | LYS |
Samples:
sample_1: EEH_04, [U-10% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; DSS 4 uM; D2O, [U-99% 2H], 10%; sodium azide 0.02%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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-13C HSQC aliphatic ct | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic ct | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H DPFGSE TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H DPFGSE NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR, Varian - collection
PROSA, Guntert - processing
XEASY, Bartels et al. - data analysis
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS, Cornilescu, Delaglio and Bax - dihedral angle prediction
PSVS, Bhattacharya and Montelione - RPF calculation, assignment validation, violations
NMR spectrometers:
- Agilent DD2 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts