BMRB Entry 26045
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26045
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Title: Solution structure of the de novo mini protein HHH_06 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:
HHH_06, polymer, 44 residues, 5119.8 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):
HHH_06: APCEDLKERLKKLGMSEECR
QRLEKMCKEGTSEDAERMAR
NCES
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 155 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 303 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HHH_06 | 1 |
Entities:
Entity 1, HHH_06 44 residues - 5119.8 Da.
| 1 | ALA | PRO | CYS | GLU | ASP | LEU | LYS | GLU | ARG | LEU | ||||
| 2 | LYS | LYS | LEU | GLY | MET | SER | GLU | GLU | CYS | ARG | ||||
| 3 | GLN | ARG | LEU | GLU | LYS | MET | CYS | LYS | GLU | GLY | ||||
| 4 | THR | SER | GLU | ASP | ALA | GLU | ARG | MET | ALA | ARG | ||||
| 5 | ASN | CYS | GLU | SER |
Samples:
sample_1: sodium phosphate 50 mM; DSS 4 uM; D2O, [U-99% 2H], 10%; sodium azide 0.02%; HHH_06, [U-100% 15N], 1 mM
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-1H DPFGSE TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H DPFGSE NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
Software:
vnmrj, 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
pdbstat, pdbstat (Moseley, Montelione) - data analysis
PSVS, Bhattacharya and Montelione - RPF calculation, validation, violations
NMR spectrometers:
- Agilent DD2 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts