BMRB Entry 30145
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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/BMR30145
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Title: NMR Solution Structure of Designed Peptide NC_cHHH_D1 PubMed: 27626386
Deposition date: 2016-07-19 Original release date: 2016-09-16
Authors: Harvey, P.; Craik, D.
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_1, polymer, 22 residues, 2563.837 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: chemical synthesis
Entity Sequences (FASTA):
entity_1: NPEDCRQDPEANKSPEECKK
LK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 60 |
| 15N chemical shifts | 22 |
| 1H chemical shifts | 142 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 22 residues - 2563.837 Da.
| 1 | ASN | PRO | GLU | ASP | CYS | ARG | GLN | ASP | PRO | GLU | ||||
| 2 | ALA | ASN | LYS | SER | PRO | GLU | GLU | CYS | LYS | LYS | ||||
| 3 | LEU | LYS |
Samples:
sample_1: design peptide NC_cHHH_D1 1.0 mg/mL
sample_2: design peptide NC_cHHH_D1 1.0 mg/mL
sample_conditions_1: pH: 3.0; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D ECOSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CcpNMR, CCPN - chemical shift assignment
TOPSPIN v2.1, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts