BMRB Entry 51592
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51592
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Title: Synthetic peptide P1-5 PubMed: 36400768
Deposition date: 2022-08-22 Original release date: 2022-11-04
Authors: Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier
Citation: Escobedo, Albert; Piccirillo, Jonathan; Aranda, Juan; Diercks, Tammo; Mateos, Borja; Garcia-Cabau, Carla; Sanchez-Navarro, Macarena; Topal, Busra; Biesaga, Mateusz; Staby, Lasse; Kragelund, Birthe; Garcia, Jesus; Millet, Oscar; Orozco, Modesto; Coles, Murray; Crehuet, Ramon; Salvatella, Xavier. "A glutamine-based single alpha-helix scaffold to target globular proteins" Nat. Commun. 13, 7073-7073 (2022).
Assembly members:
entity_1, polymer, 19 residues, Formula weight is not available
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: chemical synthesis
Entity Sequences (FASTA):
entity_1: KKPGASLLAAQQAAAAKKY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 15 |
15N chemical shifts | 16 |
1H chemical shifts | 89 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | P1-5 | 1 |
Entities:
Entity 1, P1-5 19 residues - Formula weight is not available
1 | LYS | LYS | PRO | GLY | ALA | SER | LEU | LEU | ALA | ALA | ||||
2 | GLN | GLN | ALA | ALA | ALA | ALA | LYS | LYS | TYR |
Samples:
sample_1: P1-5 100 uM; DSS 10 uM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7.4; pressure: 1 atm; temperature: 278 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
TOPSPIN - collection, processing
NMRPipe - processing
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts