BMRB Entry 51672
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51672
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: GRASP peptide PubMed: 37506293
Deposition date: 2022-10-25 Original release date: 2023-07-03
Authors: Borner, Tito; Tinsley, Ian; Milliken, Brandon; Najjar, Nicholas; Kerwood, Deborah; De Jonghe, Bart; Doyle, Robert; Hayes, Matthew
Citation: Borner, Tito; Tinsley, Ian; Milliken, Brandon; Doebley, Sarah; Najjar, Nicholas; Kerwood, Deborah; De Jonghe, Bart; Hayes, Matthew; Doyle, Robert. "Creation of a Peptide Antagonist of the GFRAL-RET Receptor Complex for the Treatment of GDF15-Induced Malaise" J. Med. Chem. 66, 11237-11249 (2023).
Assembly members:
entity_1, polymer, 29 residues, 3280 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: chemical synthesis
Entity Sequences (FASTA):
entity_1: TKEELIHAHADPMVLIQKTD
TGVSLQTYD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 75 |
| 1H chemical shifts | 175 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PeptideGRASP | 1 |
Entities:
Entity 1, PeptideGRASP 29 residues - 3280 Da.
| 1 | THR | LYS | GLU | GLU | LEU | ILE | HIS | ALA | HIS | ALA | ||||
| 2 | ASP | PRO | MET | VAL | LEU | ILE | GLN | LYS | THR | ASP | ||||
| 3 | THR | GLY | VAL | SER | LEU | GLN | THR | TYR | ASP |
Samples:
sample_1: GRASP peptide 1 mM; DSS 0.5 mM; phosphate-buffered saline 50 mM
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 1D 13C | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v18 - restraint molecular dynamic calculations
TOPSPIN v4.0.3 - collection and analysis of data
NMR spectrometers:
- Bruker AVANCE III 800 MHz