BMRB Entry 25597
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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/BMR25597
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Title: Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor PubMed: 26372966
Deposition date: 2015-05-06 Original release date: 2015-09-10
Authors: O'Connor, Casey; White, Kate; Doncescu, Nathalie; Didenko, Tatiana; Roth, Bryan; Czaplicki, Georges; Stevens, Raymond; Wuthrich, Kurt; Milon, Alain
Citation: O'Connor, Casey; White, Kate; Doncescu, Nathalie; Didenko, Tatiana; Roth, Bryan; Czaplicki, Georges; Stevens, Raymond; Wuthrich, Kurt; Milon, Alain. "NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor" Proc. Natl. Acad. Sci. U.S.A. 112, 11852-11857 (2015).
Assembly members:
Dynorphin_1-13, polymer, 13 residues, 1609.012 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
Dynorphin_1-13: YGGFLRRIRPKLK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 18 |
15N chemical shifts | 18 |
1H chemical shifts | 125 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entities:
Entity 1, entity 13 residues - 1609.012 Da.
1 | TYR | GLY | GLY | PHE | LEU | ARG | ARG | ILE | ARG | PRO | ||||
2 | LYS | LEU | LYS |
Samples:
sample_1: Dynorphin 1-13, [U-15N-GFLI], 1 mM; potassium chloride 150 mM; MES, [U-2H], 40 mM; DSS 100 uM; KOR 10 uM; DDM 8 mM; CHS 1.6 mM; H2O 90%; D2O 10%
sample_2: Dynorphin 1-13, [U-15N-GFLIR; U-13C-R], 1 mM; potassium chloride 150 mM; MES, [U-2H], 40 mM; DSS 100 uM; KOR 10 uM; DDM 8 mM; CHS 1.6 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.1; pressure: 1 atm; temperature: 280 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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D HNCACB | sample_2 | isotropic | sample_conditions_1 |
15N T1 T2 hetNOE | sample_1 | isotropic | sample_conditions_1 |
15N T2 | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2, Bruker Biospin - chemical shift assignment, peak picking, processing
AMBER v14, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - geometry optimization, structure solution
NMR spectrometers:
- Bruker Avance III 800 MHz
- Bruker Avance 800 MHz
- Bruker Avance III 700 MHz
- Bruker Avance III 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts