BMRB Entry 34309
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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/BMR34309
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Title: Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles PubMed: 30209131
Deposition date: 2018-08-24 Original release date: 2018-09-06
Authors: Zangger, K.; Hohlweg, W.; Wagner, G.
Citation: Hohlweg, W.; Wagner-Lichtenegger, G.; Hofbauer, H.; Sarkleti, F.; Setz, M.; Gubensak, N.; Lichtenegger, S.; Falsone, F.; Wolinski, H.; Kosol, S.; Oostenrbink, C.; Kohlwein, S.; Zangger, K.. "A cation-Pi interaction in a transmembrane helix of vacuolar ATPase keeps the proton transporting arginine in a hydrophobic environment" J. Biol. Chem. 293, 18977-18988 (2018).
Assembly members:
entity_1, polymer, 25 residues, 2832.328 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: synthetic construct
Entity Sequences (FASTA):
entity_1: KKSHTASYLRLWALSLAHAQ
LSSKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 4 |
| 15N chemical shifts | 2 |
| 1H chemical shifts | 158 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 25 residues - 2832.328 Da.
| 1 | LYS | LYS | SER | HIS | THR | ALA | SER | TYR | LEU | ARG | ||||
| 2 | LEU | TRP | ALA | LEU | SER | LEU | ALA | HIS | ALA | GLN | ||||
| 3 | LEU | SER | SER | LYS | LYS |
Samples:
sample_1: Deuterated DPC, [U-99% 2H], 100 mM; potassium phosphate, none, 50 mM; sodium azide, none, 0.02%; TM7 peptide, 13C and 15N labeled aminoacids 8 and 12, 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-N-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY C-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
NMR spectrometers:
- Bruker AvanceIII 700 MHz
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts