BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34309

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

Data sets:
Data typeCount
13C chemical shifts4
15N chemical shifts2
1H chemical shifts158

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 25 residues - 2832.328 Da.

1   LYSLYSSERHISTHRALASERTYRLEUARG
2   LEUTRPALALEUSERLEUALAHISALAGLN
3   LEUSERSERLYSLYS

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:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
2D TOCSYsample_1isotropicsample_conditions_1
3D NOESY-N-HSQCsample_1isotropicsample_conditions_1
2D HSQCsample_1isotropicsample_conditions_1
3D NOESY C-HSQCsample_1isotropicsample_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:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts