BMRB Entry 34309

Name: Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles
Published: 2018-09-06

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PDB ID: 6hh0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34309
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles

Deposition date:

2018-08-24

Original release date:

2018-09-06

Authors:

Zangger, K.; Hohlweg, W.; Wagner, G.

Citation:

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).
PubMed: 30209131

Assembly members:

Assembly members:
entity_1, polymer, 25 residues, 2832.328 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: synthetic construct

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKSHTASYLRLWALSLAHAQ LSSKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	4
15N chemical shifts	2
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 25 residues - 2832.328 Da.

1

LYS

SER

HIS

THR

ALA

SER

TYR

LEU

ARG

2

LEU

TRP

ALA

LEU

SER

LEU

ALA

HIS

ALA

GLN

3

LEU

SER

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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks