BMRB Entry 34457

Title:
Refined solution NMR structure of hVDAC-1 in detergent micelles
Deposition date:
2019-11-22
Original release date:
2019-12-02
Authors:
Boehm, R.; Hiller, S.; Wagner, G.
Citation:

Citation: Boehm, R.; Hiller, S.; Amodeo, G.; Murlidaran, S.; Chavali, S.; Wagner, G.; Brannigan, G.; Winterhalter, M.. "The Structural Basis for Low Conductance in the Membrane Protein VDAC upon beta-NADH Binding and Voltage Gating"  Structure 28, 206-214 (2020).
PubMed: 31862297

Assembly members:

Assembly members:
entity_1, polymer, 291 residues, 31878.662 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts739
15N chemical shifts255
1H chemical shifts510

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 291 residues - 31878.662 Da.

1   METALAVALPROPROTHRTYRALAASPLEU
2   GLYLYSSERALAARGASPVALPHETHRLYS
3   GLYTYRGLYPHEGLYLEUILELYSLEUASP
4   LEULYSTHRLYSSERGLUASNGLYLEUGLU
5   PHETHRSERSERGLYSERALAASNTHRGLU
6   THRTHRLYSVALTHRGLYSERLEUGLUTHR
7   LYSTYRARGTRPTHRGLUTYRGLYLEUTHR
8   PHETHRGLULYSTRPASNTHRASPASNTHR
9   LEUGLYTHRGLUILETHRVALGLUASPGLN
10   LEUALAARGGLYLEULYSLEUTHRPHEASP
11   SERSERPHESERPROASNTHRGLYLYSLYS
12   ASNALALYSILELYSTHRGLYTYRLYSARG
13   GLUHISILEASNLEUGLYCYSASPMETASP
14   PHEASPILEALAGLYPROSERILEARGGLY
15   ALALEUVALLEUGLYTYRGLUGLYTRPLEU
16   ALAGLYTYRGLNMETASNPHEGLUTHRALA
17   LYSSERARGVALTHRGLNSERASNPHEALA
18   VALGLYTYRLYSTHRASPGLUPHEGLNLEU
19   HISTHRASNVALASNASPGLYTHRGLUPHE
20   GLYGLYSERILETYRGLNLYSVALASNLYS
21   LYSLEUGLUTHRALAVALASNLEUALATRP
22   THRALAGLYASNSERASNTHRARGPHEGLY
23   ILEALAALALYSTYRGLNILEASPPROASP
24   ALACYSPHESERALALYSVALASNASNSER
25   SERLEUILEGLYLEUGLYTYRTHRGLNTHR
26   LEULYSPROGLYILELYSLEUTHRLEUSER
27   ALALEULEUASPGLYLYSASNVALASNALA
28   GLYGLYHISLYSLEUGLYLEUGLYLEUGLU
29   PHEGLNALALEUGLUHISHISHISHISHIS
30   HIS

Samples:

sample_1: hVDAC-1, [U-99%-2H; U-13C; U-15N], 0.6 mM; LDAO, no, 3%

sample_2: hVDAC-1, [U-99%-2H, 13C, 15N; 99%-1H delta-IL; 99%-1H gamma-V], 0.6 mM; LDAO, [U-99% 2H], 3%

sample_3: hVDAC-1, [U-99%-2H, 15N; 99%-1H delta, 13C delta-IL; 99%-1H gamma, 13C gamma-V], 0.6 mM; LDAO, [U-99% 2H], 3%

sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
4D NUS-MDD-1H-13C-13Csample_2isotropicsample_conditions_1
4D NUS-MDD-1H-15N-13Csample_3isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Bruker AVANCE 900 MHz

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