BMRB Entry 16381

Title:
Sequence-specific resonance assignments of human VDAC-1 in LDAO micelles
Deposition date:
2009-06-30
Original release date:
2010-03-01
Authors:
Hiller, Sebastian; Garces, Robert; Malia, Thomas; Orekhov, Vladislav; Wagner, Gerhard
Citation:

Citation: Raschle, Thomas; Hiller, Sebastian; Yu, Tsyr-Yan; Rice, Amanda; Walz, Thomas; Wagner, Gerhard. "Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs."  J. Am. Chem. Soc. 131, 17777-17779 (2009).
PubMed: 19916553

Assembly members:

Assembly members:
VDAC-1, polymer, 291 residues, 31050.059 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   Vector: pET21a

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts239
1H chemical shifts479

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VDAC-11

Entities:

Entity 1, VDAC-1 291 residues - 31050.059 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: VDAC-1, [U-13C; U-15N; U-2H], 1 mM; LDAO 400 mM; NaPi 25 mM; DTT 5 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 25 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB13473 BAE27004 BAE31716 BAE39878 BAE40179
EMBL CAA52962 CAB58127
GB AAA61272 AAB20246 AAB47777 AAD54939 AAF22835
REF NP_001075544 NP_001119824 NP_001248683 NP_001270163 NP_003365
SP P21796 P45879 Q60932 Q9MZ16 Q9TT15
TPG DAA27459
AlphaFold P21796 P45879 Q60932 Q9MZ16 Q9TT15

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