BMRB Entry 50890

Title:
Backbone NMR assignments of the mitochondrial membrane protein MPV17 without cysteine residues
Deposition date:
2021-04-14
Original release date:
2021-06-25
Authors:
Sperl, Laura; Hagn, Franz
Citation:

Citation: Sperl, Laura; Hagn, Franz. "NMR Structural and Biophysical Analysis of the Disease-Linked Inner Mitochondrial Membrane Protein MPV17."  J. Mol. Biol. 433, 167098-167098 (2021).
PubMed: 34116124

Assembly members:

Assembly members:
entity_1, polymer, 176 residues, Formula weight is not available

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: pET15b-GB1

Data sets:
Data typeCount
13C chemical shifts454
15N chemical shifts149
1H chemical shifts149

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MPV171

Entities:

Entity 1, MPV17 176 residues - Formula weight is not available

1   METALALEUTRPARGALATYRGLNARGALA
2   LEUALAALAHISPROTRPLYSVALGLNVAL
3   LEUTHRALAGLYSERLEUMETGLYLEUGLY
4   ASPILEILESERGLNGLNLEUVALGLUARG
5   ARGGLYLEUGLNGLUHISGLNARGGLYARG
6   THRLEUTHRMETVALSERLEUGLYALAGLY
7   PHEVALGLYPROVALVALGLYGLYTRPTYR
8   LYSVALLEUASPARGPHEILEPROGLYTHR
9   THRLYSVALASPALALEULYSLYSMETLEU
10   LEUASPGLNGLYGLYPHEALAPROALAPHE
11   LEUGLYALAPHELEUPROLEUVALGLYALA
12   LEUASNGLYLEUSERALAGLNASPASNTRP
13   ALALYSLEUGLNARGASPTYRPROASPALA
14   LEUILETHRASNTYRTYRLEUTRPPROALA
15   VALGLNLEUALAASNPHETYRLEUVALPRO
16   LEUHISTYRARGLEUALAVALVALGLNALA
17   VALALAVALILETRPASNSERTYRLEUSER
18   TRPLYSALAHISARGLEU

Samples:

sample_1: MPV17 cysfree, [U-13C; U-15N; U-2H], 400 uM; NaPi 20 mM; NaCl 50 mM; EDTA 0.5 mM; DTT 5 mM; DPC 300 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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