BMRB Entry 27543

Title:
Backbone assignment of mouse MARCH9 transmembrane domains in LMPG micelles
Deposition date:
2018-07-13
Original release date:
2018-12-12
Authors:
Tan, Cyrus; Byrne, Eamon; Call, Melissa; Call, Matthew
Citation:

Citation: Tan, Cyrus; Byrne, Eamon; Ah-Cann, Casey; Call, Melissa; Call, Matthew. "A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates"  J. Biol. Chem. 294, 2470-2485 (2019).
PubMed: 30554144

Assembly members:

Assembly members:
MARCH9-TM, polymer, 65 residues, 7123 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts63
1H chemical shifts63

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MARCH9-TM1

Entities:

Entity 1, MARCH9-TM 65 residues - 7123 Da.

This 65-residue peptide encompasses the two TM domains of mouse MARCH9 with intervening extracellular loop sequence.

1   ILEGLULYSVALGLNILEALAALAILEVAL
2   LEUGLYSERLEUPHELEUVALALASERILE
3   SERTRPLEUILETRPSERSERLEUSERPRO
4   SERALALYSTRPGLNARGGLNASPLEULEU
5   PHEGLNILESERTYRGLYVALTYRGLYPHE
6   VALASPVALVALSERILEGLYLEUILEVAL
7   HISGLUGLYSERSER

Samples:

sample_1: LMPG 250 mM; sodium phosphate 20 mM; D2O, [U-99% 2H], 5%; MARCH9-TM, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

XEASY, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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