BMRB Entry 27543

Name: Backbone assignment of mouse MARCH9 transmembrane domains in LMPG micelles
Published: 2018-12-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27543

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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:

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):

Entity Sequences (FASTA):
MARCH9-TM: IEKVQIAAIVLGSLFLVASI SWLIWSSLSPSAKWQRQDLL FQISYGVYGFVDVVSIGLIV HEGSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	63
1H chemical shifts	63

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MARCH9-TM	1

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

ILE

GLU

LYS

VAL

GLN

ILE

ALA

ILE

VAL

2

LEU

GLY

SER

LEU

PHE

LEU

VAL

ALA

SER

ILE

3

SER

TRP

LEU

ILE

TRP

SER

LEU

SER

PRO

4

SER

ALA

LYS

TRP

GLN

ARG

GLN

ASP

LEU

5

PHE

GLN

ILE

SER

TYR

GLY

VAL

TYR

GLY

PHE

6

VAL

ASP

VAL

SER

ILE

GLY

LEU

ILE

VAL

7

HIS

GLU

GLY

SER

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_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