BMRB Entry 50891

Name: NMR backbone chemical shift assignments of the mitochondrial membrane protein MPV17 labeled with MMTS in DPC micelles
Published: 2021-06-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50891

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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:

NMR backbone chemical shift assignments of the mitochondrial membrane protein MPV17 labeled with MMTS in DPC micelles

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MALWRAYQRALAAHPWKVQV LTAGSLMGLGDIISQQLVER RGLQEHQRGRTLTMVSLGCG FVGPVVGGWYKVLDRFIPGT TKVDALKKMLLDQGGFAPCF LGCFLPLVGALNGLSAQDNW AKLQRDYPDALITNYYLWPA VQLANFYLVPLHYRLAVVQC VAVIWNSYLSWKAHRL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	338
15N chemical shifts	128
1H chemical shifts	127

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MPV17wt-met	1

Entities:

Entity 1, MPV17wt-met 176 residues - Formula weight is not available

1

MET

ALA

LEU

TRP

ARG

ALA

TYR

GLN

ARG

ALA

2

LEU

ALA

HIS

PRO

TRP

LYS

VAL

GLN

VAL

3

LEU

THR

ALA

GLY

SER

LEU

MET

GLY

LEU

GLY

4

ASP

ILE

SER

GLN

LEU

VAL

GLU

ARG

5

ARG

GLY

LEU

GLN

GLU

HIS

GLN

ARG

GLY

ARG

6

THR

LEU

THR

MET

VAL

SER

LEU

GLY

CYS

GLY

7

PHE

VAL

GLY

PRO

VAL

GLY

TRP

TYR

8

LYS

VAL

LEU

ASP

ARG

PHE

ILE

PRO

GLY

THR

9

THR

LYS

VAL

ASP

ALA

LEU

LYS

MET

LEU

10

LEU

ASP

GLN

GLY

PHE

ALA

PRO

CYS

PHE

11

LEU

GLY

CYS

PHE

LEU

PRO

LEU

VAL

GLY

ALA

12

LEU

ASN

GLY

LEU

SER

ALA

GLN

ASP

ASN

TRP

13

ALA

LYS

LEU

GLN

ARG

ASP

TYR

PRO

ASP

ALA

14

LEU

ILE

THR

ASN

TYR

LEU

TRP

PRO

ALA

15

VAL

GLN

LEU

ALA

ASN

PHE

TYR

LEU

VAL

PRO

16

LEU

HIS

TYR

ARG

LEU

ALA

VAL

GLN

CYS

17

VAL

ALA

VAL

ILE

TRP

ASN

SER

TYR

LEU

SER

18

TRP

LYS

ALA

HIS

ARG

LEU

Samples:

sample_1: MPV17wt-MMTS, [U-13C; U-15N; U-2H], 430 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:

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

Software:

TOPSPIN - collection, 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