BMRB Entry 34081

Name: Solution structure of TDP-43 (residues 1-102)
Published: 2017-06-02

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PDB ID: 5mrg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34081
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3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of TDP-43 (residues 1-102)

Deposition date:

2016-12-22

Original release date:

2017-06-02

Authors:

Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Laurents, D.

Citation:

Citation: Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Buratti, E.; Laurents, D.. "Point mutations in transactive response DNA-binding protein 43 (TDP-43)'s N-terminal domain compromise its stability, dimerization and functions" J. Biol. Chem. 292, 11992-12006 (2017).
PubMed: 28566288

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, 12674.207 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAGSHHHHHHGSMSEYIRVT EDENDEPIEIPSEDDGTVLL STVTAQFPGACGLRYRNPVS QCMRGVRLVEGILHAPDAGW GNLVYVVNYPKDNKRKMDET DASSAVKVKRAVQK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	1
1H chemical shifts	584

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 114 residues - 12674.207 Da.

1

MET

ALA

GLY

SER

HIS

2

GLY

SER

MET

SER

GLU

TYR

ILE

ARG

VAL

THR

3

GLU

ASP

GLU

ASN

ASP

GLU

PRO

ILE

GLU

ILE

4

PRO

SER

GLU

ASP

GLY

THR

VAL

LEU

5

SER

THR

VAL

THR

ALA

GLN

PHE

PRO

GLY

ALA

6

CYS

GLY

LEU

ARG

TYR

ARG

ASN

PRO

VAL

SER

7

GLN

CYS

MET

ARG

GLY

VAL

ARG

LEU

VAL

GLU

8

GLY

ILE

LEU

HIS

ALA

PRO

ASP

ALA

GLY

TRP

9

GLY

ASN

LEU

VAL

TYR

VAL

ASN

TYR

PRO

10

LYS

ASP

ASN

LYS

ARG

LYS

MET

ASP

GLU

THR

11

ASP

ALA

SER

ALA

VAL

LYS

VAL

LYS

ARG

12

ALA

VAL

GLN

LYS

Samples:

sample_1: TDP-43(1-102), [U-13C; U-15N], 0.35 mM

sample_conditions_1: pH: 3.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AvanceII 800 MHz

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