BMRB Entry 27072

Name: TDP-43 NTD
Published: 2017-05-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27072

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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:

TDP-43 NTD

Deposition date:

2017-04-13

Original release date:

2017-05-15

Authors:

Afroz, Tariq

Citation:

Citation: Afroz, Tariq; Hock, Eva-Maria; Ernst, Patrick; Foglieni, Chiara; Jambeau, Melanie; Gilhespy, Larissa; Laferriere, Florent; Maniecka, Zuzanna; Pluckthun, Andreas; Mittl, Peer; Paganetti, Paolo; Allain, Frederic; Polymenidou, Magdalini. "Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation" Nat. Commun. 8, 45-45 (2017).
PubMed: 28663553

Assembly members:

Assembly members:
TDP-43_NTD, polymer, 102 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28A(1)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TDP-43_NTD: MGSSHHHHHHSSGLVPRGSH MASSEYIRVTEDENDEPIEI PSEDDGTVLLSTVTAQFPGA CGLRYRNPVSQCMRGVRLVE GILHAPDAGWGNLVYVVNYP KD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	69
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TDP-43 NTD	1

Entities:

Entity 1, TDP-43 NTD 102 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

SER

GLU

TYR

ILE

ARG

VAL

THR

4

GLU

ASP

GLU

ASN

ASP

GLU

PRO

ILE

GLU

ILE

5

PRO

SER

GLU

ASP

GLY

THR

VAL

LEU

6

SER

THR

VAL

THR

ALA

GLN

PHE

PRO

GLY

ALA

7

CYS

GLY

LEU

ARG

TYR

ARG

ASN

PRO

VAL

SER

8

GLN

CYS

MET

ARG

GLY

VAL

ARG

LEU

VAL

GLU

9

GLY

ILE

LEU

HIS

ALA

PRO

ASP

ALA

GLY

TRP

10

GLY

ASN

LEU

VAL

TYR

VAL

ASN

TYR

PRO

11

LYS

ASP

Samples:

sample_1: TDP-43 NTD, [U-100% 15N], 600 uM; TDP-43 NTD, [U-100% 13C; U-100% 15N], 600 uM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC d20	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 700 MHz
Bruker Avance 500 MHz

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