BMRB Entry 25675

Name: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF TDP-43
Published: 2016-01-11

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PDB ID: 2n4p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25675
MolProbity Validation Chart

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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:

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF TDP-43

Deposition date:

2015-06-26

Original release date:

2016-01-11

Authors:

Mompean, Miguel; Romano, Valentina; Pantoja-Uceda, David; Stuani, Cristiana; Baralle, Francisco; Buratti, Emanuele; Laurents, Douglas

Citation:

Citation: Mompean, Miguel; Romano, Valentina; Pantoja-Uceda, David; Stuani, Cristiana; Baralle, Francisco; Buratti, Emanuele; Laurents, Douglas. "The TDP-43 N-terminal domain structure at high resolution" FEBS J. 283, 1242-1260 (2016).
PubMed: 26756435

Assembly members:

Assembly members:
entity, polymer, 89 residues, 9854.009 Da.

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: pQE30-6xHis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAGSHHHHHHGSMSEYIRVT EDENDEPIEIPSEDDGTVLL STVTAQFPGACGLRYRNPVS QCMRGVRLVEGILHAPDAGW GNLVYVVNY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	351
15N chemical shifts	93
1H chemical shifts	569

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 89 residues - 9854.009 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

Samples:

sample_1: NTD, [U-13C; U-15N], 0.6 mM; TCEP mM; CD3COOD/CD3COO-Na+ mM; NaN3 mM; H20 90%; D20 10%

sample_conditions_1: pH: 3.8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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