BMRB Entry 36060

Name: Solution Structure of the N-terminal Domain of TDP-43
Published: 2017-08-14

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PDB ID: 5x4f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36060
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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:

2017-02-13

Original release date:

2017-08-14

Authors:

Jiang, L.-L., L.; Xue, W.; Hu, H.-Y., H.

Citation:

Citation: Jiang, Lei-Lei; Xue, Wei; Hong, Jun-Ye; Zhang, Jun-Ting; Li, Min-Jun; Yu, Shao-Ning; He, Jian-Hua; Hu, Hong-Yu. "The N-terminal dimerization is required for TDP-43 splicing activity." Sci. Rep. 7, 6196-6196 (2017).
PubMed: 28733604

Assembly members:

Assembly members:
entity_1, polymer, 77 residues, 8502.391 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: MSEYIRVTEDENDEPIEIPS EDDGTVLLSTVTAQFPGASG LRYRNPVSQSMRGVRLVEGI LHAPDAGWGNLVYVVNY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	275
15N chemical shifts	78
1H chemical shifts	467

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 77 residues - 8502.391 Da.

1

MET

SER

GLU

TYR

ILE

ARG

VAL

THR

GLU

ASP

2

GLU

ASN

ASP

GLU

PRO

ILE

GLU

ILE

PRO

SER

3

GLU

ASP

GLY

THR

VAL

LEU

SER

THR

4

VAL

THR

ALA

GLN

PHE

PRO

GLY

ALA

SER

GLY

5

LEU

ARG

TYR

ARG

ASN

PRO

VAL

SER

GLN

SER

6

MET

ARG

GLY

VAL

ARG

LEU

VAL

GLU

GLY

ILE

7

LEU

HIS

ALA

PRO

ASP

ALA

GLY

TRP

GLY

ASN

8

LEU

VAL

TYR

VAL

ASN

TYR

Samples:

sample_1: TDP(1-77)-GB1-C39/C50S, U-99% 13C; U-99% 15N, 1 mM; sodium azide 0.05 v/v; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

Molmol, Koradi, Billeter and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

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