BMRB Entry 50090

Name: G335D TDP43_267-414
Published: 2020-02-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50090

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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:

G335D TDP43_267-414

Deposition date:

2019-11-16

Original release date:

2020-02-21

Authors:

Conicella, Alexander; D'Ordine, Alexandra; Fawzi, Nicolas

Citation:

Citation: Conicella, Alexander; Dignon, Gregory; Zerze, Gul; Schmidt, Hermann Broder; D'Ordine, Alexandra; Kim, Young; Rohatgi, Rajat; Ayala, Yuna; Mittal, Jeetain; Fawzi, Nicolas. "TDP-43 alpha-helical structure tunes liquid-liquid phase separation and function" Proc. Natl. Acad. Sci. U.S.A. 117, 5883-5894 (2020).
PubMed: 32132204

Assembly members:

Assembly members:
entity_1, polymer, 151 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: pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMNRQLERSGRFGGNPGGF GNQGGFGNSRGGGAGLGNNQ GSNMGGGMNFGAFSINPAMM AAAQAALQSSWDMMGMLASQ QNQSGPSGNNQNQGNMQREP NQAFGSGNNSYSGSNSGAAI GWGSASNAGSGSGFNGGFGS SMDSKSSGWGM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	257
15N chemical shifts	142
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	G335D TDP-43_267-414 Monomer	1

Entities:

Entity 1, G335D TDP-43_267-414 Monomer 151 residues - Formula weight is not available

Residues 1-3 comprise the cloning artifact left after removal of the N-terminal affinity tag by cleavage with TEV protease.

1

GLY

HIS

MET

ASN

ARG

GLN

LEU

GLU

ARG

SER

2

GLY

ARG

PHE

GLY

ASN

PRO

GLY

PHE

3

GLY

ASN

GLN

GLY

PHE

GLY

ASN

SER

ARG

4

GLY

ALA

GLY

LEU

GLY

ASN

GLN

5

GLY

SER

ASN

MET

GLY

MET

ASN

PHE

6

GLY

ALA

PHE

SER

ILE

ASN

PRO

ALA

MET

7

ALA

GLN

ALA

LEU

GLN

SER

8

TRP

ASP

MET

GLY

MET

LEU

ALA

SER

GLN

9

GLN

ASN

GLN

SER

GLY

PRO

SER

GLY

ASN

10

GLN

ASN

GLN

GLY

ASN

MET

GLN

ARG

GLU

PRO

11

ASN

GLN

ALA

PHE

GLY

SER

GLY

ASN

SER

12

TYR

SER

GLY

SER

ASN

SER

GLY

ALA

ILE

13

GLY

TRP

GLY

SER

ALA

SER

ASN

ALA

GLY

SER

14

GLY

SER

GLY

PHE

ASN

GLY

PHE

GLY

SER

15

SER

MET

ASP

SER

LYS

SER

GLY

TRP

GLY

16

MET

Samples:

sample_1: entity_1 mM; MES 20 mM

sample_conditions_1: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz

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