BMRB Entry 50189

Name: hnRNPF prion-like domain 365-415 backbone and Cbeta chemical shifts
Published: 2020-12-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50189

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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: hnRNPF prion-like domain 365-415 backbone and Cbeta chemical shifts PubMed: 33349959

Deposition date: 2020-02-03 Original release date: 2020-12-07

Authors: Ryan, Veronica; Fawzi, Nicolas

Citation: Ryan, Veronica; Perdikari, Theodora; Naik, Mandar; Saueressig, Camillo; Lins, Jeremy; Dignon, Gregory; Mittal, Jeetain; Hart, Anne; Fawzi, Nicolas. "Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration" EMBO J. 40, e105001-e105001 (2021).

Assembly members:
hnRNPF PLD disordered monomer, polymer, 51 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJ411

Entity Sequences (FASTA):
hnRNPF PLD disordered monomer: TGASNGAYSSQVMQGMGVSA AQATYSGLESQSVSGCYGAG YSGQNSMGGYD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	142
15N chemical shifts	51
1H chemical shifts	51

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hnRNPF PLD	1

Entities:

Entity 1, hnRNPF PLD 51 residues - Formula weight is not available

1

THR

GLY

ALA

SER

ASN

GLY

ALA

TYR

SER

2

GLN

VAL

MET

GLN

GLY

MET

GLY

VAL

SER

ALA

3

ALA

GLN

ALA

THR

TYR

SER

GLY

LEU

GLU

SER

4

GLN

SER

VAL

SER

GLY

CYS

TYR

GLY

ALA

GLY

5

TYR

SER

GLY

GLN

ASN

SER

MET

GLY

TYR

6

ASP

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 150 uM; D2O, [U-2H], 10%; MES 20 mM; Bis-Tris 1 mM; H2O 90%; DTT 1 mM

sample_conditions_1: ionic strength: 1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	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:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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 shifts
SPARKY: Backbone or all simulated shifts