BMRB Entry 27125

Name: FUS low complexity domain with 12 phosphomimetic S/T to E mutations
Published: 2017-08-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27125

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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:

FUS low complexity domain with 12 phosphomimetic S/T to E mutations

Deposition date:

2017-06-05

Original release date:

2017-08-02

Authors:

Ryan, Veronica; Fawzi, Nicolas; Burke, Kathleen

Citation:

Citation: Monahan, Zachary; Ryan, Veronica; Janke, Abigail; Burke, Kathleen; Rhoads, Shannon; Zerze, Gul; O'Meally, Robert; Dignon, Gregory; Conicella, Alexander; Zheng, Wenwei; Best, Robert; Cole, Robert; Mittal, Jeetain; Shewmaker, Frank; Fawzi, Nicolas. "Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity" EMBO J. 36, 2951-2967 (2017).
PubMed: 28790177

Assembly members:

Assembly members:
FUS_12E_LC, polymer, 164 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: MBP-FUS_LC_12E_pTHMT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FUS_12E_LC: GMASNDYEQQAEQSYGAYPE QPGQGYEQQSEQPYGQQSYS GYEQSTDTSGYGQSSYSSYG QEQNTGYGEQSTPQGYGSTG GYGSEQSEQSSYGQQSSYPG YGQQPAPSSTSGSYGSSEQS SSYGQPQSGSYEQQPSYGGQ QQSYGQQQSYNPPQGYGQQN QYNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	423
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FUS 12E LC	1

Entities:

Entity 1, FUS 12E LC 164 residues - Formula weight is not available

Residue 1 is cleavage artifact, reside 2 is residue 1 in FUS

1

GLY

MET

ALA

SER

ASN

ASP

TYR

GLU

GLN

2

ALA

GLU

GLN

SER

TYR

GLY

ALA

TYR

PRO

GLU

3

GLN

PRO

GLY

GLN

GLY

TYR

GLU

GLN

SER

4

GLU

GLN

PRO

TYR

GLY

GLN

SER

TYR

SER

5

GLY

TYR

GLU

GLN

SER

THR

ASP

THR

SER

GLY

6

TYR

GLY

GLN

SER

TYR

SER

TYR

GLY

7

GLN

GLU

GLN

ASN

THR

GLY

TYR

GLY

GLU

GLN

8

SER

THR

PRO

GLN

GLY

TYR

GLY

SER

THR

GLY

9

GLY

TYR

GLY

SER

GLU

GLN

SER

GLU

GLN

SER

10

SER

TYR

GLY

GLN

SER

TYR

PRO

GLY

11

TYR

GLY

GLN

PRO

ALA

PRO

SER

THR

12

SER

GLY

SER

TYR

GLY

SER

GLU

GLN

SER

13

SER

TYR

GLY

GLN

PRO

GLN

SER

GLY

SER

14

TYR

GLU

GLN

PRO

SER

TYR

GLY

GLN

15

GLN

SER

TYR

GLY

GLN

SER

TYR

16

ASN

PRO

GLN

GLY

TYR

GLY

GLN

ASN

17

GLN

TYR

ASN

SER

Samples:

sample_1: FUS 12E LC, [U-99% 13C; U-99% 15N], 100 uM; D2O, [U-2H], 10%; MES 50 mM; Bis Tris 1 mM; H2O 90%

sample_conditions_1: ionic strength: 0 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CAN)NH	sample_1	isotropic	sample_conditions_1

Software:

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

CARA, Wuthrich - 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