BMRB Entry 50708

Name: N-terminal acetylated FUS LC (1-163)
Published: 2021-02-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50708

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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: N-terminal acetylated FUS LC (1-163) PubMed: 33547841

Deposition date: 2021-01-13 Original release date: 2021-02-22

Authors: Bock, Anna; Murthy, Anastasia; Fawzi, Nicolas

Citation: Bock, Anna; Murthy, Anastasia; Tang, WaiShing; Jovic, Nina; Shewmaker, Frank; Mittal, Jeetain; Fawzi, Nicolas. "N-terminal acetylation modestly enhances phase separation and reduces aggregation of the low-complexity domain of RNA-binding protein fused in sarcoma" Protein Sci. 30, 1337-1349 (2021).

Assembly members:
entity_1, polymer, 163 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: FUS_anion

Entity Sequences (FASTA):
entity_1: XASNDYTQQATQSYGAYPTQ PGQGYSQQSSQPYGQQSYSG YSQSTDTSGYGQSSYSSYGQ SQNTGYGTQSTPQGYGSTGG YGSSQSSQSSYGQQSSYPGY GQQPAPSSTSGSYGSSSQSS SYGQPQSGSYSQQPSYGGQQ QSYGQQQSYNPPQGYGQQNQ YNS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	444
15N chemical shifts	150
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FUS_LC	1

Entities:

Entity 1, FUS_LC 163 residues - Formula weight is not available

1

ACE

ALA

SER

ASN

ASP

TYR

THR

GLN

ALA

2

THR

GLN

SER

TYR

GLY

ALA

TYR

PRO

THR

GLN

3

PRO

GLY

GLN

GLY

TYR

SER

GLN

SER

4

GLN

PRO

TYR

GLY

GLN

SER

TYR

SER

GLY

5

TYR

SER

GLN

SER

THR

ASP

THR

SER

GLY

TYR

6

GLY

GLN

SER

TYR

SER

TYR

GLY

GLN

7

SER

GLN

ASN

THR

GLY

TYR

GLY

THR

GLN

SER

8

THR

PRO

GLN

GLY

TYR

GLY

SER

THR

GLY

9

TYR

GLY

SER

GLN

SER

GLN

SER

10

TYR

GLY

GLN

SER

TYR

PRO

GLY

TYR

11

GLY

GLN

PRO

ALA

PRO

SER

THR

SER

12

GLY

SER

TYR

GLY

SER

GLN

SER

13

SER

TYR

GLY

GLN

PRO

GLN

SER

GLY

SER

TYR

14

SER

GLN

PRO

SER

TYR

GLY

GLN

15

GLN

SER

TYR

GLY

GLN

SER

TYR

ASN

16

PRO

GLN

GLY

TYR

GLY

GLN

ASN

GLN

17

TYR

ASN

SER

Samples:

sample_1: FUS_LC_NtAc, [U-100% 13C; U-100% 15N], 100 uM; D2O, [U-2H], 10%; MES 50 mM; sodium chloride 150 mM; Bis Tris 1 mM

sample_conditions_1: ionic strength: 150 mM; 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - 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