BMRB Entry 50026

Name: 2H,15N,13C-labeled FUS-LC fibrils
Published: 2020-09-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50026

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: 2H,15N,13C-labeled FUS-LC fibrils PubMed: 31895552

Deposition date: 2019-10-01 Original release date: 2020-09-21

Authors: Murray, Dylan; Tycko, Robert

Citation: Murray, Dylan; Tycko, Robert. "Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy" Biochemistry 59, 364-378 (2020).

Assembly members:
entity_1, polymer, 243 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: pHis

Entity Sequences (FASTA):
entity_1: MSYYHHHHHHDYDIPTTENL YFQGAMDPASNDYTQQATQS YGAYPTQPGQGYSQQSSQPY GQQSYSGYSQSTDTSGYGQS SYSSYGQSTSQNTGYGTQST PQGYGSTGGYGSSQSSQSSY GQQSSYPGYGQQPAPSSTSG SYGSSSQSSSYGQPQSGSYS QQPSYGGQQQSYGQQQSYNP PQGYGQQNQYNSSSGGGGGG GGGGNYGQDQSSMSSGGGSG GGYGNQDQSGGGGSGGYGQQ DRG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	53
1H chemical shifts	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FUS-LC fibril	1

Entities:

Entity 1, FUS-LC fibril 243 residues - Formula weight is not available

1

MET

SER

TYR

HIS

2

ASP

TYR

ASP

ILE

PRO

THR

GLU

ASN

LEU

3

TYR

PHE

GLN

GLY

ALA

MET

ASP

PRO

ALA

SER

4

ASN

ASP

TYR

THR

GLN

ALA

THR

GLN

SER

5

TYR

GLY

ALA

TYR

PRO

THR

GLN

PRO

GLY

GLN

6

GLY

TYR

SER

GLN

SER

GLN

PRO

TYR

7

GLY

GLN

SER

TYR

SER

GLY

TYR

SER

GLN

8

SER

THR

ASP

THR

SER

GLY

TYR

GLY

GLN

SER

9

SER

TYR

SER

TYR

GLY

GLN

SER

THR

SER

10

GLN

ASN

THR

GLY

TYR

GLY

THR

GLN

SER

THR

11

PRO

GLN

GLY

TYR

GLY

SER

THR

GLY

TYR

12

GLY

SER

GLN

SER

GLN

SER

TYR

13

GLY

GLN

SER

TYR

PRO

GLY

TYR

GLY

14

GLN

PRO

ALA

PRO

SER

THR

SER

GLY

15

SER

TYR

GLY

SER

GLN

SER

16

TYR

GLY

GLN

PRO

GLN

SER

GLY

SER

TYR

SER

17

GLN

PRO

SER

TYR

GLY

GLN

18

SER

TYR

GLY

GLN

SER

TYR

ASN

PRO

19

PRO

GLN

GLY

TYR

GLY

GLN

ASN

GLN

TYR

20

ASN

SER

GLY

21

GLY

ASN

TYR

GLY

GLN

ASP

GLN

22

SER

MET

SER

GLY

SER

GLY

23

GLY

TYR

GLY

ASN

GLN

ASP

GLN

SER

GLY

24

GLY

SER

GLY

TYR

GLY

GLN

25

ASP

ARG

GLY

Samples:

sample_1: FUS-LC, [U-13C; U-15N; U-2H], 50 ± 10 %

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 301 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D NCC	sample_1	fibrils	sample_conditions_1
3D CANH	sample_1	fibrils	sample_conditions_1
3D CONH	sample_1	fibrils	sample_conditions_1
3D NHH	sample_1	fibrils	sample_conditions_1
3D HN(CO)CX	sample_1	fibrils	sample_conditions_1
3D CAN(H)H	sample_1	fibrils	sample_conditions_1
3D CON(H)H	sample_1	fibrils	sample_conditions_1
3D NHH	sample_1	fibrils	sample_conditions_1
3D CANH	sample_1	fibrils	sample_conditions_1

Software:

SPARKY, T. D. Goddard and D. G. Kneller - peak picking

NMR spectrometers:

Varian InfinityPlus 600 MHz
Varian InfinityPlus 750 MHz

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