BMRB Entry 27887

Name: Backbone (1H and 15N) Chemical Shift Assignments and Relaxation Parameters for the low complexity domain of FUS in the condensed phase
Published: 2019-06-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27887

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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:

Backbone (1H and 15N) Chemical Shift Assignments and Relaxation Parameters for the low complexity domain of FUS in the condensed phase

Deposition date:

2019-05-01

Original release date:

2019-06-11

Authors:

Murthy, Anastasia; Burke, Kathleen; Fawzi, Nicolas

Citation:

Citation: Murthy, Anastasia; Dignon, Gregory; Kan, Yelena; Zerze, Gul; Parekh, Sapun; Mittal, Jeetain; Fawzi, Nicolas. "Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain" Nat. Struct. Mol. Biol. 26, 637-648 (2019).
PubMed: 31270472

Assembly members:

Assembly members:
FUS_1-163, polymer, 163 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: Unknown

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FUS_1-163: MASNDYTQQATQSYGAYPTQ PGQGYSQQSSQPYGQQSYSG YSQSTDTSGYGQSSYSSYGQ SQNTGYGTQSTPQGYGSTGG YGSSQSSQSSYGQQSSYPGY GQQPAPSSTSGSYGSSSQSS SYGQPQSGSYSQQPSYGGQQ QSYGQQQSYNPPQGYGQQNQ YNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
15N chemical shifts	145
T1 relaxation values	35
T2 relaxation values	43
heteronuclear NOE values	35

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FUS 1-163	1

Entities:

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

The protein sequence starts from alanine 2 due to cleavage of the n-terminal methionine.

1

MET

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: Condensed FUS 1-163, [U-99% 15N], 27.8 mM; MES 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 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
hsqct2etf3gpsitc3d	sample_1	isotropic	sample_conditions_1
hsqct1etf3gpsitc3d	sample_1	isotropic	sample_conditions_1
hsqcnoef3gpsi	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 850 MHz