BMRB Entry 27932

Name: Folded ZnF in FUS (371-526)
Published: 2020-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27932

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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:

Folded ZnF in FUS (371-526)

Deposition date:

2019-05-29

Original release date:

2020-09-28

Authors:

Song, Jianxing; Lim, Liang Zhong

Citation:

Citation: Kang, Jian; Lim, Liangzhong; Lu, Yimei; Song, Jianxing. "A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids" PLoS Biol. 17, e3000327-e3000327 (2019).
PubMed: 31188823

Assembly members:

Assembly members:
FUS(371-526), polymer, 164 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FUS(371-526): RRADFNRGGGNGRGGRGRGG PMGRGGYGGGGSGGGGRGGF PSGGGGGGGQQRAGDWKCPN PTCENMNFSWRNECNQCKAP KPDGPGGGPGGSHMGGNYGD DRRGGRGGYDRGGYRGRGGD RGGFRGGRGGGDRGGFGPGK MDSRGEHRQDRRERPYLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	111
1H chemical shifts	264

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FUS (371-526)	1
2	Ligand	2

Entities:

Entity 1, FUS (371-526) 164 residues - Formula weight is not available

Fus (371-526)

1

ARG

ALA

ASP

PHE

ASN

ARG

GLY

2

ASN

GLY

ARG

GLY

ARG

GLY

ARG

GLY

3

PRO

MET

GLY

ARG

GLY

TYR

GLY

4

GLY

SER

GLY

ARG

GLY

PHE

5

PRO

SER

GLY

GLN

6

GLN

ARG

ALA

GLY

ASP

TRP

LYS

CYS

PRO

ASN

7

PRO

THR

CYS

GLU

ASN

MET

ASN

PHE

SER

TRP

8

ARG

ASN

GLU

CYS

ASN

GLN

CYS

LYS

ALA

PRO

9

LYS

PRO

ASP

GLY

PRO

GLY

PRO

GLY

10

GLY

SER

HIS

MET

GLY

ASN

TYR

GLY

ASP

11

ASP

ARG

GLY

ARG

GLY

TYR

ASP

12

ARG

GLY

TYR

ARG

GLY

ARG

GLY

ASP

13

ARG

GLY

PHE

ARG

GLY

ARG

GLY

14

GLY

ASP

ARG

GLY

PHE

GLY

PRO

GLY

LYS

15

MET

ASP

SER

ARG

GLY

GLU

HIS

ARG

GLN

ASP

16

ARG

GLU

ARG

PRO

TYR

LEU

GLU

HIS

17

HIS

Entity 2, Ligand - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: FUS(371-526), [U-99% 13C; U-99% 15N], 500 uM; ZnCl2 4 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, CCPN - chemical shift assignment, data analysis, processing

NMR spectrometers:

Bruker AMX 800 MHz

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