BMRB Entry 27932

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

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts111
1H chemical shifts264

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1FUS (371-526)1
2Ligand2

Entities:

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

Fus (371-526)

1   ARGARGALAASPPHEASNARGGLYGLYGLY
2   ASNGLYARGGLYGLYARGGLYARGGLYGLY
3   PROMETGLYARGGLYGLYTYRGLYGLYGLY
4   GLYSERGLYGLYGLYGLYARGGLYGLYPHE
5   PROSERGLYGLYGLYGLYGLYGLYGLYGLN
6   GLNARGALAGLYASPTRPLYSCYSPROASN
7   PROTHRCYSGLUASNMETASNPHESERTRP
8   ARGASNGLUCYSASNGLNCYSLYSALAPRO
9   LYSPROASPGLYPROGLYGLYGLYPROGLY
10   GLYSERHISMETGLYGLYASNTYRGLYASP
11   ASPARGARGGLYGLYARGGLYGLYTYRASP
12   ARGGLYGLYTYRARGGLYARGGLYGLYASP
13   ARGGLYGLYPHEARGGLYGLYARGGLYGLY
14   GLYASPARGGLYGLYPHEGLYPROGLYLYS
15   METASPSERARGGLYGLUHISARGGLNASP
16   ARGARGGLUARGPROTYRLEUGLUHISHIS
17   HISHISHISHIS

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:

NameSampleSample stateSample conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_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