BMRB Entry 51299

Title:
SRSF1 Unphosphorylated
Deposition date:
2022-02-02
Original release date:
2023-03-21
Authors:
Fargason, Talia; Zhang, Jun
Citation:

Citation: Fargason, Talia; De Silva, Naiduwadura Ivon Upekala; King, Erin; Zhang, Zihan; Paul, Trenton; Shariq, Jamal; Zaharias, Steve; Zhang, Jun. "Peptides that Mimic RS repeats modulate phase separation of SRSF1, revealing a reliance on combined stacking and electrostatic interactions"  Elife 12, e84412-e84412 (2023).
PubMed: 36862748

Assembly members:

Assembly members:
entity_1, polymer, 248 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: PSMT3

Data sets:
Data typeCount
13C chemical shifts580
15N chemical shifts191
1H chemical shifts192

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SRSF11

Entities:

Entity 1, SRSF1 248 residues - Formula weight is not available

1   METSERGLYGLYGLYVALILEARGGLYPRO
2   ALAGLYASNASNASPCYSARGILETYRVAL
3   GLYASNLEUPROPROASPILEARGTHRLYS
4   ASPILEGLUASPVALPHETYRLYSTYRGLY
5   ALAILEARGASPILEASPLEULYSASNARG
6   ARGGLYGLYPROPROPHEALAPHEVALGLU
7   PHEGLUASPPROARGASPALAGLUASPALA
8   VALTYRGLYARGASPGLYTYRASPTYRASP
9   GLYTYRARGLEUARGVALGLUPHEPROARG
10   SERGLYARGGLYTHRGLYARGGLYGLYGLY
11   GLYGLYGLYGLYGLYGLYALAPROARGGLY
12   ARGTYRGLYPROPROSERARGARGSERGLU
13   ASNARGVALVALVALSERGLYLEUPROPRO
14   SERGLYSERTRPGLNASPLEULYSASPHIS
15   METARGGLUALAGLYASPVALCYSTYRALA
16   ASPVALTYRARGASPGLYTHRGLYVALVAL
17   GLUPHEVALARGLYSGLUASPMETTHRTYR
18   ALAVALARGLYSLEUASPASNTHRLYSPHE
19   ARGSERHISGLUGLYGLUTHRALATYRILE
20   ARGVALLYSVALASPGLYPROARGSERPRO
21   SERTYRGLYARGSERARGSERARGSERARG
22   SERARGSERARGSERARGSERARGSERASN
23   SERARGSERARGSERTYRSERPROARGARG
24   SERARGGLYSERPROARGTYRSERPROARG
25   HISSERARGSERARGSERARGTHR

Samples:

sample_1: SRSF1, [U-2H; U-13C; U-15N], 370 uM; D2O, [U-2H], 5%; Arginine/Glutamate 400 mM; ERER peptide 100 mM; TCEP 1 mM; sodium azide 0.02%

sample_2: SRSF1, [U-13C; U-15N], 370 uM; D2O, [U-2H], 5%; Arginine/Glutamate 400 mM; ERER peptide 100 mM; TCEP 1 mM; sodium azide 0.02%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
2D MUSIC TAVIsample_2isotropicsample_conditions_1
2D MUSIC TAVI_2sample_2isotropicsample_conditions_1
2D MUSIC QN_2sample_2isotropicsample_conditions_1
2D MUSIC FYHWsample_2isotropicsample_conditions_1
2D MUSIC FYHW_2sample_2isotropicsample_conditions_1
2D MUSIC KRsample_2isotropicsample_conditions_1
2D MUSIC KR_2sample_2isotropicsample_conditions_1
2D MUSIC Glysample_2isotropicsample_conditions_1
2D MUSIC Gly_2sample_2isotropicsample_conditions_1
2D MUSIC Prosample_2isotropicsample_conditions_1
2D MUSIC Pro_2sample_2isotropicsample_conditions_1
2D MUSIC TAVIsample_2isotropicsample_conditions_1
2D MUSIC TAVI_2sample_2isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment, data analysis, peak picking

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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