BMRB Entry 36445

Title:
Solution structure of the chimeric peptide of the first SURP domain of Human SF3A1 and the interacting region of SF1.
Deposition date:
2021-09-21
Original release date:
2022-10-03
Authors:
Muto, Y.; Kuwasako, K.; Takizawa, M.; Kobayashi, N.; Sakamoto, T.
Citation:

Citation: Nameki, Nobukazu; Takizawa, Masayuki; Suzuki, Takayuki; Tani, Shoko; Kobayashi, Naohiro; Sakamoto, Taiichi; Muto, Yutaka; Kuwasako, Kanako. "Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1"  Protein Sci. 31, e4437-e4437 (2022).
PubMed: 36173164

Assembly members:

Assembly members:
entity_1, polymer, 111 residues, 12133.198 Da.

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 BL21(DE3)   Vector: pET-15b

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts98
1H chemical shifts676

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 111 residues - 12133.198 Da.

1   GLYGLUVALARGASNILEVALASPLYSTHR
2   ALASERPHEVALALAARGASNGLYPROGLU
3   PHEGLUALAARGILEARGGLNASNGLUILE
4   ASNASNPROLYSPHEASNPHELEUASNPRO
5   ASNASPPROTYRHISALATYRTYRARGHIS
6   LYSVALSERGLUPHELYSGLUGLYLYSALA
7   GLNGLUPROSERSERGLYSERSERGLYSER
8   SERGLYSERSERGLYSERSERGLYGLNARG
9   PROGLYASPPROGLNSERALAGLNASPLYS
10   ALAARGMETASPLYSGLUTYRLEUSERLEU
11   METALAGLULEUGLYGLUALAPROVALPRO
12   ALA

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 1.4 mM; Sodium Phosphate, [U=100% 2H], 20 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_13C,15N-SEPARATED_NOESY SPECTRAsample_1isotropicsample_conditions_1

Software:

Amber v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

MagRO-NMRView, Kobayshi, N. - chemical shift assignment

NMRPipe v2007, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - peak picking

TALOS v2007, Cornilescu, Delaglio and Bax - geometry optimization

TopSpin v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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