BMRB Entry 27885

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the N-terminal domain of Sfr1   PubMed: 32204793
Deposition date:
2019-04-27
Original release date:
2020-03-18
Authors:
Sakakura, Masayoshi; Kurihara, Misato; Ito, Kentaro; Maki, Takahisa; Argunhan, Bilge; Iwasaki, Hiroshi; Takahashi, Hideo
Citation:

Citation: Argunhan, Bilge; Sakakura, Masayoshi; Afshar, Negar; Kurihara, Misato; Ito, Kentaro; Maki, Takahisa; Kanamaru, Shuji; Murayama, Yasuto; Tsubouchi, Hideo; Takahashi, Masayuki; Takahashi, Hideo; Iwasaki, Hiroshi. "Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex"  Elife 9, e52566-e52566 (2020).

Assembly members:

Assembly members:
Sfr1N, polymer, 176 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBKN220

Experimental source:

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBKN220

Data sets:
Data typeCount
13C chemical shifts515
15N chemical shifts157
1H chemical shifts157

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sfr1N1

Entities:

Entity 1, Sfr1N 176 residues - Formula weight is not available

1   METSERGLNTHRILEASNSERGLULEUASN
2   GLUASNALATHRSERGLNCYSLYSGLUASP
3   LEULYSVALSERLEUSERGLUSERASPLEU
4   ARGASPSERGLNGLYGLNLEUGLYILEGLU
5   ASNPROPROLYSCYSASNASNSERGLYASN
6   HISSERASPASNLEUGLYPHEILEGLUGLN
7   SERGLUTHRVALHISPROGLUASNGLULYS
8   ALALEUTHRPROASPLEUARGASPTHRLYS
9   ILEHISTHRSERLEUPROILETHRTHRPRO
10   PHESERLYSLYSARGALAARGGLUALALYS
11   ASNILELEULEULYSPROPHELYSSERPRO
12   LEUARGGLNTHRALASERPROGLNVALALA
13   ASPTHRASNLEULYSPROSERLEUALAVAL
14   THRASNLEUASNSERASPGLUTHRASNTHR
15   SERSERGLUPROVALTHRSERPROLEUARG
16   THRTHRPROASNSERILELYSARGGLNLYS
17   ARGLEUPHELYSSERPROILESERASNCYS
18   LEUASNPROLYSSERASP

Samples:

sample_1: Sfr1N, [U-13C; U-15N], 0.175 mM; sodium phosphate 20 mM; sodium chloride 25 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

NMRPipe v2012.090.12.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.134, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts