BMRB Entry 26328

Title:
Backbone assignment of the N-terminal SH2 domain of PI3K
Deposition date:
2022-03-19
Original release date:
2023-06-05
Authors:
Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Asahina, Yuya; Kawakami, Toru; Kuroda, Mataka; Mizuguchi, Kenji; Oda, Masayuki
Citation:

Citation: Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Ochi, Saki; Asahina, Yuya; Kawakami, Toru; Kuroda, Masataka; Mizuguchi, Kenji; Oda, Masayuki. "Structural dynamics of the N-terminal SH2 domain of PI3K in its free and CD28-bound states"  FEBS J. 290, 2366-2378 (2023).
PubMed: 36282120

Assembly members:

Assembly members:
N-terminal SH2 domain of PI3K, polymer, 107 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: pGEX

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts301
15N chemical shifts100
1H chemical shifts100

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nSH2 of PI3K1

Entities:

Entity 1, nSH2 of PI3K 107 residues - Formula weight is not available

1   SERASNMETSERLEUGLNASNALAGLUTRP
2   TYRTRPGLYASPILESERARGGLUGLUVAL
3   ASNGLULYSLEUARGASPTHRALAASPGLY
4   THRPHELEUVALARGASPALASERTHRLYS
5   METHISGLYASPTYRTHRLEUTHRLEUARG
6   LYSGLYGLYASNASNLYSLEUILELYSILE
7   PHEHISARGASPGLYLYSTYRGLYPHESER
8   ASPPROLEUTHRPHESERSERVALVALGLU
9   LEUILEASNHISTYRARGASNGLUSERLEU
10   ALAGLNTYRASNPROLYSLEUASPVALLYS
11   LEULEUTYRPROVALSERLYS

Samples:

sample_1: N-terminal SH2 domain of PI3K, [U-99% 13C; U-99% 15N], 0.1 – 0.3 mM; potassium phosphate 10 mM; sodium 2,2-dimethyl-2-silapentane-5-sulfonate 0.01 % v/v; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz

Related Database Links:

PDB

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