BMRB Entry 53254

Title:
1H, 15N N-SH2 of Shp2 bound to 2pY-Gab1 617-684
Deposition date:
2025-07-05
Original release date:
2025-12-16
Authors:
Machner, Lisa; Balbach, Jochen
Citation:

Citation: Machner, Lisa; Shaikhqasem, Alaa; Hamdi, Farzad; Gruber, Tobias; Wiebe, Felix; Breithaupt, Constanze; Kniest, Judith; Lewitzky, Marc; Parthier, Christoph; Kyrilis, Fotios; Balbach, Jochen; Kastritis, Panagiotis; Feller, Stephan; Stubbs, Milton. "Mechanism of SHP2 activation by bis-Tyr-phosphorylated Gab1"  Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, Formula weight is not available
entity_2, polymer, 68 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: pETSUMO

Data sets:
Data typeCount
15N chemical shifts86
1H chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-Sh21
2Gab12

Entities:

Entity 1, N-Sh2 106 residues - Formula weight is not available

1   METTHRSERARGARGTRPPHEHISPROASN
2   ILETHRGLYVALGLUALAGLUASNLEULEU
3   LEUTHRARGGLYVALASPGLYSERPHELEU
4   ALAARGPROSERLYSSERASNPROGLYASP
5   PHETHRLEUSERVALARGARGASNGLYALA
6   VALTHRHISILELYSILEGLNASNTHRGLY
7   ASPTYRTYRASPLEUTYRGLYGLYGLULYS
8   PHEALATHRLEUALAGLULEUVALGLNTYR
9   TYRMETGLUHISHISGLYGLNLEULYSGLU
10   LYSASNGLYASPVALILEGLULEULYSTYR
11   PROLEUASNCYSALAASP

Entity 2, Gab1 68 residues - Formula weight is not available

both tyrosines are phosphorylated

1   ILELYSPROLYSGLYASPLYSGLNVALGLU
2   TYRLEUASPLEUASPLEUASPSERGLYLYS
3   SERTHRPROPROARGLYSGLNLYSSERSER
4   GLYSERGLYSERSERVALALAASPGLUARG
5   VALASPTYRVALVALVALASPGLNGLNLYS
6   THRLEUALALEULYSSERTHRARGGLUALA
7   TRPTHRASPGLYARGGLNSERTHR

Samples:

sample_1: N-SH2, [U-100% 13C; U-100% 15N], 750 uM; Gab1 1.125 mM; Bis Tris / HCl 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRView - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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