BMRB Entry 27362

Title:
Backbone (HN, N) Resonance Assignment and 15N T1, T2 Relaxation Parameters for doubly phosphorylated Abl1 SH3 pY89/pY134
Deposition date:
2018-01-16
Original release date:
2019-01-18
Authors:
Toke, Orsolya; Mero, Balazs; Radnai, Laszlo; Buday, Laszlo
Citation:

Citation: Mero, Balazs; Radnai, Laszlo; Gogl, Gergo; Toke, Orsolya; Leveles, Ibolya; Koprivanacz, Kitti; Szeder, Balint; Dulk, Metta; Kudlik, Gyongyi; Vas, Virag; Cserkaszky, Anna; Sipeki, Szabolcs; Nyitray, Laszlo; Vertessy, Beata; Buday, Laszlo. "Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions"  J. Biol. Chem. 294, 4608-4620 (2019).
PubMed: 30659095

Assembly members:

Assembly members:
Abl1_SH3_pY89pY134, polymer, 58 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: modified pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Abl1_SH3_pY89pY134: MNLFVALXDFVASGDNTLSI TKGEKLRVLGYNHNGEWCEA QTKNGQGWVPSNXITPVN

Data sets:
Data typeCount
15N chemical shifts49
1H chemical shifts49
T1 relaxation values49
T2 relaxation values49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Src homology domain 31

Entities:

Entity 1, Src homology domain 3 58 residues - Formula weight is not available

1   METASNLEUPHEVALALALEUPTRASPPHE
2   VALALASERGLYASPASNTHRLEUSERILE
3   THRLYSGLYGLULYSLEUARGVALLEUGLY
4   TYRASNHISASNGLYGLUTRPCYSGLUALA
5   GLNTHRLYSASNGLYGLNGLYTRPVALPRO
6   SERASNPTRILETHRPROVALASN

Samples:

sample_1: Abl1 SH3 pY89pY134, [U-15N], 1.0 mM; NaN3 3 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T1 relaxationsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T2 relaxationsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - data collection

Felix, Accelrys - chemical shift assignment

CcpNMR, CCPN - data analysis

NMR spectrometers:

  • Varian Varian NMR System 600 MHz

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