Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18119

Title: ITK-SH3   PubMed: 31484725

Deposition date: 2011-12-05 Original release date: 2012-12-04

Authors: Kristiansen, Per Eugen; Bie Andersen, Thorny Cesilie; Huszenicza, Zsuzsi; Andreotti, Amy; Spurkland, Anne

Citation: Andersen, Thorny Cesilie Bie; Kristiansen, Per Eugen; Huszenicza, Zsuzsa; Johansson, Maria; Gopalakrishnan, Ramakrishna Prabhu; Kjelstrup, Hanna; Boyken, Scott; Sundvold-Gjerstad, Vibeke; Granum, Stine; Sorli, Morten; Backe, Paul Hoff; Fulton, D Bruce; Karlsson, B Goran; Andreotti, Amy; Spurkland, Anne. "The SH3 domains of the protein kinases ITK and LCK compete for adjacent sites on T cell-specific adapter protein"  J. Biol. Chem. 294, 15480-15494 (2019).

Assembly members:
entity, polymer, 66 residues, 7658.411 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGex-6P-1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts67
1H chemical shifts459

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, ITK-SH3 66 residues - 7658.411 Da.



sample_1: ITK-SH3, [U-98% 13C; U-98% 15N], 1.0 ± 0.1 mM; H2O 95%; D2O, [U-98% 2H], 5%; DSS 0.2 ± 0.02 mM; potassium phosphate 20 ± 1.0 mM

sample_2: ITK-SH3, [U-98% 13C; U-98% 15N], 1.0 ± 0.1 mM; D2O, [U-99.98% 2H], 100%; DSS 0.2 ± 0.02 mM; potassium phosphate 20 ± 1.0 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

sample_conditions_3: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K

sample_conditions_4: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K

sample_conditions_5: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_6: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_3
2D 1H-15N HSQCsample_1isotropicsample_conditions_4
2D 1H-15N HSQCsample_1isotropicsample_conditions_5
2D 1H-15N HSQCsample_1isotropicsample_conditions_6


CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

SPARKY v3.114, T. D. Goddard and D. G. Kneller, - chemical shift assignment

CARA v1.0, Fred Damberger - chemical shift assignment, peak picking

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN v2.1p4, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance II 600 MHz

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