BMRB Entry 26870

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26870

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Title:
NMR chemical shifts of the N-terminal SH3 domain from CT10-Regulator of Kinase (Crk)-II
Deposition date:
2016-08-08
Original release date:
2019-07-10
Authors:
Zeng, Danyun; Cho, Jae-Hyun
Citation:

Citation: Zeng, Danyun; Bhatt, Veer; Shen, Qingliang; Cho, Jae-Hyun. "Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl."  Biophys. J. 111, 1843-1853 (2016).
PubMed: 27806266

Assembly members:

Assembly members:
nSH3_of_CrkII, polymer, 83 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nSH3_of_CrkII: SGVILRQEEAEYVRALFDFN GNDEEDLPFKKGDILRIRDK PEEQWWNAEDSEGKRGMIPV PYVEKYRPASASVSALIGGN QEG

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts91
1H chemical shifts577

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal SH31

Entities:

Entity 1, N-terminal SH3 83 residues - Formula weight is not available

1   SERGLYVALILELEUARGGLNGLUGLUALA
2   GLUTYRVALARGALALEUPHEASPPHEASN
3   GLYASNASPGLUGLUASPLEUPROPHELYS
4   LYSGLYASPILELEUARGILEARGASPLYS
5   PROGLUGLUGLNTRPTRPASNALAGLUASP
6   SERGLUGLYLYSARGGLYMETILEPROVAL
7   PROTYRVALGLULYSTYRARGPROALASER
8   ALASERVALSERALALEUILEGLYGLYASN
9   GLNGLUGLY

Samples:

sample_1: nSH3 of CrkII, [U-99% 13C; U-99% 15N], 300 uM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 80 mM

sample_conditions_1: ionic strength: 80 mM; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C TOCSY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CDCG)HGsample_1isotropicsample_conditions_1
2D (HB)CB(CDCGCE)HEsample_1isotropicsample_conditions_1
2D CO(side-chain carboxyl)NHsample_1isotropicsample_conditions_1
2D H(C)CO(side-chain carboxyl)sample_1isotropicsample_conditions_1

Software:

CARA v1.9.1.4, Keller and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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