BMRB Entry 36493

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36493
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Insight into the C-terminal SH3 domain mediated binding of Drosophila Drk to Sos and Dos
Deposition date:
2022-06-15
Original release date:
2026-01-08
Authors:
Pooppadi, M.; Ikeya, T.; Sugasawa, H.; Watanabe, R.; Mishima, M.; Inomata, K.; Ito, Y.
Citation:

Citation: Sayeesh, P.; Ikeya, T.; Sugasawa, H.; Watanabe, R.; Mishima, M.; Inomata, K.; Ito, Y.. "Insight into the C-terminal SH3 domain mediated binding of Drosophila Drk to Sos and Dos."  Biochem. Biophys. Res. Commun. 625, 87-93 (2022).
PubMed: 35952612

Assembly members:

Assembly members:
Growth factor receptor-bound protein 2, polymer, 60 residues, 6913.521 Da.

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7211   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Growth factor receptor-bound protein 2: GEEMLVQALYDFVPQESGEL DFRRGDVITVTDRSDENWWN GEIGNRKGIFPATYVTPYHS

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts56
1H chemical shifts377

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 60 residues - 6913.521 Da.

1   GLYGLUGLUMETLEUVALGLNALALEUTYR
2   ASPPHEVALPROGLNGLUSERGLYGLULEU
3   ASPPHEARGARGGLYASPVALILETHRVAL
4   THRASPARGSERASPGLUASNTRPTRPASN
5   GLYGLUILEGLYASNARGLYSGLYILEPHE
6   PROALATHRTYRVALTHRPROTYRHISSER

Samples:

sample_1: the C-terminal SH3 domain of Drosophila, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: the C-terminal SH3 domain of Drosophila, [U-100% 15N], 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
13C-separated NOESYsample_1isotropicsample_conditions_1
15N-sperated NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_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 CBCANHsample_1isotropicsample_conditions_1
3D CCCONHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N COSYsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1

Software:

Azara v2.8, Boucher, W. - processing

CYANA v3.98, Guntert, P., Mumenthaler, C., and Wuthrich, K. - structure calculation

CcpNmr Analysis v2.5.1, CCPN - chemical shift assignment

OPALp, Luginbuhl, R., Guntert, P., Billeter, M., and Wuthrich, K. - refinement

TopSpin v3.5 PL7, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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