BMRB Entry 34570

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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/BMR34570
MolProbity Validation Chart

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Title:
Solution NMR structure of the SH3 domain of human Caskin1
Deposition date:
2020-11-01
Original release date:
2021-02-01
Authors:
Toke, O.; Koprivanacz, K.; Radnai, L.; Mero, B.; Juhasz, T.; Liliom, K.; Buday, L.
Citation:

Citation: Toke, O.; Koprivanacz, K.; Radnai, L.; Mero, B.; Juhasz, T.; Liliom, K.; Buday, L.. "Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding"  Cells 10, 173-173 (2021).
PubMed: 33467043

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, 7458.308 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMLQVRATKDYCNNYDLT SLNVKAGDIITVLEQHPDGR WKGCIHDNRTGNDRVGYFPS SLGEAIV

Data sets:
Data typeCount
13C chemical shifts101
15N chemical shifts69
1H chemical shifts400

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 67 residues - 7458.308 Da.

1   GLYSERHISMETLEUGLNVALARGALATHR
2   LYSASPTYRCYSASNASNTYRASPLEUTHR
3   SERLEUASNVALLYSALAGLYASPILEILE
4   THRVALLEUGLUGLNHISPROASPGLYARG
5   TRPLYSGLYCYSILEHISASPASNARGTHR
6   GLYASNASPARGVALGLYTYRPHEPROSER
7   SERLEUGLYGLUALAILEVAL

Samples:

sample_1: human caskin1 SH3 domain, [U-13C; U-15N], 0.6 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_2: human caskin1 SH3 domain, [U-15N], 0.6 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_3: human caskin1 SH3 domain 1 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CC-TOCSY-NNHsample_1isotropicsample_conditions_1
3D HCC-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D Met-Met NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

VnmrJ, Varian - collection

Felix, Accelrys Software Inc. - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

  • Varian Uniform 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