BMRB Entry 51327

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51327

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Title:
Backbone 1H, 13C and 15N chemical shift assignments for the N-terminal SH3 domain of Drk
Deposition date:
2022-02-13
Original release date:
2022-04-22
Authors:
Toyama, Yuki; Harkness, Robert; Kay, Lewis
Citation:

Citation: Toyama, Yuki; Harkness, Robert; Kay, Lewis. "Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease"  Proc. Nat. Acad. Sci., U. S. A. 119, e2203172119-e2203172119 (2022).

Assembly members:

Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GMEAIAKHDFSATADDELSF RKTQILKILNMEDDSNWYRA ELDGKEGLIPSNYIEMKNHD

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts114
1H chemical shifts114

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1drkN SH3 folded state1
2drkN SH3 unfolded state1

Entities:

Entity 1, drkN SH3 folded state 60 residues - Formula weight is not available

The first Glycine residue (G-1) is from the TEV-cleavage site. The sequence numbering starts from the second Methionine (M1).

1   GLYMETGLUALAILEALALYSHISASPPHE
2   SERALATHRALAASPASPGLULEUSERPHE
3   ARGLYSTHRGLNILELEULYSILELEUASN
4   METGLUASPASPSERASNTRPTYRARGALA
5   GLULEUASPGLYLYSGLUGLYLEUILEPRO
6   SERASNTYRILEGLUMETLYSASNHISASP

Samples:

sample_1: drkN SH3, [U-98% 13C; U-98% 15N], 0.4 mM; HEPES 20 mM; sodium chloride 50 mM; EDTA 1 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

TOPSPIN - collection

SMILE - processing

SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Related Database Links:

UNP Q08012
AlphaFold Q9V6Q5

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