BMRB Entry 51327

Name: Backbone 1H, 13C and 15N chemical shift assignments for the N-terminal SH3 domain of Drk
Published: 2022-04-22

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

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

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

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

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

Entity Sequences (FASTA):
entity_1: GMEAIAKHDFSATADDELSF RKTQILKILNMEDDSNWYRA ELDGKEGLIPSNYIEMKNHD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	342
15N chemical shifts	114
1H chemical shifts	114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	drkN SH3 folded state	1
2	drkN SH3 unfolded state	1

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	GLY	MET	GLU	ALA	ILE	ALA	LYS	HIS	ASP	PHE
2	SER	ALA	THR	ALA	ASP	ASP	GLU	LEU	SER	PHE
3	ARG	LYS	THR	GLN	ILE	LEU	LYS	ILE	LEU	ASN
4	MET	GLU	ASP	ASP	SER	ASN	TRP	TYR	ARG	ALA
5	GLU	LEU	ASP	GLY	LYS	GLU	GLY	LEU	ILE	PRO
6	SER	ASN	TYR	ILE	GLU	MET	LYS	ASN	HIS	ASP

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

TOPSPIN - collection

SMILE - processing

SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

UNP	Q08012
AlphaFold	Q9V6Q5

Biological Magnetic Resonance Data Bank