BMRB Entry 52618

Name: Backbone and sidechain chemical shift assignment of DRB2 dsRBD1 (i.e., DRB2 (1-72))
Published: 2025-11-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52618

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

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Title:

Backbone and sidechain chemical shift assignment of DRB2 dsRBD1 (i.e., DRB2 (1-72))

Deposition date:

2024-09-24

Original release date:

2025-11-19

Authors:

Patra, Debadutta; Rai, Upasana; Deshmukh, Mandar V.

Citation:

Citation: Rai, Upasana; Patra, Debadutta; Deshmukh, Mandar V.. "Chemical shift assignments of DRB2 domains, a dsRNA binding protein in A. thaliana RNAi pathway" Biomol. NMR Assignments 19, 71-76 (2025).
PubMed: 39881054

Assembly members:

Assembly members:
entity_1, polymer, 80 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MYKNQLQELAQRSCFNLPSY TCIREGPDHAPRFKATVNFN GEIFESPQYCSTLRQAEHSA AEVALNALSNRGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	68
1H chemical shifts	435

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DRB2 dsRBD1	1

Entities:

Entity 1, DRB2 dsRBD1 80 residues - Formula weight is not available

1	MET	TYR	LYS	ASN	GLN	LEU	GLN	GLU	LEU	ALA
2	GLN	ARG	SER	CYS	PHE	ASN	LEU	PRO	SER	TYR
3	THR	CYS	ILE	ARG	GLU	GLY	PRO	ASP	HIS	ALA
4	PRO	ARG	PHE	LYS	ALA	THR	VAL	ASN	PHE	ASN
5	GLY	GLU	ILE	PHE	GLU	SER	PRO	GLN	TYR	CYS
6	SER	THR	LEU	ARG	GLN	ALA	GLU	HIS	SER	ALA
7	ALA	GLU	VAL	ALA	LEU	ASN	ALA	LEU	SER	ASN
8	ARG	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: DRB2 dsRBD1, [U-98% 15N], 200 uM; DRB2 dsRBD1, [U-98% 13C; U-98% 15N], 500 uM; KPhos 50 mM; NaCl 50 mM; Na2SO4 50 mM; DTT 4 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH- TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)C(CCO)NH- TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection, data analysis, processing

CARA v1.8.4 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance II 600 MHz

1	MET	TYR	LYS	ASN	GLN	LEU	GLN	GLU	LEU	ALA
2	GLN	ARG	SER	CYS	PHE	ASN	LEU	PRO	SER	TYR
3	THR	CYS	ILE	ARG	GLU	GLY	PRO	ASP	HIS	ALA
4	PRO	ARG	PHE	LYS	ALA	THR	VAL	ASN	PHE	ASN
5	GLY	GLU	ILE	PHE	GLU	SER	PRO	GLN	TYR	CYS
6	SER	THR	LEU	ARG	GLN	ALA	GLU	HIS	SER	ALA
7	ALA	GLU	VAL	ALA	LEU	ASN	ALA	LEU	SER	ASN
8	ARG	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	TYR	LYS	ASN	GLN	LEU	GLN	GLU	LEU	ALA
2	GLN	ARG	SER	CYS	PHE	ASN	LEU	PRO	SER	TYR
3	THR	CYS	ILE	ARG	GLU	GLY	PRO	ASP	HIS	ALA
4	PRO	ARG	PHE	LYS	ALA	THR	VAL	ASN	PHE	ASN
5	GLY	GLU	ILE	PHE	GLU	SER	PRO	GLN	TYR	CYS
6	SER	THR	LEU	ARG	GLN	ALA	GLU	HIS	SER	ALA
7	ALA	GLU	VAL	ALA	LEU	ASN	ALA	LEU	SER	ASN
8	ARG	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS