BMRB Entry 52133

Name: Backbone and sidechain chemical shift assignment of DRB3 dsRBD1
Published: 2024-09-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52133

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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 DRB3 dsRBD1

Deposition date:

2023-09-18

Original release date:

2024-09-20

Authors:

Paul, Jaydeep; Deshmukh, Mandar V.

Citation:

Citation: Paul, Jaydeep; Deshmukh, Mandar V.. "Chemical shift assignment of dsRBD1 and dsRBD2 of Arabidopsis thaliana DRB3, an essential protein involved in RNAi-mediated antiviral defense" Biomol. NMR Assign. 18, 99-9104 (2024).
PubMed: 38668800

Assembly members:

Assembly members:
entity_1, polymer, 83 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: MYKNQLQELAQRSCFSLPSY TCTREGPDHAPRFKASVNFN GEIFESPTYCSTLRQAEHSA AEVALSALSSKGPSKLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	297
15N chemical shifts	71
1H chemical shifts	427

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DRB3D1	1

Entities:

Entity 1, DRB3D1 83 residues - Formula weight is not available

dsRBD1 (1-75)

1

MET

TYR

LYS

ASN

GLN

LEU

GLN

GLU

LEU

ALA

2

GLN

ARG

SER

CYS

PHE

SER

LEU

PRO

SER

TYR

3

THR

CYS

THR

ARG

GLU

GLY

PRO

ASP

HIS

ALA

4

PRO

ARG

PHE

LYS

ALA

SER

VAL

ASN

PHE

ASN

5

GLY

GLU

ILE

PHE

GLU

SER

PRO

THR

TYR

CYS

6

SER

THR

LEU

ARG

GLN

ALA

GLU

HIS

SER

ALA

7

ALA

GLU

VAL

ALA

LEU

SER

ALA

LEU

SER

8

LYS

GLY

PRO

SER

LYS

LEU

GLU

HIS

9

HIS

Samples:

sample_1: DRB3 dsRBD1 200 uM; Pottasium phosphate buffer 50 mM; NaCl 50 mM; Na2SO4 50 mM

sample_2: DRB3 dsRBD1, [U-98% 15N], 550 uM; Pottasium phosphate buffer 50 mM; NaCl 50 mM; Na2SO4 50 mM

sample_3: DRB3 dsRBD1, [U-98% 13C; U-98% 15N], 550 uM; Pottasium phosphate buffer 50 mM; NaCl 50 mM; Na2SO4 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection

TOPSPIN v4.0 - processing

CARA v1.9.1 - peak picking

CARA v1.9.1 - chemical shift assignment

TALOS-N - data analysis

NMR spectrometers:

Bruker AVANCE NEO 600 MHz