BMRB Entry 51886

Name: Backbone and Sidechain Chemical Shift Assignments for D. melanogaster R2D2 dsRBD1 region
Published: 2023-08-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51886

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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 Assignments for D. melanogaster R2D2 dsRBD1 region

Deposition date:

2023-03-23

Original release date:

2023-08-31

Authors:

Aute, Ramdas; Deshmukh, Mandar V

Citation:

Citation: Aute, Ramdas; Deshmukh, Mandar V. "Chemical shift assignments of dsRBD1 and linker region of R2D2, a siRNA binding protein in the Drosophila RNAi pathway" Biomol. NMR Assign. 17, 211-215 (2023).
PubMed: 37405581

Assembly members:

Assembly members:
entity_1, polymer, 102 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: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDNKSAVSALQEFCARTQIN LPTYSFIPGEDGGYVCKVEL LEIEALGNGRSKRDAKHLAA SNILRKIQLLPGIHGLMKDS TVGDVGDELTNLNRLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	378
15N chemical shifts	91
1H chemical shifts	472

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R2D2 dsRBD1 and linker	1

Entities:

Entity 1, R2D2 dsRBD1 and linker 102 residues - Formula weight is not available

1

MET

ASP

ASN

LYS

SER

ALA

VAL

SER

ALA

LEU

2

GLN

GLU

PHE

CYS

ALA

ARG

THR

GLN

ILE

ASN

3

LEU

PRO

THR

TYR

SER

PHE

ILE

PRO

GLY

GLU

4

ASP

GLY

TYR

VAL

CYS

LYS

VAL

GLU

LEU

5

LEU

GLU

ILE

GLU

ALA

LEU

GLY

ASN

GLY

ARG

6

SER

LYS

ARG

ASP

ALA

LYS

HIS

LEU

ALA

7

SER

ASN

ILE

LEU

ARG

LYS

ILE

GLN

LEU

8

PRO

GLY

ILE

HIS

GLY

LEU

MET

LYS

ASP

SER

9

THR

VAL

GLY

ASP

VAL

GLY

ASP

GLU

LEU

THR

10

ASN

LEU

ASN

ARG

LEU

GLU

HIS

11

HIS

Samples:

sample_1: R2D2 dsRBD1 and linker, [U-100% 15N], 150 uM; R2D2 dsRBD1 and linker, [U-98% 13C; U-98% 15N], 500 uM; R2D2 dsRBD1 and linker, [U-10% 13C], 500 uM; Kphosphate 50 mM; Na2SO4 50 mM; NaCl 50 mM; DTT 2 mM

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

sample_conditions_2: ionic strength: 100 mM; pH: 7.0; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2

Software:

TOPSPIN v4.0 - collection, data analysis

CARA v1.8.4 - chemical shift assignment

CARA v1.8.4 - NOE assignments

X-PLOR NIH v2.37 - structure solution

CS-Rosetta v2021.16.61629 - structure solution

NMRFAM-SPARKY - structure solution

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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