BMRB Entry 51073

Name: The 1H, 15N, and 13C resonance assignments of the truncated Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region
Published: 2022-11-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51073

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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:

The 1H, 15N, and 13C resonance assignments of the truncated Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region

Deposition date:

2021-08-29

Original release date:

2022-11-28

Authors:

Barbosa, Glauce; Da Poian, Andrea; Almeida, Fabio

Citation:

Citation: Barbosa, Glauce; Morando, Maria; Da Poian, Andrea; Almeida, Fabio. "The 1H, 15N, and 13C resonance assignments of the truncated Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region" Biomol. NMR Assignments 17, 23-26 (2023).
PubMed: 36723824

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MRNRVSTVQQLTKRFSLGML QGRGPLKLFMALVAFLRFLT IPPTAGILKRWGTIKKSKAI NVLRGFRKEIGRMLNILNRR RR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	204
15N chemical shifts	58
1H chemical shifts	254

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Monomer	1

Entities:

Entity 1, Monomer 82 residues - Formula weight is not available

1

MET

ARG

ASN

ARG

VAL

SER

THR

VAL

GLN

2

LEU

THR

LYS

ARG

PHE

SER

LEU

GLY

MET

LEU

3

GLN

GLY

ARG

GLY

PRO

LEU

LYS

LEU

PHE

MET

4

ALA

LEU

VAL

ALA

PHE

LEU

ARG

PHE

LEU

THR

5

ILE

PRO

THR

ALA

GLY

ILE

LEU

LYS

ARG

6

TRP

GLY

THR

ILE

LYS

SER

LYS

ALA

ILE

7

ASN

VAL

LEU

ARG

GLY

PHE

ARG

LYS

GLU

ILE

8

GLY

ARG

MET

LEU

ASN

ILE

LEU

ASN

ARG

9

ARG

Samples:

sample_1: Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region, [U-100% 13C; U-100% 15N], 200 uM; D2O, [U-100% 2H], 10%; PMSF 2 mM; sodium azide 5 mM; EDTA 5 mM; sodium chloride 200 mM; sodium phosphate 55 mM; H2O 90%

sample_conditions_1: ionic strength: 0.25 M; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, data analysis

NMRDraw - data analysis, processing

CcpNMR - chemical shift assignment, data analysis, peak picking

TALOS-N - data analysis, geometry optimization

NMRbox - chemical shift assignment, collection, data analysis, geometry optimization, peak picking, processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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