BMRB Entry 50994

Name: Backbone 1H, 15N and 13C resonance assignments of a non-structural protein NS2B of Zika virus
Published: 2021-12-13

Click here to enlarge.

PDB ID: 8v0h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50994
MolProbity Validation Chart

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, 15N and 13C resonance assignments of a non-structural protein NS2B of Zika virus PubMed: 34817802

Deposition date: 2021-06-23 Original release date: 2021-12-13

Authors: Penna, Beatriz; de Oliveira, Danielle Maria; Anobom, Cristiane; Valente, Ana Paula

Citation: Penna, Beatriz; de Oliveira, Danielle; Anobom, Cristiane; Valente, Ana Paula. "Backbone 1 H, 15 N, and 13 C resonance assignments of the non-structural protein NS2B of Zika virus" Biomolecular NMR Assignments 16, 31-35 (2022).

Assembly members:
entity_1, polymer, 160 residues, Formula weight is not available

Natural source: Common Name: Zika Virus Taxonomy ID: 64320 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Zika Virus

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MGSENLYFQGSWPPSEVLTA VGLICALAGGFAKADIEMAG PMAAVGLLIVSYVVSGKSVD MYIERAGDITWEKDAEVTGN SPRLDVALDESGDFSLVEED GPPMREIILKVVLMAICGMN PIAIPFAAGAWYVYVKTGKR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	388
15N chemical shifts	126
1H chemical shifts	126

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS2B Protein	1

Entities:

Entity 1, NS2B Protein 160 residues - Formula weight is not available

Residues 1-30 represent a hexa-histidine tag, thrombin and TEV cleavage sites.

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	GLY	SER	GLU	ASN	LEU	TYR	PHE	GLN	GLY
4	SER	TRP	PRO	PRO	SER	GLU	VAL	LEU	THR	ALA
5	VAL	GLY	LEU	ILE	CYS	ALA	LEU	ALA	GLY	GLY
6	PHE	ALA	LYS	ALA	ASP	ILE	GLU	MET	ALA	GLY
7	PRO	MET	ALA	ALA	VAL	GLY	LEU	LEU	ILE	VAL
8	SER	TYR	VAL	VAL	SER	GLY	LYS	SER	VAL	ASP
9	MET	TYR	ILE	GLU	ARG	ALA	GLY	ASP	ILE	THR
10	TRP	GLU	LYS	ASP	ALA	GLU	VAL	THR	GLY	ASN
11	SER	PRO	ARG	LEU	ASP	VAL	ALA	LEU	ASP	GLU
12	SER	GLY	ASP	PHE	SER	LEU	VAL	GLU	GLU	ASP
13	GLY	PRO	PRO	MET	ARG	GLU	ILE	ILE	LEU	LYS
14	VAL	VAL	LEU	MET	ALA	ILE	CYS	GLY	MET	ASN
15	PRO	ILE	ALA	ILE	PRO	PHE	ALA	ALA	GLY	ALA
16	TRP	TYR	VAL	TYR	VAL	LYS	THR	GLY	LYS	ARG

Samples:

sample_1: NS2B, [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 20 mM; sodium azide 5 mM; beta-mercaptoethanol 2 mM; SDS 0.1%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	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)CA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN vTopSpin3.1 - processing

NMRPipe - processing

CcpNMR vAnalysis v.2.4.2 - data analysis

NMRbox - data analysis

NMR spectrometers:

Bruker AVANCE III 900 MHz

Biological Magnetic Resonance Data Bank