BMRB Entry 16166

Name: 1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1)
Published: 2009-03-20

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16166

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:

1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1)

Deposition date:

2009-02-11

Original release date:

2009-03-20

Authors:

Hanoulle, Xavier; Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Penin, Francois; Lippens, Guy

Citation:

Citation: Hanoulle, Xavier; Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Penin, Francois; Lippens, Guy. "Domain 3 of non structural protein 5A from hepatitis C virus is natively unfolded" Biochem. Biophys. Res. Commun. ., 634-638 (2009).
PubMed: 19249289

Assembly members:

Assembly members:
HCV_(Con1)_NS5A-D3, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Hepatitis C Virus Taxonomy ID: 11103 Superkingdom: Hepatitis C Virus Kingdom: not available Genus/species: Hepacivirus Hepatitis C Virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pT7.7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HCV_(Con1)_NS5A-D3: MRTVVLSESTVSSALAELAT KTFGSSESSAVDSGTATASP DQPSDDGDAGSDVESYSSMP PLEGEPGDPDLSDGSWSTVS EEASEDVVLQHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	257
15N chemical shifts	82
1H chemical shifts	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS5A-D3	1

Entities:

Entity 1, NS5A-D3 96 residues - Formula weight is not available

The first Methionine residue is a cloning artifact. The last 8 residues represent a non-native affinity tag. This is the domain 3 of the HCV (Con1, genotype 1b) NS5A protein.

1

MET

ARG

THR

VAL

LEU

SER

GLU

SER

THR

2

VAL

SER

ALA

LEU

ALA

GLU

LEU

ALA

THR

3

LYS

THR

PHE

GLY

SER

GLU

SER

ALA

4

VAL

ASP

SER

GLY

THR

ALA

THR

ALA

SER

PRO

5

ASP

GLN

PRO

SER

ASP

GLY

ASP

ALA

GLY

6

SER

ASP

VAL

GLU

SER

TYR

SER

MET

PRO

7

PRO

LEU

GLU

GLY

GLU

PRO

GLY

ASP

PRO

ASP

8

LEU

SER

ASP

GLY

SER

TRP

SER

THR

VAL

SER

9

GLU

ALA

SER

GLU

ASP

VAL

LEU

GLN

10

HIS

Samples:

sample_1: HCV (Con1) NS5A-D3, [U-95% 13C; U-98% 15N], 440 uM; sodium phosphate 20 mM; sodium chloride 30 mM; THP 1 mM; sodium azide 0.02%; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCANNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

In_house_product_plane_algorithm, Dries Verdegem & Guy Lippens - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 800 MHz

Swiss-Prot	Q9WMX2
Genbank	AJ238799
euHCVdb	AJ238799
BMRB	16800
DBJ	BAD73972 BAD73974 BAD73975 BAD73984 BAD73985
EMBL	CAB46677 CAB46911 CAB46913 CAB46915 CAB46917
GB	AAL55821 AAY23099 AAY23100 AAY23101 AAY23102
SP	Q9WMX2
AlphaFold	Q9WMX2