BMRB Entry 18769

Name: Structural study of NS2(32-57) GBVB protein
Published: 2014-04-07

Click here to enlarge.

PDB ID: 2lzq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18769
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:

Structural study of NS2(32-57) GBVB protein

Deposition date:

2012-10-08

Original release date:

2014-04-07

Authors:

Montserret, Roland; Penin, Francois; Martin, Annette

Citation:

Citation: Boukadida, Celia; Marnata, Caroline; Montserret, Roland; Cohen, Lisette; Blumen, Brigitte; Gouttenoire, Jerome; Moradpour, Darius; Penin, Francois; Martin, Annette. "NS2 proteins of GB virus B and hepatitis C virus share common protease activities and membrane topologies." J. Virol. 88, 7426-7444 (2014).
PubMed: 24741107

Assembly members:

Assembly members:
NS2_32-57_GBVB, polymer, 26 residues, 3411.867 Da.

Natural source:

Natural source: Common Name: Hepatitis GB virus B Taxonomy ID: 39113 Superkingdom: Viruses Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS2_32-57_GBVB: RSALVNSYLWQRWENWFWNV TLRPER

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	108
1H chemical shifts	205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS2_32-57_GBVB	1

Entities:

Entity 1, NS2_32-57_GBVB 26 residues - 3411.867 Da.

1

ARG

SER

ALA

LEU

VAL

ASN

SER

TYR

LEU

TRP

2

GLN

ARG

TRP

GLU

ASN

TRP

PHE

TRP

ASN

VAL

3

THR

LEU

ARG

PRO

GLU

ARG

Samples:

sample_1: NS2_32-57_GBVB, [U-99% 2H], 2 ± 0.1 mM; TFE 50 ± 1 % v/v; H2O 50 ± 1 % v/v; DSS 0.2 ± 0.05 uM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 500 MHz