BMRB Entry 18768

Name: Structural study of NS2(2-32) GBVB protein
Published: 2014-04-07

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PDB ID: 2lzp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18768
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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:

Structural study of NS2(2-32) 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_2-32_GBVB, polymer, 31 residues, 3370.069 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 Host organism: none Vector: none

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS2_2-32_GBVB: DTEIIGGLTIPPVVALVVMS RFGFFAHLLPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	102
1H chemical shifts	230

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS2_2-32_GBVB	1

Entities:

Entity 1, NS2_2-32_GBVB 31 residues - 3370.069 Da.

1

ASP

THR

GLU

ILE

GLY

LEU

THR

ILE

2

PRO

VAL

ALA

LEU

VAL

MET

SER

3

ARG

PHE

GLY

PHE

ALA

HIS

LEU

PRO

4

ARG

Samples:

sample_1: NS2_2-32_GBVB, [U-99% 2H], 2 ± 0.1 mM; TFE 50 % v/v; H2O 50 % v/v

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 - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis, structure solution

NMR spectrometers:

Bruker Avance 500 MHz