BMRB Entry 15579

Name: NS2(1-27)
Published: 2008-06-04

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PDB ID: 2jy0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15579
MolProbity Validation Chart

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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:

NS2(1-27)

Deposition date:

2007-12-04

Original release date:

2008-06-04

Authors:

Montserret, Roland; Penin, Francois

Citation:

Citation: Jirasko, Vlastimil; Montserret, Roland; Appel, Nicole; Janvier, Anne; Eustachi, Leah; Brohm, Christiane; Steinmann, Eike; Pietschmann, Thomas; Penin, Francois; Bartenschlager, Ralf. "Structural and functional characterization of non-structural protein 2 for its role in hepatitis C virus assembly" J. Biol. Chem. 283, 28546-28562 (2008).
PubMed: 18644781

Assembly members:

Assembly members:
NS2(1-27), polymer, 27 residues, 2834.36 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis Host organism: none Vector: none

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS2(1-27): MDREMAASAGGAVFVGLVLL TLSPHYK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	83
1H chemical shifts	187

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NS2(1-27)	1

Entities:

Entity 1, NS2(1-27) 27 residues - 2834.36 Da.

1

MET

ASP

ARG

GLU

MET

ALA

SER

ALA

GLY

2

GLY

ALA

VAL

PHE

VAL

GLY

LEU

VAL

LEU

3

THR

LEU

SER

PRO

HIS

TYR

LYS

Samples:

sample_1: NS2(1-27) 0.9 ± 0.1 mM; Trifluoro ethanol D2OH, [U-100% 2H], 50 % v/v; H2O 90 % v/v

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

sample_conditions_2: temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2

Software:

VNMR, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

Varian UnityPlus 500 MHz