BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15579

Title: NS2(1-27)   PubMed: 18644781

Authors: Montserret, Roland; Penin, Francois

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts83
1H chemical shifts187

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS2(1-27)1

Entities:

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

1   METASPARGGLUMETALAALASERALAGLY
2   GLYALAVALPHEVALGLYLEUVALLEULEU
3   THRLEUSERPROHISTYRLYS

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:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_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

Related Database Links:

PDB