BMRB Entry 16800

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16800

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Title:
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) in presence of 50%TFE
Deposition date:
2010-03-29
Original release date:
2011-05-02
Authors:
Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Landrieu, Isabelle; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy; Hanoulle, Xavier
Citation:

Citation: Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Landrieu, Isabelle; Leroy, Arnaud; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy; Hanoulle, Xavier. "Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A."  J. Biol. Chem. 286, 20441-20454 (2011).
PubMed: 21489988

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: 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:
Data typeCount
13C chemical shifts252
15N chemical shifts82
1H chemical shifts82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS5A-D31

Entities:

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

1   METARGTHRVALVALLEUSERGLUSERTHR
2   VALSERSERALALEUALAGLULEUALATHR
3   LYSTHRPHEGLYSERSERGLUSERSERALA
4   VALASPSERGLYTHRALATHRALASERPRO
5   ASPGLNPROSERASPASPGLYASPALAGLY
6   SERASPVALGLUSERTYRSERSERMETPRO
7   PROLEUGLUGLYGLUPROGLYASPPROASP
8   LEUSERASPGLYSERTRPSERTHRVALSER
9   GLUGLUALASERGLUASPVALVALLEUGLN
10   HISHISHISHISHISHIS

Samples:

sample_1: HCV (Con1) NS5A-D3, [U-95% 13C; U-98% 15N], 360 uM; sodium phosphate 20 mM; sodium chloride 30 mM; sodium azide 0.02%; THP 1 mM; D2O, [U-99.9% 2H], 5%; H2O 95%; TFE, [U-100% 2H], 50%

sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

In_house_product_plane_algorithm v1.5, Dries Verdegem & Guy Lippens - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16166
DBJ BAD73972 BAD73974 BAD73975 BAD73984 BAD73985
EMBL CAB46677 CAB46911 CAB46913 CAB46915 CAB46917
GB AAL55821 AAY23099 AAY23100 AAY23101 AAY23102
SP Q9WMX2
AlphaFold Q9WMX2

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks