BMRB Entry 17468

Title:
Resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A
Deposition date:
2011-02-14
Original release date:
2011-05-03
Authors:
Feuerstein, Sophie; Willbold, Dieter; Brutscher, Bernhard
Citation:

Citation: Feuerstein, Sophie; Solyom, Zsofia; Alada, Amine; Hoffmann, Silke; Willbold, Dieter; Brutscher, Bernhard. "1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A."  Biomol. NMR Assignments 5, 241-243 (2011).
PubMed: 21516467

Assembly members:

Assembly members:
NS5A_fragment_(191-369), polymer, 188 residues, 20400 Da.

Natural source:

Natural source:   Common Name: Hepatitis C virus subtype 1b   Taxonomy ID: 31647   Superkingdom: virus   Kingdom: not available   Genus/species: Hepacivirus Hepatitis C virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-2

Data sets:
Data typeCount
13C chemical shifts511
15N chemical shifts160
1H chemical shifts160

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS5A fragment (191-369) monomer1

Entities:

Entity 1, NS5A fragment (191-369) monomer 188 residues - 20400 Da.

residue 1-9 non-native linker between protease cleavage site and NS5A residues 191-369

1   GLYPROLEUGLYSERLEUARGGLYGLYGLU
2   PROGLUPROASPVALTHRVALLEUTHRSER
3   METLEUTHRASPPROSERHISILETHRALA
4   GLUTHRALALYSARGARGLEUALAARGGLY
5   SERPROPROSERLEUALASERSERSERALA
6   SERGLNLEUSERALAPROSERLEULYSALA
7   THRCYSTHRTHRHISHISASPSERPROASP
8   ALAASPLEUILEGLUALAASNLEULEUTRP
9   ARGGLNGLUMETGLYGLYASNILETHRARG
10   VALGLUSERGLUASNLYSVALVALILELEU
11   ASPSERPHEGLUPROLEUHISALAASPGLY
12   ASPGLUARGGLUILESERVALALAALAGLU
13   ILELEUARGLYSSERARGLYSPHEPROSER
14   ALALEUPROILETRPALAARGPROASPTYR
15   ASNPROPROLEULEUGLUSERTRPLYSASP
16   PROASPTYRVALPROPROVALVALHISGLY
17   CYSPROLEUPROPROTHRLYSALAPROPRO
18   ILEPROPROPROARGARGLYSARGTHRVAL
19   VALLEUTHRGLUSERASNVALSER

Samples:

sample_1: NS5A fragment (191-369), [U-98% 13C; U-98% 15N], 130 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST-TROSYsample_1isotropicsample_conditions_1
2D HADAMACsample_1isotropicsample_conditions_1
3D BEST-TROSY HNCOsample_1isotropicsample_conditions_1
3D BEST-TROSY HNcoCAsample_1isotropicsample_conditions_1
3D BEST-TROSY iHNCAsample_1isotropicsample_conditions_1
3D BEST-TROSY HNcoCACBsample_1isotropicsample_conditions_1
3D BEST-TROSY iHNCACBsample_1isotropicsample_conditions_1
3D BEST-TROSY hNcocaNHsample_1isotropicsample_conditions_1
3D BEST-TROSY hnCOcaNHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

VNMRJ, Varian - collection

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Varian VNMRS 800 MHz

Related Database Links:

BMRB 26549
DBJ BAA01583 BAA02756
GB AAC15722 AAC15723 AAC15724 AAC15725 AAC15726
SP O92972
AlphaFold O92972

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