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Biological Magnetic Resonance Data Bank


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BMRB Entry 17468

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17468

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Title: Resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A   PubMed: 21516467

Deposition date: 2011-02-14 Original release date: 2011-05-03

Authors: Feuerstein, Sophie; Willbold, Dieter; Brutscher, Bernhard

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).

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

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:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NS5A_fragment_(191-369): GPLGSLRGGEPEPDVTVLTS MLTDPSHITAETAKRRLARG SPPSLASSSASQLSAPSLKA TCTTHHDSPDADLIEANLLW RQEMGGNITRVESENKVVIL DSFEPLHADGDEREISVAAE ILRKSRKFPSALPIWARPDY NPPLLESWKDPDYVPPVVHG CPLPPTKAPPIPPPRRKRTV VLTESNVS

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

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