BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26549

Title: Backbone 1H, 13C and 15N assignment of the intrinsically disordered region of HCV protein NS5A (191-447)   PubMed: 6445449

Deposition date: 2015-03-30 Original release date: 2015-04-27

Authors: Solyom, Zsofia; Schwarten, Melanie; Willbold, Dieter; Brutscher, Bernhard

Citation: Solyom, Zsofia; Ma, Peixiang; Schwarten, Melanie; Durand, Gregory; Willbold, Dieter; Brutscher, Bernhard. "Conformational properties of the disordered region of the NS5A protein from hepatitis C virus and their modulation by SH3 binding and phosphorylation"  Biophys J. 109, 1483-1496 (2015).

Assembly members:
NS5A(191-447), polymer, 268 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NS5A(191-447): GHMASGSLRGGEPEPDVTVL TSMLTDPSHITAETAKRRLA RGSPPSLASSSASQLSAPSL KATCTTHHDSPDADLIEANL LWRQEMGGNITRVESENKVV ILDSFEPLHADGDEREISVA AEILRKSRKFPSALPIWARP DYNPPLLESWKDPDYVPPVV HGCPLPPTKAPPIPPPRRKR TVVLTESNVSSALAELATKT FGSSGSSAVDSGTATALPDQ ASDDGDKGSDVESYSSMPPL EGEPGDPDLSDGSWSTVSEE ASEDVVCC

Data sets:
Data typeCount
13C chemical shifts689
15N chemical shifts235
1H chemical shifts433

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1NS5A D2D31

Entities:

Entity 1, NS5A D2D3 268 residues - Formula weight is not available

1   GLYHISMETALASERGLYSERLEUARGGLY
2   GLYGLUPROGLUPROASPVALTHRVALLEU
3   THRSERMETLEUTHRASPPROSERHISILE
4   THRALAGLUTHRALALYSARGARGLEUALA
5   ARGGLYSERPROPROSERLEUALASERSER
6   SERALASERGLNLEUSERALAPROSERLEU
7   LYSALATHRCYSTHRTHRHISHISASPSER
8   PROASPALAASPLEUILEGLUALAASNLEU
9   LEUTRPARGGLNGLUMETGLYGLYASNILE
10   THRARGVALGLUSERGLUASNLYSVALVAL
11   ILELEUASPSERPHEGLUPROLEUHISALA
12   ASPGLYASPGLUARGGLUILESERVALALA
13   ALAGLUILELEUARGLYSSERARGLYSPHE
14   PROSERALALEUPROILETRPALAARGPRO
15   ASPTYRASNPROPROLEULEUGLUSERTRP
16   LYSASPPROASPTYRVALPROPROVALVAL
17   HISGLYCYSPROLEUPROPROTHRLYSALA
18   PROPROILEPROPROPROARGARGLYSARG
19   THRVALVALLEUTHRGLUSERASNVALSER
20   SERALALEUALAGLULEUALATHRLYSTHR
21   PHEGLYSERSERGLYSERSERALAVALASP
22   SERGLYTHRALATHRALALEUPROASPGLN
23   ALASERASPASPGLYASPLYSGLYSERASP
24   VALGLUSERTYRSERSERMETPROPROLEU
25   GLUGLYGLUPROGLYASPPROASPLEUSER
26   ASPGLYSERTRPSERTHRVALSERGLUGLU
27   ALASERGLUASPVALVALCYSCYS

Samples:

sample_1: NS5A(191-447), [U-100% 13C; U-100% 15N], 120 uM; D2O, [U-100% 2H], 10%; potassium phosphate 50 mM; sodium chloride 20 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.32 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N BEST-TROSYsample_1isotropicsample_conditions_1
3D BT-HNCOCACBsample_1isotropicsample_conditions_1
3D BT-iHNCACBsample_1isotropicsample_conditions_1
3D BT-hNcocaNHsample_1isotropicsample_conditions_1
3D BT-hnCOcaNHsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts