BMRB Entry 34709

Title:
Solution structure of homodimeric Capsid protein (residues 17-95) of Tick-borne encephalitis virus (d16-TBEVC)
Deposition date:
2022-02-14
Original release date:
2022-10-14
Authors:
Novotny, R.
Citation:

Citation: Selinger, Martin; Novotny, Radim; Sys, Jakub; Roby, Justin; Tykalova, Hana; Ranjani, Ganji Sri; Vancova, Marie; Jaklova, Katerina; Kaufman, Filip; Bloom, Marshall; Zdrahal, Zbynek; Grubhoffer, Libor; Forwood, Jade; Hrabal, Richard; Rumlova, Michaela; Sterba, Jan. "Tick-borne encephalitis virus capsid protein induces translational shutoff as revealed by its structural-biological analysis"  J. Biol. Chem. 298, 102585-102585 (2022).
PubMed: 36223838

Assembly members:

Assembly members:
entity_1, polymer, 79 residues, 8869.752 Da.

Natural source:

Natural source:   Common Name: Tick-borne encephalitis virus   Taxonomy ID: 11084   Superkingdom: Viruses   Kingdom: not available   Genus/species: Flavivirus Tick-borne encephalitis virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET22B

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts58
1H chemical shifts394

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 79 residues - 8869.752 Da.

1   VALSERLYSGLUTHRALATHRLYSTHRARG
2   GLNPROARGVALGLNMETPROASNGLYLEU
3   VALLEUMETARGMETMETGLYILELEUTRP
4   HISALAVALALAGLYTHRALAARGASNPRO
5   VALLEULYSALAPHETRPASNSERVALPRO
6   LEULYSGLNALATHRALAALALEUARGLYS
7   ILELYSARGTHRVALSERALALEUMETVAL
8   GLYLEUGLNLYSARGGLYLYSARGARG

Samples:

sample_1: d16-TBEVC, [U-99% 13C; U-99% 15N], 0.4 mM; NaCl, none, 50 mM; sodium phosphate, none, 50 mM; glycerol, none, 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - collection, processing

CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment, data analysis, peak picking

X-PLOR NIH v3.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

HADDOCK v2.2, Bonvin - processing

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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