BMRB Entry 51073

Title:
The 1H, 15N, and 13C resonance assignments of the truncated Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region
Deposition date:
2021-08-29
Original release date:
2022-11-28
Authors:
Barbosa, Glauce; Da Poian, Andrea; Almeida, Fabio
Citation:

Citation: Barbosa, Glauce; Morando, Maria; Da Poian, Andrea; Almeida, Fabio. "The 1H, 15N, and 13C resonance assignments of the truncated Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region"  Biomol. NMR Assignments 17, 23-26 (2023).
PubMed: 36723824

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts204
15N chemical shifts58
1H chemical shifts254

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Monomer1

Entities:

Entity 1, Monomer 82 residues - Formula weight is not available

1   METARGASNARGVALSERTHRVALGLNGLN
2   LEUTHRLYSARGPHESERLEUGLYMETLEU
3   GLNGLYARGGLYPROLEULYSLEUPHEMET
4   ALALEUVALALAPHELEUARGPHELEUTHR
5   ILEPROPROTHRALAGLYILELEULYSARG
6   TRPGLYTHRILELYSLYSSERLYSALAILE
7   ASNVALLEUARGGLYPHEARGLYSGLUILE
8   GLYARGMETLEUASNILELEUASNARGARG
9   ARGARG

Samples:

sample_1: Dengue Virus capsid protein with the deletion of the intrinsically disordered N-terminal region, [U-100% 13C; U-100% 15N], 200 uM; D2O, [U-100% 2H], 10%; PMSF 2 mM; sodium azide 5 mM; EDTA 5 mM; sodium chloride 200 mM; sodium phosphate 55 mM; H2O 90%

sample_conditions_1: ionic strength: 0.25 M; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, data analysis

NMRDraw - data analysis, processing

CcpNMR - chemical shift assignment, data analysis, peak picking

TALOS-N - data analysis, geometry optimization

NMRbox - chemical shift assignment, collection, data analysis, geometry optimization, peak picking, processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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