BMRB Entry 52440

Title:
B19 VP1u receptor-binding domain (RBD)
Deposition date:
2024-05-02
Original release date:
2024-07-19
Authors:
Caldas Nogueira, Maria Luiza; Lakshmanan, Renuk; Riviere, Gwladys; Mietzsch, Mario; Bennett, Antonette; Mckenna, Robert; Long, Joanna
Citation:

Citation: Caldas Nogueira, Maria Luiza; Lakshmanan, Renuk; Riviere, Gwladys; Mietzsch, Mar; Bennett, Antonette; Mckenna, Robert; Long, Joanna. "Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19"  Biomol. NMR Assignments 18, 147-152 (2024).
PubMed: 38904726

Assembly members:

Assembly members:
entity_1, polymer, 98 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human parvovirus B19   Taxonomy ID: 10798   Superkingdom: Viruses   Kingdom: not available   Genus/species: Erythroparvovirus Erythroparvovirus primate1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts78
1H chemical shifts327

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VP1u receptor biding domain1

Entities:

Entity 1, VP1u receptor biding domain 98 residues - Formula weight is not available

1   METSERLYSGLUSERGLYLYSTRPTRPGLU
2   SERASPASPGLUPHEALALYSALAVALTYR
3   GLNGLNPHEVALGLUPHETYRGLULYSVAL
4   THRGLYTHRASPLEUGLULEUILEGLNILE
5   LEULYSASPHISTYRASNILESERLEUASP
6   ASNPROLEUGLUASNPROSERSERLEUPHE
7   ASPLEUVALALAARGILELYSASNASNLEU
8   LYSASNSERPROASPLEUTYRSERHISHIS
9   PHEGLNSERHISGLYGLNLEUSERASPHIS
10   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: VP1u receptor binding domain, [U-100% 13C; U-100% 15N], 450 uM; D2O 10%; sodium phosphate 20 mM; sodium chloride 50 mM; arginine 25 mM; Glutamic acid 25 mM; Trimethylsilylpropanoic acid 112 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR v3.2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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