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 19003

Title: Solution structure of the Core Domain (10-76) of the Feline Calicivirus VPg protein.   PubMed: 23487472

Authors: Kwok, Rex; Leen, Eoin; Birtley, James; Prater, Sean; Simpson, Pete; Curry, Stephen; Matthews, Steve; Marchant, Jan

Citation: Leen, Eoin; Kwok, K. Y Rex; Birtley, James; Simpson, Peter; Subba-Reddy, Chennareddy; Chaudhry, Yasmin; Sosnovtsev, Stanislav; Green, Kim; Prater, Sean; Tong, Michael; Young, Joanna; Chung, Liliane; Marchant, Jan; Roberts, Lisa; Kao, C. Cheng; Matthews, Stephen; Goodfellow, Ian; Curry, Stephen. "Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins."  J. Virol. 87, 5318-5330 (2013).

Assembly members:
FCV_VPg, polymer, 71 residues, 7906.722 Da.

Natural source:   Common Name: Feline calicivirus   Taxonomy ID: 11978   Superkingdom: Viruses   Kingdom: not available   Genus/species: Feline calicivirus

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts307
15N chemical shifts81
1H chemical shifts465

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID


Entity 1, FCV_VPg_9-76 71 residues - 7906.722 Da.

8   VAL


sample_1: FCV VPg 7-76, [U-99% 13C; U-99% 15N], 100 – 200 uM; sodium chloride 300 mM; HEPES pH7 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_2: FCV VPg 7-76, [U-99% 13C; U-99% 15N], 100 – 200 uM; sodium chloride 300 mM; sodium azide 1 mM; HEPES pH7 20 mM; D2O 100%

sample_3: FCV VPg 7-76, [U-99% 13C; U-99% 15N], 100 – 200 uM; sodium chloride 300 mM; sodium azide 1 mM; HEPES pH7 20 mM; Pf1 phage 15 mg/mL; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 283 K

sample_conditions_2: ionic strength: 300 mM; pH: 7; pressure: 1 bar; temperature: 283 K

sample_conditions_3: ionic strength: 300 mM; pH: 7; pressure: 1 Pa; temperature: 280 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_3anisotropicsample_conditions_3
3D HN(CA)COsample_1isotropicsample_conditions_1


TALOS, Cornilescu, Delaglio and Bax - geometry optimization

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

MARS, Zweckstetter et al., 2004 - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 800 MHz

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