BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27972

Title: VSV Phosphoprotein 35-106   PubMed: 31896592

Deposition date: 2019-07-12 Original release date: 2020-02-11

Authors: Petit, Chad; Green, Todd

Citation: Gould, Joseph; Qiu, Shihong; Shang, Qiao; Ogino, Tomoaki; Prevelige, Peter; Petit, Chad; Green, Todd. "The Connector Domain of Vesicular Stomatitis Virus Large Protein Interacts with the Viral Phosphoprotein"  J. Virol. 94, e01729-19-e01729-19 (2020).

Assembly members:
L_Protein, polymer, 72 residues, Formula weight is not available

Natural source:   Common Name: Vesicular Stomatitis Virus   Taxonomy ID: 11276   Superkingdom: Viruses   Kingdom: not available   Genus/species: Vesiculovirus Vesicular Stomatitis Virus

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

Entity Sequences (FASTA):
L_Protein: SNYELFQEDGVEEHTRPSYF QAADDSDTESEPEIEDNQGL YVPDPEAEQVEGFIQGPLDD YADEDVDVVFTS

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts60
1H chemical shifts60

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1VSV Phosphoprotein 35-1061

Entities:

Entity 1, VSV Phosphoprotein 35-106 72 residues - Formula weight is not available

1   SERASNTYRGLULEUPHEGLNGLUASPGLY
2   VALGLUGLUHISTHRARGPROSERTYRPHE
3   GLNALAALAASPASPSERASPTHRGLUSER
4   GLUPROGLUILEGLUASPASNGLNGLYLEU
5   TYRVALPROASPPROGLUALAGLUGLNVAL
6   GLUGLYPHEILEGLNGLYPROLEUASPASP
7   TYRALAASPGLUASPVALASPVALVALPHE
8   THRSER

Samples:

sample_1: VSV Phosphoprotein 35-106, [U-13C; U-15N], 1 mM; HEPES 20 mM; Sodium Chloride 150 mM; glycerol 10%; TCEP 1 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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