BMRB Entry 27728

Title:
Structure determination of N-terminal fragment of UL49.5 protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics
Deposition date:
2018-12-14
Original release date:
2019-02-25
Authors:
Karska, Natalia; Graul, Malgorzata; Sikorska, Emilia; Zhukov, Igor; Slusarz, Magdalena; Kasprzykowski, Franciszek; Lipinska, Andrea; Rodziewicz-Motowidlo, Sylwia
Citation:

Citation: Karska, Natalia; Graul, Malgorzata; Sikorska, Emilia; Zhukov, Igor; Slusarz, Magdalena; Kasprzykowski, Franciszek; Lipinska, Andrea; Rodziewicz-Motowidlo, Sylwia. "Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics."  Biochim. Biophys. Acta Biomembr. 1861, 926-938 (2019).
PubMed: 30772281

Assembly members:

Assembly members:
N.BHV, polymer, 35 residues, 3819 Da.

Natural source:

Natural source:   Common Name: BHV-1   Taxonomy ID: 10320   Superkingdom: Viruses   Kingdom: not available   Genus/species: Varicellovirus BHV-1

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N.BHV: RDPLLDAXRREGAXDFWSAG XYARGVPLSEPPQAL

Data sets:
Data typeCount
1H chemical shifts218

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N.BHV1

Entities:

Entity 1, N.BHV 35 residues - 3819 Da.

This is the N-terminal domain of a transmembrane protein

1   ARGASPPROLEULEUASPALANLEARGARG
2   GLUGLYALANLEASPPHETRPSERALAGLY
3   ABATYRALAARGGLYVALPROLEUSERGLU
4   PROPROGLNALALEU

Samples:

sample_1: N.BHV 4.8 mM; DPC 100 mM; Acetic Acid-d4 0.02 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1

Software:

SPARKY v3, Goddard - chemical shift assignment, chemical shift calculation, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution

AMBER v15, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Agilent Uniform NMR System 800 MHz