BMRB Entry 16700

Title:
1H Chemical Shift Assignments for gH626-639 fusion peptide from HSV-1 gH protein
Deposition date:
2010-02-01
Original release date:
2010-05-05
Authors:
Russo, Luigi; Isernia, Carla; Galdiero, Stefania; Falanga, Annarita; Vitiello, Mariateresa; Raiola, Luca; Pedone, Carlo; Galdiero, Massimiliano
Citation:

Citation: Galdiero, Stefania; Falanga, Annarita; Vitiello, Mariateresa; Raiola, Luca; Russo, Luigi; Pedone, Carlo; Isernia, Carla; Galdiero, Massimiliano. "The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H."  J. Biol. Chem. 285, 17123-17136 (2010).
PubMed: 20348105

Assembly members:

Assembly members:
HSV-1_gH_protein,_gH626-639_fusion_peptide, polymer, 14 residues, 1560.7 Da.

Natural source:

Natural source:   Common Name: Human herpesvirus 1   Taxonomy ID: 10298   Superkingdom: Viruses   Kingdom: not available   Genus/species: Simplexvirus Human herpesvirus 1

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSV-1_gH_protein,_gH626-639_fusion_peptide: GLASTLTRWAHYNA

Data sets:
Data typeCount
1H chemical shifts94
coupling constants10

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HSV-1 gH protein, gH626-639 fusion peptide1

Entities:

Entity 1, HSV-1 gH protein, gH626-639 fusion peptide 14 residues - 1560.7 Da.

1   GLYLEUALASERTHRLEUTHRARGTRPALA
2   HISTYRASNALA

Samples:

sample_gH626-639: HSV-1 gH protein, gH626-639 fusion peptide 1 mM; TFE, [U-99% 2H], 80 % v/v; H2O 20 % v/v

sample_condition_gH626-639: pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_gH626-639isotropicsample_condition_gH626-639
2D 1H-1H NOESYsample_gH626-639isotropicsample_condition_gH626-639
2D DQF-COSYsample_gH626-639isotropicsample_condition_gH626-639

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Varian Unity 500 MHz