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 16700

Title: 1H Chemical Shift Assignments for gH626-639 fusion peptide from HSV-1 gH protein   PubMed: 20348105

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: 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).

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

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

Experimental source:   Production method: chemical synthesis

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


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



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


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


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