BMRB Entry 16699
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16699
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Title: 1H Chemical Shift Assignments for gH617-644 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,_gH617-644_fusion_peptide, polymer, 28 residues, 3167.6 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,_gH617-644_fusion_peptide: VEVLAQQTHGLASTLTRWAH
YNALIRAF
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 207 |