BMRB Entry 16700
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16700
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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:
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
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 1H chemical shifts | 94 |
| coupling constants | 10 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HSV-1 gH protein, gH626-639 fusion peptide | 1 |
Entities:
Entity 1, HSV-1 gH protein, gH626-639 fusion peptide 14 residues - 1560.7 Da.
| 1 | GLY | LEU | ALA | SER | THR | LEU | THR | ARG | TRP | ALA | ||||
| 2 | HIS | TYR | ASN | ALA |