BMRB Entry 16700

Name: 1H Chemical Shift Assignments for gH626-639 fusion peptide from HSV-1 gH protein
Published: 2010-05-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16700

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- Assigned_chem_shift_gH626-639
coupling_constants
- coupling_constant_gH626-639

Data type	Count
1H chemical shifts	94
coupling constants	10

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_gH626-639	isotropic	sample_condition_gH626-639
2D 1H-1H NOESY	sample_gH626-639	isotropic	sample_condition_gH626-639
2D DQF-COSY	sample_gH626-639	isotropic	sample_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