BMRB Entry 34809

Name: Why does the herpes simplex 1 virus-encoded UL49.5 protein fail to inhibit the TAP-dependent antigen presentation?
Published: 2024-04-23

Click here to enlarge.

PDB ID: 8osq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34809
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Why does the herpes simplex 1 virus-encoded UL49.5 protein fail to inhibit the TAP-dependent antigen presentation?

Deposition date:

2023-04-19

Original release date:

2024-04-23

Authors:

Zhukov, I.; Krupa, P.; Karska, N.; Rodziewicz-Motowidlo, S.; Lipinska, A.

Citation:

Citation: Karska, N.; Zhukov, I.; Lipinska, A.; Rodziewicz-Motowidlo, S.; Krupa, P.. "Why does the herpes simplex 1 virus-encoded UL49.5 protein fail to inhibit the TAP-dependent antigen presentation?" Biochim. Biophys. Acta Biomembr. 1865, 184200-184200 (2023).
PubMed: 37517559

Assembly members:

Assembly members:
entity_1, polymer, 35 residues, 3379.504 Da.

Natural source:

Natural source: Common Name: Herpes simplex virus type 1 Taxonomy ID: 10298 Superkingdom: Viruses Kingdom: not available Genus/species: Simplexvirus HSV-1

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DAGPRGEPPGEEGGRDGIGG ARXETQNTGQXSAPG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 35 residues - 3379.504 Da.

1

ASP

ALA

GLY

PRO

ARG

GLY

GLU

PRO

GLY

2

GLU

GLY

ARG

ASP

GLY

ILE

GLY

3

ALA

ARG

ABA

GLU

THR

GLN

ASN

THR

GLY

GLN

4

NLE

SER

ALA

PRO

GLY

Samples:

sample_1: NHSV 0.4 ± 0.1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 bar; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H ROESY	sample_1	isotropic	sample_conditions_1

Software:

VnmrJ v4.3, Agilent Inc. - collection

TopSpin v3.5, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - data analysis

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure calculation

NMR spectrometers:

Varian INOVA 500 MHz
Bruker AVANCE 700 MHz