BMRB Entry 34809
Click here to enlarge.
PDB ID:
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
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: Karska, N.; Zhukov, I.; Lipinska, A.; Rodziewicz-Motowidlo, S.; Krupa, P.. "Why doesn't the UL49.5 protein from HSV-1 virus inhibit the TAP antigen presentation pathway?" .
Assembly members:
entity_1, polymer, 35 residues, 3379.504 Da.
Natural source: Common Name: Herpes simplex virus type 1 Taxonomy ID: 10298 Superkingdom: Viruses Kingdom: not available Genus/species: Simplexvirus HSV-1
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: DAGPRGEPPGEEGGRDGIGG
ARXETQNTGQXSAPG
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 164 |
Additional metadata:
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 | PRO | GLY | ||||
| 2 | GLU | GLU | GLY | GLY | ARG | ASP | GLY | ILE | GLY | 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