BMRB Entry 34239
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34239
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: Gp36-MPER PubMed: 30240422
Deposition date: 2018-02-22 Original release date: 2019-03-14
Authors: D'Ursi, Anna Maria; Grimaldi, M.
Citation: Grimaldi, Manuela; Stillitano, Ilaria; Amodio, Giuseppina; Santoro, Angelo; Buonocore, Michela; Moltedo, Ornella; Remondelli, Paolo; D'Ursi, Anna Maria. "Structural basis of antiviral activity of peptides from MPER of FIV gp36" PLoS ONE 13, e0204042-e0204042 (2018).
Assembly members:
entity_1, polymer, 50 residues, 6126.001 Da.
Natural source: Common Name: isolate Petaluma Taxonomy ID: 11673 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus FIV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-31b(+)
Entity Sequences (FASTA):
entity_1: LQTKDLQQKFYEIILDIEQN
NVQGKTGIQQLQKWEDWVRW
IGNIPQYLKM
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 71 |
| 15N chemical shifts | 48 |
| 1H chemical shifts | 262 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 50 residues - 6126.001 Da.
| 1 | LEU | GLN | THR | LYS | ASP | LEU | GLN | GLN | LYS | PHE | |
| 2 | TYR | GLU | ILE | ILE | LEU | ASP | ILE | GLU | GLN | ASN | |
| 3 | ASN | VAL | GLN | GLY | LYS | THR | GLY | ILE | GLN | GLN | |
| 4 | LEU | GLN | LYS | TRP | GLU | ASP | TRP | VAL | ARG | TRP | |
| 5 | ILE | GLY | ASN | ILE | PRO | GLN | TYR | LEU | LYS | MET |
Samples:
sample_1: entity_1 mM; glucose, [U-95% 13C], 2 g/L; ammonium sulfate, [U-98% 15N], 1 g/L
sample_conditions_1: ionic strength: 0.15 Not defined; pH: 7.4; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY 13C-HSQC | sample_1 | isotropic | sample_conditions_1 |
| NOESY 15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3, Goddard - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
TALOS+, Cornilescu, Delaglio and Bax - refinement
NMR spectrometers:
- Bruker AvanceIII 900 MHz
- Bruker AvanceIII 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts