BMRB Entry 26987
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26987
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Title: HIV1 protease folded and cold-denatured PubMed: 28168877
Deposition date: 2017-01-03 Original release date: 2021-07-22
Authors: Roesner, Heike; Kragelund, Birthe; Prestel, Andreas; Caldarini, Martina; Tiana, Guido; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro
Citation: Roesner, Heike; Caldarini, Martina; Prestel, Andreas; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro; Tiana, Guido; Kragelund, Birthe. "Cold denaturation of the HIV-1 protease monomer" Biochemistry 56, 1029-1032 (2017).
Assembly members:
HIV1_protease_monomer, polymer, 95 residues, Formula weight is not available
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a
Entity Sequences (FASTA):
HIV1_protease_monomer: PQITLWKRPLVTIRIGGQLK
EALLNTGADDTVLEEMNLPG
KWKPKMIGGIGGFIKVRQYD
QIPVEIAGHKAIGTVLVGPT
PVNIIGRNLLTQIGA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 259 |
| 15N chemical shifts | 158 |
| 1H chemical shifts | 158 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HIV1 protease monomer, folded | 1 |
| 2 | HIV1 protease monomer, unfolded | 1 |
Entities:
Entity 1, HIV1 protease monomer, folded 95 residues - Formula weight is not available
| 1 | PRO | GLN | ILE | THR | LEU | TRP | LYS | ARG | PRO | LEU | ||||
| 2 | VAL | THR | ILE | ARG | ILE | GLY | GLY | GLN | LEU | LYS | ||||
| 3 | GLU | ALA | LEU | LEU | ASN | THR | GLY | ALA | ASP | ASP | ||||
| 4 | THR | VAL | LEU | GLU | GLU | MET | ASN | LEU | PRO | GLY | ||||
| 5 | LYS | TRP | LYS | PRO | LYS | MET | ILE | GLY | GLY | ILE | ||||
| 6 | GLY | GLY | PHE | ILE | LYS | VAL | ARG | GLN | TYR | ASP | ||||
| 7 | GLN | ILE | PRO | VAL | GLU | ILE | ALA | GLY | HIS | LYS | ||||
| 8 | ALA | ILE | GLY | THR | VAL | LEU | VAL | GLY | PRO | THR | ||||
| 9 | PRO | VAL | ASN | ILE | ILE | GLY | ARG | ASN | LEU | LEU | ||||
| 10 | THR | GLN | ILE | GLY | ALA |
Samples:
sample_1: HIV1 protease monomer, [U-13C; U-15N], 200 uM; sodium phosphate 20 mM; DSS 125 uM
sample_2: HIV1 protease monomer, [U-13C; U-15N], 200 uM; sodium phosphate 20 mM; DSS 125 uM
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K
sample_conditions_2: pH: 6; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRDraw, CCPN - chemical shift assignment
NMR spectrometers:
- Agilent Avance 800 MHz
- Varian INOVA 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts