BMRB Entry 5967
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5967
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
Citation: Ishima, R.; Torchia, D.; Lynch, S.; Gronenborn, A.; Louis, J.. "Solution structure of the mature HIV-1 protease monomer: Insight into the
tertiary fold and stability of a precursor " J. Biol. Chem. 278, 43311-43319 (2003).
PubMed: 12933791
Assembly members:
HIV-1 protease (E.C.3.4.23.16), 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: chemical synthesis
Entity Sequences (FASTA):
HIV-1 protease (E.C.3.4.23.16): PQITLWKRPLVTIKIGGQLK
EALLDTGADDTVIEEMSLPG
RWKPKMIGGIGGFIKVRQYD
QIIIEIAGHKAIGTVLVGPT
PVNIIGRNLLTQIGA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 89 |
| 13C chemical shifts | 175 |
| 15N chemical shifts | 89 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HIV-1 protease | 1 |
Entities:
Entity 1, HIV-1 protease 95 residues - Formula weight is not available
| 1 | PRO | GLN | ILE | THR | LEU | TRP | LYS | ARG | PRO | LEU | ||||
| 2 | VAL | THR | ILE | LYS | ILE | GLY | GLY | GLN | LEU | LYS | ||||
| 3 | GLU | ALA | LEU | LEU | ASP | THR | GLY | ALA | ASP | ASP | ||||
| 4 | THR | VAL | ILE | GLU | GLU | MET | SER | LEU | PRO | GLY | ||||
| 5 | ARG | TRP | LYS | PRO | LYS | MET | ILE | GLY | GLY | ILE | ||||
| 6 | GLY | GLY | PHE | ILE | LYS | VAL | ARG | GLN | TYR | ASP | ||||
| 7 | GLN | ILE | ILE | ILE | 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: HIV-1 protease (E.C.3.4.23.16), [U-13C; U-15N], 0.5 mM; phosphate buffer 20 mM; D2O 5%; H2O 95%
sample_cond_1: pH: 5.8 na; temperature: 293 K; ionic strength: 20 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | not available | not available | not available |
| 3D 15N-separated NOESY | not available | not available | not available |
Software:
XWINNMR v2.6 - collection
NMRPipe - data analysis
X-PLOR v1.0.6 - structure solution, refinement
NMR spectrometers:
- Bruker DMX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks