BMRB Entry 34409
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/BMR34409
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: Structure of HIV-1 CAcSP1NC mutant(W41A,M42A) interacting with maturation inhibitor EP39 PubMed: 32717487
Deposition date: 2019-06-05 Original release date: 2020-05-15
Authors: Chen, X.; Coric, P.; Larue, V.; Nonin-Lecomte, S.; Bouaziz, S.; Structural Genomics Consortium (SGC), SGC
Citation: Chen, Xiaowei; Coric, Pascale; Larue, Valery; Turcaud, Serge; Wang, Xiao; Nonin-Lecomte, Sylvie; Bouaziz, Serge. "Structure of HIV-1 CAcSP1NC mutant(W41A,M42A) interacting with maturation inhibitor EP39" Eur. J. Med. Chem. 204, 112634-112634 (2020).
Assembly members:
entity_1, polymer, 157 residues, 17446.146 Da.
entity_ZN, non-polymer, 65.409 Da.
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
Entity Sequences (FASTA):
entity_1: MYSPTSILDIRQGPKEPFRD
YVDRFYKTLRAEQASQEVKN
AATETLLVQNANPDCKTILK
ALGPGATLEEMMTACQGVGG
PGHKARVLAEAMSQVTNPAT
IMIQKGNFRNQRKTVKCFNC
GKEGHIAKNCRAPRKKGCWK
CGKEGHQMKDCTERQAN
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 921 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2, 1 | 2 |
| 3 | entity_2, 2 | 2 |
Entities:
Entity 1, entity_1 157 residues - 17446.146 Da.
| 1 | MET | TYR | SER | PRO | THR | SER | ILE | LEU | ASP | ILE | ||||
| 2 | ARG | GLN | GLY | PRO | LYS | GLU | PRO | PHE | ARG | ASP | ||||
| 3 | TYR | VAL | ASP | ARG | PHE | TYR | LYS | THR | LEU | ARG | ||||
| 4 | ALA | GLU | GLN | ALA | SER | GLN | GLU | VAL | LYS | ASN | ||||
| 5 | ALA | ALA | THR | GLU | THR | LEU | LEU | VAL | GLN | ASN | ||||
| 6 | ALA | ASN | PRO | ASP | CYS | LYS | THR | ILE | LEU | LYS | ||||
| 7 | ALA | LEU | GLY | PRO | GLY | ALA | THR | LEU | GLU | GLU | ||||
| 8 | MET | MET | THR | ALA | CYS | GLN | GLY | VAL | GLY | GLY | ||||
| 9 | PRO | GLY | HIS | LYS | ALA | ARG | VAL | LEU | ALA | GLU | ||||
| 10 | ALA | MET | SER | GLN | VAL | THR | ASN | PRO | ALA | THR | ||||
| 11 | ILE | MET | ILE | GLN | LYS | GLY | ASN | PHE | ARG | ASN | ||||
| 12 | GLN | ARG | LYS | THR | VAL | LYS | CYS | PHE | ASN | CYS | ||||
| 13 | GLY | LYS | GLU | GLY | HIS | ILE | ALA | LYS | ASN | CYS | ||||
| 14 | ARG | ALA | PRO | ARG | LYS | LYS | GLY | CYS | TRP | LYS | ||||
| 15 | CYS | GLY | LYS | GLU | GLY | HIS | GLN | MET | LYS | ASP | ||||
| 16 | CYS | THR | GLU | ARG | GLN | ALA | ASN |
Entity 2, entity_2, 1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: HIV-1 CAcSP1NC, [U-15N], 300 uM
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.5 pl 7, Bruker Biospin - processing
CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment
ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation
TALOS, Cornilescu, Delaglio and Bax - data analysis
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- 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