OrganismNot specified
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | No other associated polymer | Consistent with protein count |
| UniProt name | Q73369_9HIV1 |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–96； UniProt 1–96 |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
| Entry ID entry_id | 1esx |
| Deposition date deposition_date | 2000-04-11 |
| Structure title title | 1H, 15N AND 13C STRUCTURE OF THE HIV-1 REGULATORY PROTEIN VPR : COMPARISON WITH THE N-AND C-TERMINAL DOMAIN STRUCTURE, (1-51)VPR AND (52-96)VPR |
| Keywords keywords | helix, amphipatic, turn, Viral protein; VIRAL PROTEIN |
| Experimental Method method | SOLUTION NMR |
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 26.32 Å |
| Rg (electron density) | 25.29 Å |
| Total Rg | 26.17 Å |
| Atom count | 1608 |
| Residues | 96 |
| Excluded volume | 14162 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1esxa_ |
| Class class | j — Peptides |
| Fold Fold fold | j.11 — VPR protein fragments |
| Superfamily Superfamily superfamily | j.11.1 — VPR protein fragments |
| Family Family family | j.11.1.1 — VPR protein fragments |
| Domain ID domain_id | 1esxA01 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 20 — Up-down Bundle |
| Topology topology | 5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
| Homologous superfamily homologous superfamily | 4730 — |