Homo sapiens
| 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 | A4_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–28； UniProt 672–699 |
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 | 1amb |
| Deposition date deposition_date | 1994-10-21 |
| Structure title title | SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE |
| Keywords keywords | PROTEINASE INHIBITOR(TRYPSIN); PROTEINASE INHIBITOR(TRYPSIN) |
| 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） | 12.89 Å |
| Rg (electron density) | 12.25 Å |
| Total Rg | 13.19 Å |
| Atom count | 438 |
| Residues | 28 |
| Excluded volume | 3971 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1amba_ |
| Class class | j — Peptides |
| Fold Fold fold | j.42 — Amyloid peptides |
| Superfamily Superfamily superfamily | j.42.1 — Amyloid peptides |
| Family Family family | j.42.1.1 — Amyloid peptides |