Streptomyces tendae
| 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 | IAA_STRTE |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–74； UniProt 31–104 |
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 | 3ait |
| Deposition date deposition_date | 1990-05-14 |
| Structure title title | RESTRAINED ENERGY REFINEMENT WITH TWO DIFFERENT ALGORITHMS AND FORCE FIELDS OF THE STRUCTURE OF THE ALPHA-AMYLASE INHIBITOR TENDAMISTAT DETERMINED BY NMR IN SOLUTION |
| Keywords keywords | ALPHA-AMYLASE INHIBITOR; ALPHA-AMYLASE INHIBITOR |
| 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） | 12.98 Å |
| Rg (electron density) | 11.81 Å |
| Total Rg | 13.06 Å |
| Atom count | 1076 |
| Residues | 74 |
| Excluded volume | 9741 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d3aita_ |
| Class class | b — All beta proteins |
| Fold Fold fold | b.5 — alpha-Amylase inhibitor tendamistat |
| Superfamily Superfamily superfamily | b.5.1 — alpha-Amylase inhibitor tendamistat |
| Family Family family | b.5.1.1 — alpha-Amylase inhibitor tendamistat |
| Domain ID domain_id | 3aitA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 60 — Sandwich |
| Topology topology | 40 — Immunoglobulin-like |
| Homologous superfamily homologous superfamily | 20 — Alpha-amylase inhibitor |