Bacillus amyloliquefaciens
| 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 | BARS_BACAM |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–89； UniProt 1–89 |
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 | 1bta |
| Deposition date deposition_date | 1994-05-09 |
| Structure title title | THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY |
| Keywords keywords | RIBONUCLEASE INHIBITOR; RIBONUCLEASE 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） | 13.69 Å |
| Rg (electron density) | 11.84 Å |
| Total Rg | 13.31 Å |
| Atom count | 1434 |
| Residues | 89 |
| Excluded volume | 12854 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d1btaa_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.9 — Barstar-like |
| Superfamily Superfamily superfamily | c.9.1 — Barstar-related |
| Family Family family | c.9.1.1 — Barstar-related |
| Domain ID domain_id | 1btaA00 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 370 — Barnase; Chain D |
| Homologous superfamily homologous superfamily | 10 — Barstar-like |