Phase 6C.1 · Original deposited experimental coordinates
Comprehensive structure quality
Residue and heavy-atom completeness calculated directly from 230 source PDBx/mmCIF files, each verified against its frozen historical checksum. Each mapped PWWP chain/domain, NMR model and qualified source-supported ligand environment is tracked individually.
Experimental-coordinate case studies
Inspect actual examples
9FOC · NSD2 PWWP1
Newly assessed ligand-bearing structure
Protein and bound ligand coordinates are deposited, but the literature's assayed compound 11 preparation remains stereochemically unresolved. Structural components do not fix that ambiguity.
Inspect 9FOC completeness and ligands2M16 · PSIP1 PWWP
Deposited NMR ensemble
All model-specific atom observations are retained. Ensemble variation is not represented by a single first-model structure alone.
Inspect model coverage11OA · DNMT3A PWWP1
Independently confirmed side-chain gaps
Five observed-core chains each lack 198 standard side-chain heavy atoms; 13 other mapped chains contain no observed core coordinates.
Inspect exact missing atomsAnalyze family-wide experimental binding-site differences →
All 666 original chain/domain mappings
Search structural evidence
3 matching chain/domain records. Filters must be satisfied by the same experimental chain/domain. Model-specific assessment is available within each detail record.
| PDB · chain | Target/domain | Core observed | Experiment | Missing side-chain atoms | Backbone gaps | Research ligand environments | Assessment |
|---|---|---|---|---|---|---|---|
| 6IIQ · A | HDGFL3 PWWP1 | 58 / 58 | X-RAY DIFFRACTION · 1.85 Å | 0 | 0 | 0 | atomic completeness calculated |
| 6IIQ · B | HDGFL3 PWWP1 | 58 / 58 | X-RAY DIFFRACTION · 1.85 Å | 0 | 0 | 0 | atomic completeness calculated |
| 6IIQ · C | HDGFL3 PWWP1 | 58 / 58 | X-RAY DIFFRACTION · 1.85 Å | 0 | 0 | 0 | atomic completeness calculated |
Reproducible scientific exports
Individual experimental mmCIF files are verified by their original SHA-256. Core coordinates, standard heavy-atom templates and source UniProt mappings are analyzed model-by-model. Union-of-alternates and conformer-consistent completeness are distinct; 5 Å and 6 Å geometric proximity are not equivalent to a validated interaction.