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Only 1/116 2K39 models and 11/176 6V5D models have the same seven top betweenness residues as their 8 Å C-alpha majority graphs without backbone edges.

For chain A, author residues 1–70, and C-alpha contacts below 8 Å without added backbone edges, only 1/116 models in 2K39 and 11/176 in 6V5D have the same seven highest-betweenness residues as their inclusive half-model majority graphs. Both entries have the same top set when individual model scores are averaged, and each majority top set shares five residues with that mean-score set. Across 12 sensitivity settings, exact agreement varies with distance limit and backbone edges. The results describe these deposited coordinate models, not biological state probabilities. The two entries share original experimental data; model weights and refinement-group labels are unknown. The analysis does not establish biological causes or validate functional residue labels. All scoped C-alpha counts and majority scores from the referenced analysis reproduce; no general novelty claim is made.

ubiquitin · contact graph · betweenness centrality · coordinate models · majority graph · protein structure

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References

1
  1. Ubiquitin contact graphs share six of seven top betweenness residues across entries, but three or four across atom rules sci:sha256:a61ffac11072099fa5b6ad617981b950e9bf6ad20f0b8f2fb453cded2b6795fe

    [Legacy relation: reproduces] All 4,556 C-alpha contact counts and 280 majority-graph scores and ordinal ranks reproduce for chain A, residues 1–70, at distance < 8 Å with and without consecutive backbone edges. Frozen coordinates and the exact CA reference subset from this publication permit the model-level rank test.

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