We report docking performance on the six targets of Critical Assessment of PRedicted Interactions (CAPRI) rounds 39‐45 that involved heteromeric protein‐protein interactions and had the solved structures released since the rounds were held. Our general strategy involved protein‐protein docking using ZDOCK, reranking using IRAD, and structural refinement using Rosetta. In addition, we made extensive use of experimental data to guide our docking runs. All the experimental information at the amino‐acid level proved correct. However, for two targets, we also used protein‐complex structures as templates for modeling interfaces. These resulted in incorrect predictions, presumably due to the low sequence identity between the targets and templates. Albeit a small number of targets, the performance described here compared somewhat less favorably with our previous CAPRI reports, which may be due to the CAPRI targets being increasingly challenging.

中文翻译：

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ZDOCK 和 IRAD 在 CAPRI 第 39-45 轮中的表现。

我们报告了预测相互作用关键评估 (CAPRI) 第 39-45 轮的六个目标的对接性能，这些目标涉及异聚体蛋白质-蛋白质相互作用，并且自这些轮次举行以来已释放已解决的结构。我们的总体策略包括使用 ZDOCK 进行蛋白质-蛋白质对接、使用 IRAD 重新排序以及使用 Rosetta 进行结构细化。此外，我们广泛使用实验数据来指导我们的对接运行。氨基酸水平的所有实验信息都证明是正确的。然而，对于两个目标，我们还使用蛋白质复合结构作为界面建模的模板。这些导致了错误的预测，大概是由于目标和模板之间的低序列同一性。目标虽然少，