Improved model quality assessment using sequence and structural information by enhanced deep neural networks

Protein model quality assessment plays an important role in protein structure prediction, protein design and drug discovery. In this work, DeepUMQA2, a substantially improved version of DeepUMQA for protein model quality assessment, is proposed. First, sequence features containing protein co -evolution information and structural features reflecting family information are extracted to complement model -dependent features. Second, a novel backbone network based on triangular multiplication update and axial attention mechanism is designed to enhance information exchange between inter-residue pairs. On CASP13 and CASP14 datasets, the performance of DeepUMQA2 increases by 20.5 and 20.4% compared with DeepUMQA, respectively (measured by top 1 loss). Moreover, on the three-month CAMEO dataset (11 March to 04 June 2022), DeepUMQA2 outperforms DeepUMQA by 15.5% (measured by local AUC0,0.2) and ranks first among all competing server methods in CAMEO blind test. Experimental results show that DeepUMQA2 outperforms state-of-the-art model quality assessment methods, such as ProQ3D-LDDT, ModFOLD8, and DeepAccNet and DeepUMQA2 can select more suitable best models than state-of-the-art protein structure methods, such as AlphaFold2, RoseTTAFold and I-TASSER, provided themselves.

Automated summary

In this study, an improved protein model quality assessment method, DeepUMQA2, is proposed, which plays a crucial role in protein structure prediction, protein design, and drug discovery. The method extracts sequence features with protein co-evolution information and structural features reflecting family information to complement model-dependent features. A novel backbone network based on triangular multiplication update and axial attention mechanism is designed to enhance information exchange between inter-residue pairs. Experimental results demonstrate that DeepUMQA2 outperforms state-of-the-art model quality assessment methods and can select more suitable best models than state-of-the-art protein structure methods.