Sequence assignment for low-resolution modelling of protein crystal structures.
The performance of automated model building in crystal structure determination usually decreases with the resolution of the experimental data, and may result in fragmented models and incorrect side-chain assignment. Presented here are new methods for machine-learning-based docking of main-chain fragments to the sequence and for their sequence-independent connection using a dedicated library of protein fragments. The combined use of these new methods noticeably increases sequence coverage and reduces fragmentation of the protein models automatically built with ARP/wARP.
['Chojnowski|Grzegorz|G|', 'Pereira|Joana|J|0000-0002-5588-6588', 'Lamzin|Victor S|VS|']
D000465:Algorithms D000595:Amino Acid Sequence D018360:Crystallography, X-Ray D030562:Databases, Protein D066264:Datasets as Topic D000069550:Machine Learning D062105:Molecular Docking Simulation D011487:Protein Conformation D011506:Proteins D012984:Software
sequence assignment low-resolution modelling model building ARP/wARP loop building macromolecular crystallography