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Sequence assignment for low‐resolution modelling of protein crystal structures
Author(s) -
Chojnowski Grzegorz,
Pereira Joana,
Lamzin Victor S.
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319009392
Subject(s) - computer science , sequence (biology) , fragmentation (computing) , low resolution , docking (animal) , resolution (logic) , algorithm , artificial intelligence , high resolution , chemistry , programming language , geography , remote sensing , medicine , biochemistry , nursing
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 .