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	<title>2022Terashi DAQ - Revision history</title>
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	<updated>2026-05-24T21:07:00Z</updated>
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		<id>https://3demmethods.i2pc.es/index.php?title=2022Terashi_DAQ&amp;diff=4319&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Terashi, Genki / Wang, Xiao / Maddhuri Venkata Subramaniya, Sai Raghavendra / Tesmer, John J. G. / Kihara, Daisuke  Residue-wise local quality estimation for p...&quot;</title>
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		<updated>2023-06-07T18:33:10Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Terashi, Genki / Wang, Xiao / Maddhuri Venkata Subramaniya, Sai Raghavendra / Tesmer, John J. G. / Kihara, Daisuke  Residue-wise local quality estimation for p...&amp;quot;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;== Citation ==&lt;br /&gt;
&lt;br /&gt;
Terashi, Genki / Wang, Xiao / Maddhuri Venkata Subramaniya, Sai Raghavendra / Tesmer, John J. G. / Kihara, Daisuke &lt;br /&gt;
Residue-wise local quality estimation for protein models from cryo-EM maps. 2022. Nature Methods, Vol. 19, No. 9, p. 1116-1125 &lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
An increasing number of protein structures are being determined by cryogenic electron microscopy (cryo-EM). Although the&lt;br /&gt;
resolution of determined cryo-EM density maps is improving in general, there are still many cases where amino acids of a protein&lt;br /&gt;
are assigned with different levels of confidence. Here we developed a method that identifies potential misassignment of&lt;br /&gt;
residues in the map, including residue shifts along an otherwise correct main-chain trace. The score, named DAQ, computes&lt;br /&gt;
the likelihood that the local density corresponds to different amino acids, atoms, and secondary structures, estimated via deep&lt;br /&gt;
learning, and assesses the consistency of the amino acid assignment in the protein structure model with that likelihood. When&lt;br /&gt;
DAQ was applied to different versions of model structures in the Protein Data Bank that were derived from the same density&lt;br /&gt;
maps, a clear improvement in the DAQ score was observed in the newer versions of the models. DAQ also found potential misassignment&lt;br /&gt;
errors in a substantial number of deposited protein structure models built into cryo-EM maps.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
https://www.nature.com/articles/s41592-022-01574-4&lt;br /&gt;
&lt;br /&gt;
== Related software ==&lt;br /&gt;
&lt;br /&gt;
== Related methods ==&lt;br /&gt;
&lt;br /&gt;
== Comments ==&lt;/div&gt;</summary>
		<author><name>WikiSysop</name></author>
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