5wot: Difference between revisions
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==NMR solution structure of a-lytic protease using two 4D-spectra== | |||
<StructureSection load='5wot' size='340' side='right'caption='[[5wot]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5wot]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WOT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wot OCA], [https://pdbe.org/5wot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wot RCSB], [https://www.ebi.ac.uk/pdbsum/5wot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wot ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days. | |||
Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.,Evangelidis T, Nerli S, Novacek J, Brereton AE, Karplus PA, Dotas RR, Venditti V, Sgourakis NG, Tripsianes K Nat Commun. 2018 Jan 26;9(1):384. doi: 10.1038/s41467-017-02592-z. PMID:29374165<ref>PMID:29374165</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5wot" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lysobacter enzymogenes]] | |||
[[Category: Evangelidis T]] | |||
[[Category: Nerli S]] | |||
[[Category: Sgourakis NG]] | |||
[[Category: Tripsianes K]] | |||
Latest revision as of 09:34, 23 October 2024
NMR solution structure of a-lytic protease using two 4D-spectra
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