View source for 5wot


==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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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]]