5wox: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5wox is ~~ON HOLD until Paper~~ Publication

==NMR solution structure of KanY protein (ms6282) using two 4D-spectra==

== Structural highlights ==

<table><tr><td colspan='2'>[[5wox]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WOX FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wox OCA], [http://pdbe.org/5wox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wox RCSB], [http://www.ebi.ac.uk/pdbsum/5wox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wox ProSAT]</span></td></tr>

</table>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Evangelidis, T]]

[[Category: Nerli, S]]

[[Category: Sgourakis, N G]]

[[Category: Tripsianes, K]]

[[Category: Predicted polyketide cyclase/dehydratase]]

[[Category: Unknown function]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5wox is ON HOLD  until Paper Publication
+==NMR solution structure of KanY protein (ms6282) using two 4D-spectra==
+<StructureSection load='5wox' size='340' side='right' caption='[[5wox]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5wox]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WOX FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wox OCA], [http://pdbe.org/5wox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wox RCSB], [http://www.ebi.ac.uk/pdbsum/5wox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wox ProSAT]</span></td></tr>
+</table>
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5wox" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Evangelidis, T]]
+[[Category: Nerli, S]]
+[[Category: Sgourakis, N G]]
+[[Category: Tripsianes, K]]
+[[Category: Predicted polyketide cyclase/dehydratase]]
+[[Category: Unknown function]]