2n0t: Difference between revisions

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 ==Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution==
-<StructureSection load='2n0t' size='340' side='right'caption='[[2n0t]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
+<StructureSection load='2n0t' size='340' side='right'caption='[[2n0t]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0T FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mzu|2mzu]]</div></td></tr>
+</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=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [https://pdbe.org/2n0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [https://www.ebi.ac.uk/pdbsum/2n0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0t ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [https://pdbe.org/2n0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [https://www.ebi.ac.uk/pdbsum/2n0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0t ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Bibow S]]
-[[Category: Bibow, S]]
+[[Category: Chi CN]]
-[[Category: Chi, C N]]
+[[Category: Guntert P]]
-[[Category: Guntert, P]]
+[[Category: Orts J]]
-[[Category: Orts, J]]
+[[Category: Riek R]]
-[[Category: Riek, R]]
+[[Category: Strotz D]]
-[[Category: Strotz, D]]
+[[Category: Voegeli B]]
-[[Category: Voegeli, B]]
-[[Category: Isomerase]]