1tec: Difference between revisions

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 <StructureSection load='1tec' size='340' side='right'caption='[[1tec]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43649 Atcc 43649] and [https://en.wikipedia.org/wiki/Hirme Hirme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tec OCA], [https://pdbe.org/1tec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tec RCSB], [https://www.ebi.ac.uk/pdbsum/1tec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tec ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
+[https://www.uniprot.org/uniprot/THET_THEVU THET_THEVU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tec ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In order to investigate the principles of protein thermostability, the crystal structure of thermitase from Thermoactinomyces vulgaris, a thermostable member of the subtilisin family of serine proteases, has been determined in a complex with eglin c. Eglin c is a serine protease inhibitor from the leech Hirudo medicinalis. After data collection with a television area-detector diffractometer and initial structure solution by molecular-replacement methods, crystallographic refinement proceeded with incorporation of molecular-dynamics techniques. It appeared that this refinement procedure has a large convergence radius with movements of more than 5 A for many atoms. Two procedures for the crystallographic molecular-dynamics refinement have been tested. They differed mainly in time span and weight on the X-ray 'energy'. The best results were obtained with a procedure which allowed the molecular-dynamics technique to search a large area in conformational space by having less weight on the X-ray restraints and allowing more time. The use of molecular-dynamics refinement considerably simplified the laborious and difficult task of fitting the model in its electron density during the refinement process. The final crystallographic R factor is 17.9% at 2.2 A resolution.
-Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c.,Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG Acta Crystallogr B. 1989 Oct 1;45 ( Pt 5):488-99. PMID:2688688<ref>PMID:2688688</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1tec" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Eglin|Eglin]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43649]]
+[[Category: Hirudo medicinalis]]
-[[Category: Hirme]]
 [[Category: Large Structures]]
-[[Category: Thermitase]]
+[[Category: Thermoactinomyces vulgaris]]
-[[Category: Dijkstra, B W]]
+[[Category: Dijkstra BW]]
-[[Category: Gros, P]]
+[[Category: Gros P]]
-[[Category: Hol, W G.J]]
+[[Category: Hol WGJ]]