1h34
From Proteopedia
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| - | [[Image:1h34.jpg|left|200px]]<br /><applet load="1h34" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h34, resolution 2.04Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF LIMA BEAN TRYPSIN INHIBITOR'''<br /> | ||
| - | == | + | ==Crystal structure of lima bean trypsin inhibitor== |
| + | <StructureSection load='1h34' size='340' side='right'caption='[[1h34]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1h34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaseolus_lunatus Phaseolus lunatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H34 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLX:GLU/GLN+AMBIGUOUS'>GLX</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=1h34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h34 OCA], [https://pdbe.org/1h34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h34 RCSB], [https://www.ebi.ac.uk/pdbsum/1h34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h34 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/1h34_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1h34 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
SAD (single-wavelength anomalous diffraction) has enormous potential for phasing proteins using only the anomalous signal of the almost ubiquitous native sulfur, but requires extremely precise data. The previously unknown structure of the lima bean trypsin inhibitor (LBTI) was solved using highly redundant data collected to 3 A using a CCD detector with a rotating-anode generator and three-circle goniometer. The seven 'super-S' atoms (disulfide bridges) were located by dual-space recycling with SHELXD and the high solvent content enabled the density-modification program SHELXE to generate high-quality maps despite the modest resolution. Subsequently, a 2.05 A synchrotron data set was collected and used for further phase extension and structure refinement. | SAD (single-wavelength anomalous diffraction) has enormous potential for phasing proteins using only the anomalous signal of the almost ubiquitous native sulfur, but requires extremely precise data. The previously unknown structure of the lima bean trypsin inhibitor (LBTI) was solved using highly redundant data collected to 3 A using a CCD detector with a rotating-anode generator and three-circle goniometer. The seven 'super-S' atoms (disulfide bridges) were located by dual-space recycling with SHELXD and the high solvent content enabled the density-modification program SHELXE to generate high-quality maps despite the modest resolution. Subsequently, a 2.05 A synchrotron data set was collected and used for further phase extension and structure refinement. | ||
| - | + | In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case.,Debreczeni JE, Bunkoczi G, Girmann B, Sheldrick GM Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):393-5. Epub 2003, Jan 23. PMID:12554963<ref>PMID:12554963</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1h34" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Phaseolus lunatus]] | [[Category: Phaseolus lunatus]] | ||
| - | + | [[Category: Bunkoczi G]] | |
| - | [[Category: Bunkoczi | + | [[Category: Debreczeni JE]] |
| - | [[Category: Debreczeni | + | [[Category: Girmann B]] |
| - | [[Category: Girmann | + | [[Category: Sheldrick GM]] |
| - | [[Category: Sheldrick | + | |
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Current revision
Crystal structure of lima bean trypsin inhibitor
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