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<StructureSection load='7ku3' size='340' side='right'caption='[[7ku3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='7ku3' size='340' side='right'caption='[[7ku3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7ku3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KU3 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KU3 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&#8491;</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ku3 OCA], [https://pdbe.org/7ku3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ku3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ku3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ku3 ProSAT]</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=7ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ku3 OCA], [https://pdbe.org/7ku3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ku3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ku3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ku3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
One often observes small but measurable differences in the diffraction data measured from different crystals of a single protein. These differences might reflect structural differences in the protein and may reveal the natural dynamism of the molecule in solution. Partitioning these mixed-state data into single-state clusters is a critical step that could extract information about the dynamic behavior of proteins from hundreds or thousands of single-crystal data sets. Mixed-state data can be obtained deliberately (through intentional perturbation) or inadvertently (while attempting to measure highly redundant single-crystal data). To the extent that different states adopt different molecular structures, one expects to observe differences in the crystals; each of the polystates will create a polymorph of the crystals. After mixed-state diffraction data have been measured, deliberately or inadvertently, the challenge is to sort the data into clusters that may represent relevant biological polystates. Here, this problem is addressed using a simple multi-factor clustering approach that classifies each data set using independent observables, thereby assigning each data set to the correct location in conformational space. This procedure is illustrated using two independent observables, unit-cell parameters and intensities, to cluster mixed-state data from chymotrypsinogen (ChTg) crystals. It is observed that the data populate an arc of the reaction trajectory as ChTg is converted into chymotrypsin.
A simple technique to classify diffraction data from dynamic proteins according to individual polymorphs.,Nguyen T, Phan KL, Kozakov D, Gabelli SB, Kreitler DF, Andrews LC, Jakoncic J, Sweet RM, Soares AS, Bernstein HJ Acta Crystallogr D Struct Biol. 2022 Mar 1;78(Pt 3):268-277. doi:, 10.1107/S2059798321013425. Epub 2022 Feb 18. PMID:35234141<ref>PMID:35234141</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ku3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Andrews LC]]
[[Category: Andrews LC]]

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