1pts: Difference between revisions

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 <StructureSection load='1pts' size='340' side='right'caption='[[1pts]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pts]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pts]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTS FirstGlance]. <br>
-</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=1pts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pts OCA], [https://pdbe.org/1pts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pts RCSB], [https://www.ebi.ac.uk/pdbsum/1pts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pts ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pts OCA], [https://pdbe.org/1pts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pts RCSB], [https://www.ebi.ac.uk/pdbsum/1pts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pts ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV]] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
+[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
 == 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=1pts ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The thermodynamic binding parameters and crystal structure for streptavidin-peptide complexes where the peptide sequences were obtained by random screening methods are reported. The affinities between streptavidin and two heptapeptides were determined by titrating calorimetric methods [Phe-Ser-His-Pro-Gln-Asn-Thr, Ka = 7944 (+/- 224) M-1, delta G degrees = -5.32 (+/- 0.01) kcal/mol, and delta H degrees = -19.34 (+/- 0.48) kcal/mol; His-Asp-His-Pro-Gln-Asn-Leu, Ka = 3542 (+/- 146) M-1, delta G degrees = -4.84 (+/- 0.03) kcal/mol, and delta H degrees = -19.00 (+/- 0.64) kcal/mol]. The crystal structure of streptavidin complexed with one of these peptides has been determined at 2.0-A resolution. The peptide (Phe-Ser-His-Pro-Gln-Asn-Thr) binds in a turn conformation with the histidine, proline, and glutamine side chains oriented inward at the biotin-binding site. A water molecule is immobilized between the histidine and glutamine side chains of the peptide and an aspartic acid side chain of the protein. Although some of the residues that participate in binding biotin also interact with the screened peptide, the peptide adopts an alternate method of utilizing binding determinants in the biotin-binding site of streptavidin.
-Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin.,Weber PC, Pantoliano MW, Thompson LD Biochemistry. 1992 Oct 6;31(39):9350-4. PMID:1390720<ref>PMID:1390720</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1pts" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Avidin 3D structures|Avidin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: As 4 1583]]
 [[Category: Large Structures]]
-[[Category: Pantoliano, M W]]
+[[Category: Streptomyces avidinii]]
-[[Category: Thompson, L D]]
+[[Category: Pantoliano MW]]
-[[Category: Weber, P C]]
+[[Category: Thompson LD]]
-[[Category: Biotin-binding protein-peptide complex]]
+[[Category: Weber PC]]
-[[Category: Glycoprotein]]