1ikf: Difference between revisions

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@@ Line 3: / Line 3: @@
 <StructureSection load='1ikf' size='340' side='right'caption='[[1ikf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ikf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IKF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ikf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IKF FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bck|1bck]], [[1c5f|1c5f]], [[1csa|1csa]], [[1cwa|1cwa]], [[1cwb|1cwb]], [[1cwc|1cwc]], [[1cwf|1cwf]], [[1cwh|1cwh]], [[1cwi|1cwi]], [[1cwj|1cwj]], [[1cwk|1cwk]], [[1cwl|1cwl]], [[1cwm|1cwm]], [[1cwo|1cwo]], [[1cya|1cya]], [[1cyb|1cyb]], [[1cyn|1cyn]], [[1m63|1m63]], [[1mf8|1mf8]], [[1mik|1mik]], [[1qng|1qng]], [[1qnh|1qnh]], [[1xq7|1xq7]], [[2esl|2esl]], [[2oju|2oju]], [[2poy|2poy]], [[2rma|2rma]], [[2rmb|2rmb]], [[2rmc|2rmc]], [[2wfj|2wfj]], [[2x2c|2x2c]], [[2x7k|2x7k]], [[2z6w|2z6w]], [[3bo7|3bo7]], [[3cys|3cys]], [[3eov|3eov]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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=1ikf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ikf OCA], [https://pdbe.org/1ikf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ikf RCSB], [https://www.ebi.ac.uk/pdbsum/1ikf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ikf ProSAT]</span></td></tr>
 </table>
@@ Line 18: / Line 18: @@
 </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=1ikf ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The conformation of the immunosuppressive drug cyclosporin A (CsA) in a complex with a Fab molecule has been established by crystallographic analysis to 2.65 angstrom resolution. This conformation of CsA is similar to that recently observed in the complex with the rotamase cyclophilin, its binding protein in vivo, and totally different from its conformation in an isolated form as determined from x-ray and nuclear magnetic resonance analysis. Because the surfaces of CsA interacting with cyclophilin or with the Fab are not identical, these results suggest that the conformation of CsA observed in the bound form preexists in aqueous solution and is not produced by interaction with the proteins.
-A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex.,Altschuh D, Vix O, Rees B, Thierry JC Science. 1992 Apr 3;256(5053):92-4. PMID:1566062<ref>PMID:1566062</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ikf" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 23: @@
 *[[Sandbox 20009|Sandbox 20009]]
 *[[3D structures of human antibody|3D structures of human antibody]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Altschuh, D]]
+[[Category: Tolypocladium inflatum]]
-[[Category: Rees, B]]
+[[Category: Altschuh D]]
-[[Category: Thierry, J C]]
+[[Category: Rees B]]
-[[Category: Vix, O]]
+[[Category: Thierry J-C]]
-[[Category: Cyclosporin some]]
+[[Category: Vix O]]
-[[Category: Fab-cyclosporin complex]]
-[[Category: Immune system-immunosuppressant complex]]
-[[Category: Immunosuppressant]]