1j4v: Difference between revisions

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-[[Image:1j4v.png|left|200px]]
+==CYANOVIRIN-N==
+<StructureSection load='1j4v' size='340' side='right' caption='[[1j4v]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1j4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J4V FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ezm|2ezm]], [[2ezn|2ezn]], [[3ezm|3ezm]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j4v RCSB], [http://www.ebi.ac.uk/pdbsum/1j4v PDBsum]</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/j4/1j4v_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A simple and robust method for determining the relative orientations of covalently linked protein domains using conjoined rigid body/torsion angle dynamics simulated annealing on the basis of residual dipolar couplings is presented. In this approach each domain is treated as a rigid body and the relevant degrees of conformational freedom are restricted to the backbone torsion angles (phi, psi) of the linker between the domains. By this means translational information afforded by the presence of an intact linker is preserved. We illustrate this approach using the domain-swapped dimer of the HIV-inactivating protein cyanovirin-N as an example.
-{{STRUCTURE_1j4v|  PDB=1j4v  |  SCENE=  }}
+Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings.,Clore GM, Bewley CA J Magn Reson. 2002 Feb;154(2):329-35. PMID:11846592<ref>PMID:11846592</ref>
-===CYANOVIRIN-N===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11846592}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1j4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4V OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011846592</ref><references group="xtra"/>
 [[Category: Nostoc ellipsosporum]]
 [[Category: Bewley, C A.]]