1hb9: Difference between revisions

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 <StructureSection load='1hb9' size='340' side='right' caption='[[1hb9]], [[Resolution|resolution]] 25.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hb9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HB9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hb9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpprd Bpprd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HB9 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cjd|1cjd]], [[1hb5|1hb5]], [[1hb7|1hb7]], [[1hqn|1hqn]], [[1hx6|1hx6]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hb9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hb9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb9 OCA], [http://pdbe.org/1hb9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hb9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hb9 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COA3_BPPRD COA3_BPPRD]] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins.
+[[http://www.uniprot.org/uniprot/CAPSD_BPPRD CAPSD_BPPRD]] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1hb9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Enterobacteria phage prd1]]
+[[Category: Bpprd]]
 [[Category: Bamford, D H]]
 [[Category: Burnett, R M]]