1ccn
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ccn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCN FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ccn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCN FirstGlance]. <br> | ||
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1ccn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccn OCA], [https://pdbe.org/1ccn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccn RCSB], [https://www.ebi.ac.uk/pdbsum/1ccn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccn 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=1ccn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccn OCA], [https://pdbe.org/1ccn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccn RCSB], [https://www.ebi.ac.uk/pdbsum/1ccn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/1ccn_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/1ccn_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/main_output.php?pdb_ID=1ccn ConSurf]. | </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=1ccn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A set of computer programs called DINOSAUR has been developed, which allows the refinement of biomolecular structures directly from 2D NOE intensities. The NOE restraining potential implemented emphasises the weak intensities corresponding to larger distances which are more likely to determine the three-dimensional structure. An approximation based on a two-spin approximation is proposed for the gradient of the NOE intensities instead of the exact solution which is extremely time-consuming. The DINOSAUR routines have been implemented in various refinement programs (Distance bound Driven Dynamics, Molecular Dynamics and Energy Minimisation) and tested on an eight-residue model peptide. | ||
| + | |||
| + | Direct NOE refinement of biomolecular structures using 2D NMR data.,Bonvin AM, Boelens R, Kaptein R J Biomol NMR. 1991 Sep;1(3):305-9. PMID:1841701<ref>PMID:1841701</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1ccn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL
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