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==DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL==
==DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL==
<StructureSection load='1ccn' size='340' side='right'caption='[[1ccn]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1ccn' size='340' side='right'caption='[[1ccn]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ccn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Abyssinian_crambe Abyssinian crambe]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ccm|1ccm]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB]] The function of this hydrophobic plant seed protein is not known.  
[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=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&reg;/PubMed&reg;, 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>
[[Category: Abyssinian crambe]]
[[Category: Crambe hispanica subsp. abyssinica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boelens, R]]
[[Category: Boelens R]]
[[Category: Bonvin, A M.J J]]
[[Category: Bonvin AMJJ]]
[[Category: Kaptein, R]]
[[Category: Kaptein R]]
[[Category: Lamerichs, R M.J N]]
[[Category: Lamerichs RMJN]]
[[Category: Rullmann, J A.C]]
[[Category: Rullmann JAC]]
[[Category: Plant seed protein]]

Revision as of 15:39, 13 March 2024

DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL

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