2kib

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 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kib OCA], [https://pdbe.org/2kib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kib RCSB], [https://www.ebi.ac.uk/pdbsum/2kib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kib ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 A resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils.
-Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.,Nielsen JT, Bjerring M, Jeppesen MD, Pedersen RO, Pedersen JM, Hein KL, Vosegaard T, Skrydstrup T, Otzen DE, Nielsen NC Angew Chem Int Ed Engl. 2009;48(12):2118-21. PMID:19130518<ref>PMID:19130518</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2kib" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>