3gb1

<StructureSection load='3gb1' size='340' side='right'caption='[[3gb1]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[3gb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GB1 FirstGlance]. <br>

</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=3gb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gb1 OCA], [https://pdbe.org/3gb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gb1 RCSB], [https://www.ebi.ac.uk/pdbsum/3gb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gb1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.,Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM Science. 1991 Aug 9;253(5020):657-61. PMID:1871600<ref>PMID:1871600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Strsg]]

[[Category: Clore, G M]]

[[Category: Immunoglobulin binding protein]]