1mso: Difference between revisions

Revision as of 14:36, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mso.png

Template:STRUCTURE 1mso

T6 Human Insulin at 1.0 A ResolutionT6 Human Insulin at 1.0 A Resolution

Template:ABSTRACT PUBMED 12595704

About this StructureAbout this Structure

1MSO is a Protein complex structure. Full crystallographic information is available from OCA.

ReferenceReference

The structure of T6 human insulin at 1.0 A resolution., Smith GD, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):474-82. Epub 2003, Feb 21. PMID:12595704

Page seeded by OCA on Tue Jul 29 14:36:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1mso.gif|left|200px]]
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 {{STRUCTURE_1mso|  PDB=1mso  |  SCENE=  }}
-'''T6 Human Insulin at 1.0 A Resolution'''
+===T6 Human Insulin at 1.0 A Resolution===
-==Overview==
+<!--
-The structure of T(6) human insulin has been determined at 120 K at a resolution of 1.0 A and refined to a residual of 0.183. As a result of cryofreezing, the first four residues of the B chain in one of the two crystallographically independent AB monomers in the hexameric [Zn(1/3)(AB)(2)Zn(1/3)](3) complex undergo a conformational shift that displaces the C(alpha) atom of PheB1 by 7.86 A relative to the room-temperature structure. A least-squares superposition of all backbone atoms of the room-temperature and low-temperature structures yielded a mean displacement of 0.422 A. Omitting the first four residues of the B chain reduced the mean displacement to 0.272 A. At 120 K, nine residues were found to exhibit two discrete side-chain conformations, but only two of these residues are in common with the seven residues found to have disordered side chains in the room-temperature structure. As a result of freezing, the disorder observed at room temperature in both ArgB22 side chains is eliminated. The close contact between pairs of O( epsilon 2) atoms in GluB13 observed at room temperature is maintained at cryotemperature and suggests that a carboxylate-carboxylic acid centered hydrogen bond exists [-C(=O)-O.H.O-C(=O)-] such that the H atom is equally shared between the two partially charged O atoms.
+The line below this paragraph, {{ABSTRACT_PUBMED_12595704}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12595704 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12595704}}
 ==About this Structure==
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 [[Category: Smith, G D.]]
 [[Category: T6 conformation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:40:41 2008''
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