2aas: Difference between revisions

Revision as of 15:13, 29 July 2008

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File:2aas.png

Template:STRUCTURE 2aas

HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPYHIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Template:ABSTRACT PUBMED 8381876

About this StructureAbout this Structure

2AAS is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

ReferenceReference

High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy., Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M, J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:8381876

Page seeded by OCA on Tue Jul 29 15:13:36 2008

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

OCA

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-'''HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''
+===HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY===
-==Overview==
+<!--
-High-resolution three-dimensional structures of bovine pancreatic ribonuclease A in aqueous solution have been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. The structures are based on: (1) 464 interproton distance constraints with accurate upper and lower limits, determined from build-up rates of nuclear Overhauser effects (NOE) by using the complete relaxation matrix; (2) 999 more approximate upper limits for interproton distances; and (3) 42 dihedral angle constraints (37 for phi and 5 for chi 1). A total of 16 structures were calculated, which show a root-mean-square (r.m.s.) deviation of 0.66 A for the backbone atoms and 1.68 A for all heavy-atoms. The converged structures are highly similar to those found in the crystal state. r.m.s. deviation of backbone atom positions in the crystal as compared to those in the average solution structure is 0.92 A. Observed differences are concentrated in loop regions and in the neighborhood of His119 and His48 side-chains. Dynamic aspects, such as H/D amide proton exchange and side-chain mobility have been examined.
+The line below this paragraph, {{ABSTRACT_PUBMED_8381876}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8381876 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8381876}}
 ==About this Structure==
-AAS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAS OCA].
+AAS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAS OCA].
 ==Reference==
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 [[Category: Rico, M.]]
 [[Category: Santoro, J.]]
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