1bgi: Difference between revisions

Revision as of 19:06, 30 June 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:1bgi.png

Template:STRUCTURE 1bgi

ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)

Template:ABSTRACT PUBMED 10089401

About this StructureAbout this Structure

1BGI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401

Page seeded by OCA on Mon Jun 30 19:06:56 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bgi.gif|left|200px]]
+{{Seed}}
+[[Image:1bgi.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bgi|  PDB=1bgi  |  SCENE=  }}
-'''ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)'''
+===ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)===
-==Overview==
+<!--
-The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.
+The line below this paragraph, {{ABSTRACT_PUBMED_10089401}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10089401 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10089401}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Hydrolase]]
 [[Category: O-glycosyl]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:28:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:06:56 2008''