3ebx: Difference between revisions

Revision as of 20:09, 21 February 2008

REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER

OverviewOverview

The latter stages in the refinement of the protein erabutoxin b are described. The crystal structure of the 62-residue protein has been refined to a conventional R factor of 0.144 by stereochemically restrained least-squares methods using diffraction data to a limit of 1.4 A spacings. Emphasis was placed on determining as accurately as possible the solvent structure and the structures of heterogeneous groups in the protein. The final model includes two conformers for each of seven side chains and for an octapeptide segment. A total of 111 sites for water molecules have been located as well as one sulfate ion with a total of 68 site occupancies. 65 of the solvent sites overlap either with protein atoms belonging to groups in two alternative conformations or with other solvent sites. Dual protein conformers and overlapping solvent sites were both included in the least-squares refinement. Individual thermal and occupancy parameters were refined for solvent molecules. An analysis of these parameters has provided useful structural information.

About this StructureAbout this Structure

3EBX is a Single protein structure of sequence from Laticauda semifasciata with as ligand. This structure supersedes the now removed PDB entry 2EBX. Full crystallographic information is available from OCA.

ReferenceReference

Refinement at 1.4 A resolution of a model of erabutoxin b: treatment of ordered solvent and discrete disorder., Smith JL, Corfield PW, Hendrickson WA, Low BW, Acta Crystallogr A. 1988 May 1;44 ( Pt 3):357-68. PMID:3272151

Page seeded by OCA on Thu Feb 21 19:09:11 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:3ebx.gif|left|200px]]<br /><applet load="3ebx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:3ebx.gif|left|200px]]<br /><applet load="3ebx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="3ebx, resolution 1.4&Aring;" />
 '''REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER'''<br />
 ==Overview==
-The latter stages in the refinement of the protein erabutoxin b are, described. The crystal structure of the 62-residue protein has been, refined to a conventional R factor of 0.144 by stereochemically restrained, least-squares methods using diffraction data to a limit of 1.4 A spacings., Emphasis was placed on determining as accurately as possible the solvent, structure and the structures of heterogeneous groups in the protein. The, final model includes two conformers for each of seven side chains and for, an octapeptide segment. A total of 111 sites for water molecules have been, located as well as one sulfate ion with a total of 68 site occupancies. 65, of the solvent sites overlap either with protein atoms belonging to groups, in two alternative conformations or with other solvent sites. Dual protein, conformers and overlapping solvent sites were both included in the, least-squares refinement. Individual thermal and occupancy parameters were, refined for solvent molecules. An analysis of these parameters has, provided useful structural information.
+The latter stages in the refinement of the protein erabutoxin b are described. The crystal structure of the 62-residue protein has been refined to a conventional R factor of 0.144 by stereochemically restrained least-squares methods using diffraction data to a limit of 1.4 A spacings. Emphasis was placed on determining as accurately as possible the solvent structure and the structures of heterogeneous groups in the protein. The final model includes two conformers for each of seven side chains and for an octapeptide segment. A total of 111 sites for water molecules have been located as well as one sulfate ion with a total of 68 site occupancies. 65 of the solvent sites overlap either with protein atoms belonging to groups in two alternative conformations or with other solvent sites. Dual protein conformers and overlapping solvent sites were both included in the least-squares refinement. Individual thermal and occupancy parameters were refined for solvent molecules. An analysis of these parameters has provided useful structural information.
 ==About this Structure==
-EBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 2EBX. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3EBX OCA].
+EBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 2EBX. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EBX OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Laticauda semifasciata]]
 [[Category: Single protein]]
-[[Category: Corfield, P.W.R.]]
+[[Category: Corfield, P W.R.]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson, W A.]]
-[[Category: Low, B.W.]]
+[[Category: Low, B W.]]
-[[Category: Smith, J.L.]]
+[[Category: Smith, J L.]]
 [[Category: SO4]]
 [[Category: toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:39:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:11 2008''