3ebx
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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 SO4 as ligand. This structure superseeds 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 Tue Nov 20 19:39:51 2007