4RHV

THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT OF THE HUMAN RHINOVIRUS 14 STRUCTURE

Replaces:  2RHVReplaces:  1RHV

Summary for 4RHV

• Entry DOI: 10.2210/pdb4rhv/pdb
• Descriptor: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2), HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3), ... (5 entities in total)
• Functional Keywords: rhinovirus coat protein, icosahedral virus, virus
• Biological source: Human rhinovirus 14; More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03303 P03303 P03303 P03303
• Total number of polymer chains: 4
• Total formula weight: 94482.53

Authors

Arnold, E.,Rossmann, M.G. (deposition date: 1988-01-25, release date: 1988-04-16, Last modification date: 2024-05-22)

Primary citation

Arnold, E.,Rossmann, M.G.
The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure.
Acta Crystallogr.,Sect.A, 44:270-282, 1988

PubMed Abstract: The structure of human rhinovirus 14 has been refined, by the method of restrained least squares, to an R factor of 0.16 for various random samples between 6 and 3 A resolution with F greater than 3 sigma (F). As a first step the non-crystallographic symmetry parameters were optimized using the initial atomic model in a rigid-body refinement procedure. Phase determination by the molecular-replacement phase extension and refinement procedure was continued to 2.94 A resolution, employing the improved non-crystallographic symmetry operators. The resultant structure-factor phases and weights, together with the measured amplitudes, constituted the X-ray observations used in the restrained refinement. The Hendrickson-Konnert program system [Konnert & Hendrickson (1980). Acta Cryst. A36, 344-350] was modified to incorporate non-crystallographic symmetry constrains and structure-factor phases as observations. The non-bonded contacts between subunits related by non-crystallographic symmetry were also restrained.

PubMed: 2856083
DOI: 10.1107/S0108767387011875

Experimental method

X-RAY DIFFRACTION (3 Å)