The refined crystal structure of ribonuclease A at 2.0 A resolution.
作者： A. Wlodawer , R. Bott , L. Sjölin
DOI: 10.1016/S0021-9258(19)68195-0
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摘要: This paper describes the structure of bovine pancreatic ribonuclease A, refined by a restrained parameter least squares procedure at 2.0 A resolution, and rebuilt using computer graphics. The final agreement factor (formula see text) is 0.159. positions 951 main chain atoms have been determined with an estimated accuracy 0.17 A. In addition, model includes phosphate group in active site 176 waters, many them partial occupancy. bond lengths RNase differ from ideal values overall root mean square deviation 0.022 A; corresponding value for angle distances 0.06 planar ideality 0.017 peptide torsion angles 180 degrees 3.4 degrees. good difference Fourier maps. Two histidines, His 12 119, form hydrogen bonds to ion. 119 also bonded carboxyl ASp 121 carbonyl Thr 45. very similar that S, particularly region. discrepancy all residues 1 16 24 123 1.06 region 0.6
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