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由分辨率<0.25nm,同一性(identity)<30％的2401条肽链中计算提取了全部顺式与反式脯氨酸肽键的位置,数目分别为1221个与26401个,从而建立了一个较大规模的脯氨酸肽键数据集。统计分析了该数据集的基本特征:肽键N端残基的分布、N端残基的二面角统计、在二级结构中的分布情况、顺式肽键在脯氨酸肽键中所占比例。此数据集对于进一步研究顺反X-Pro肽键的结构、与氨基酸序列之间的关系,以及肽链折叠动力学具有重要作用。
The positions of all cis- and trans-proline peptide bonds were calculated from 2401 peptide chains with resolution <0.25nm and identity <30%, with numbers of 1221 and 26401 respectively, thus establishing A larger-scale proline peptide bond data set. The basic characteristics of the data set were statistically analyzed: distribution of N-terminal residues of peptide bond, dihedral angle statistics of N-terminal residues, distribution in secondary structure, cis peptide bond in proline peptide bond Proportion. This data set plays an important role in further studying the structure of cis-trans X-Pro peptide bonds, the relationship with amino acid sequences and the kinetics of peptide chain folding.