Sali A, Overington J P
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.
Protein Sci. 1994 Sep;3(9):1582-96. doi: 10.1002/pro.5560030923.
We describe a database of protein structure alignments as well as methods and tools that use this database to improve comparative protein modeling. The current version of the database contains 105 alignments of similar proteins or protein segments. The database comprises 416 entries, 78,495 residues, 1,233 equivalent entry pairs, and 230,396 pairs of equivalent alignment positions. At present, the main application of the database is to improve comparative modeling by satisfaction of spatial restraints implemented in the program MODELLER (Sali A, Blundell TL, 1993, J Mol Biol 234:779-815). To illustrate the usefulness of the database, the restraints on the conformation of a disulfide bridge provided by an equivalent disulfide bridge in a related structure are derived from the alignments; the prediction success of the disulfide dihedral angle classes is increased to approximately 80%, compared to approximately 55% for modeling that relies on the stereochemistry of disulfide bridges alone. The second example of the use of the database is the derivation of the probability density function for comparative modeling of the cis/trans isomerism of the proline residues; the prediction success is increased from 0% to 82.9% for cis-proline and from 93.3% to 96.2% for trans-proline. The database is available via electronic mail.
我们描述了一个蛋白质结构比对数据库以及使用该数据库来改进比较蛋白质建模的方法和工具。该数据库的当前版本包含105个相似蛋白质或蛋白质片段的比对。该数据库由416个条目、78495个残基、1233对等效条目对以及230396对等效比对位置组成。目前,该数据库的主要应用是通过程序MODELLER(Sali A,Blundell TL,1993,J Mol Biol 234:779 - 815)中实现的空间约束来改进比较建模。为了说明该数据库的有用性,在相关结构中由等效二硫键提供的对二硫键构象的约束是从比对中推导出来的;与仅依赖二硫键立体化学的建模相比,二硫键二面角类别的预测成功率提高到了约80%,而仅依赖二硫键立体化学的建模预测成功率约为55%。该数据库使用的第二个例子是脯氨酸残基顺/反异构化比较建模的概率密度函数的推导;顺式脯氨酸的预测成功率从0%提高到了82.9%,反式脯氨酸的预测成功率从93.3%提高到了96.2%。该数据库可通过电子邮件获取。