MODBASE: a database of annotated comparative protein structure models and associated resources.
MODBASE: a database of annotated comparative protein structure models and associated resources.
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DOI：
10.1093/nar/gkj059
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发表时间：
2006-01-01
影响因子：
14.9
通讯作者：
Sali A
中科院分区：
文献类型：
--
作者：
Pieper U;Eswar N;Davis FP;Braberg H;Madhusudhan MS;Rossi A;Marti-Renom M;Karchin R;Webb BM;Eramian D;Shen MY;Kelly L;Melo F;Sali A
MODBASE()是所有可与至少一个已知蛋白质结构匹配的可用蛋白质序列的带注释的比较蛋白质结构模型的数据库。模型由MODPIPE计算，这是一种自动建模管道，依赖建模师进行折叠分配、序列结构比对、模型构建和模型评估()。MODBASE定期更新，以反映蛋白质序列和结构数据库的增长，以及计算模型的软件的改进。MODBASE目前包含3个 094 524结构域的可靠模型，用于UniProt数据库中1个 094 750中的1个 817 889唯一蛋白质序列(2005年7月5日)；仅包括基于统计显著比对的模型和尽管不显著比对但被评估为具有正确折叠的模型。MODBASE还允许用户使用自动建模服务器MODWEB()为感兴趣的蛋白质生成比较模型。我们与MODBASE集成的其他资源包括多个蛋白质结构比对的综合数据库(DBALI，)、结构定义的配体结合位点和结构定义的二元域界面(PIBASE，)以及配体结合位点的预测，酵母蛋白之间的相互作用，以及人类nsSNPs的功能后果(LS-SNP，)。
MODBASE () is a database of annotated comparative protein structure models for all available protein sequences that can be matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on MODELLER for fold assignment, sequence–structure alignment, model building and model assessment (). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, and improvements in the software for calculating the models. MODBASE currently contains 3 094 524 reliable models for domains in 1 094 750 out of 1 817 889 unique protein sequences in the UniProt database (July 5, 2005); only models based on statistically significant alignments and models assessed to have the correct fold despite insignificant alignments are included. MODBASE also allows users to generate comparative models for proteins of interest with the automated modeling server MODWEB (). Our other resources integrated with MODBASE include comprehensive databases of multiple protein structure alignments (DBAli, ), structurally defined ligand binding sites and structurally defined binary domain interfaces (PIBASE, ) as well as predictions of ligand binding sites, interactions between yeast proteins, and functional consequences of human nsSNPs (LS-SNP, ).
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影响因子：
14.9
作者：
Eswar, N;John, B;Sali, A
通讯作者：
Sali, A
影响因子：
7.4
作者：
Hillisch A;Pineda LF;Hilgenfeld R
通讯作者：
Hilgenfeld R
影响因子：
5.8
作者：
Davis, FP;Sali, A
通讯作者：
Sali, A
影响因子：
13.8
作者：
Henrick, K;Thornton, JM
通讯作者：
Thornton, JM
影响因子：
3
作者：
Pettersen, EF;Goddard, TD;Ferrin, TE
通讯作者：
Ferrin, TE