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SECOST: sequence-conformation-structure database for amino acid residues in proteins
O Shats1, I I Vaisman, A Shats
1Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-6805, USA.
Bioinformatics (Oxford, England)
|June 26, 1999
Summary
This study presents a comprehensive database detailing amino acid residue sequence, conformation, and structure from 473 proteins. This resource aids in protein modeling and understanding molecular structures.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Understanding protein structure-function relationships is crucial in molecular biology.
- High-quality structural data is essential for accurate protein modeling.
- A consolidated resource for amino acid residue information is needed.
Purpose of the Study:
- To create a comprehensive database of amino acid residue sequence-conformation-structure relationships.
- To provide a valuable resource for protein modeling applications.
- To facilitate research in structural biology and bioinformatics.
Main Methods:
- Compiled data from 473 high-quality, non-homologous protein spatial structures.
- Extracted and organized information on 114,828 individual amino acid residues.
- Utilized diverse data acquisition and processing methods.
Main Results:
- Established a database containing 114,828 amino acid residues with sequence, conformation, and structure data.
- The dataset is derived from 473 distinct, high-quality protein structures.
- Information was gathered using various established scientific methodologies.
Conclusions:
- The sequence-conformation-structure database is a significant resource for the scientific community.
- This database supports diverse protein modeling applications.
- It advances the understanding of amino acid residue behavior in protein structures.