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Multistep modeling of protein structure: Application towards refinement of tyr‐tRNA synthetase
Author(s) -
Srinivasan Subhashini,
Shibata Masayuki,
Roychoudhury Mihir,
Rein Robert
Publication year - 1987
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560320825
Subject(s) - transfer rna , least squares function approximation , angstrom , crystallography , chemistry , root mean square , physics , geometry , mathematics , quantum mechanics , rna , biochemistry , statistics , estimator , gene
The scope of multistep modeling (MSM) is expanded by adding a least‐squares minimization step in the procedure to fit backbone reconstruction consistent with a set of C‐alpha coordinates. The analytical solution of Phi and Psi angles, that fits a C‐alpha x‐ray coordinate [1] is used for tyr‐tRNA synthetase. Phi and Psi angles for the region where the above mentioned method fails, are obtained by minimizing the difference in C‐alpha distances between the computed model and the crystal structure in a least‐squares sense. We present a stepwise application of this part of MSM to the determination of the complete backbone geometry of the 321 N terminal residues of tyrosine tRNA synthetase to a root mean square deviation of 0.47 Å from the crystallographic C‐alpha coordinates.