A tracked approach for automated NMR assignments in proteins (TATAPRO)

Atreya, H. S. ; Sahu, S. C. ; Chary, K. V. R. ; Govil, Girjesh (2006) A tracked approach for automated NMR assignments in proteins (TATAPRO) Journal of Biomolecular NMR, 17 (2). pp. 125-136. ISSN 0925-2738

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Official URL: http://www.springerlink.com/content/ml03h77v703531...

Related URL: http://dx.doi.org/10.1023/A:1008315111278


A novel automated approach for the sequence specific NMR assignments of 1HN, 13Cα, 13Cβ, 13C'/1Hα and 15N spins in proteins, using triple resonance experimental data, is presented. The algorithm, TATAPRO (Tracked AuTomated Assignments in Proteins) utilizes the protein primary sequence and peak lists from a set of triple resonance spectra which correlate 1HN and 15N chemical shifts with those of 13Cα, 13Cβ and 13C'/1Hα. The information derived from such correlations is used to create a 'master list' consisting of all possible sets of 1HN i, 15Ni, 13Cα i, 13Cβ i, 13C'i/1Hα i, 13Cα i-1, 13Cβ i-1 and 13C'i-1/ 1Hα i-1 chemical shifts. On the basis of an extensive statistical analysis of 13Cα and 13Cβ chemical shift data of proteins derived from the BioMagResBank (BMRB), it is shown that the 20 amino acid residues can be grouped into eight distinct categories, each of which is assigned a unique two-digit code. Such a code is used to tag individual sets of chemical shifts in the master list and also to translate the protein primary sequence into an array called pps array. The program then uses the master list to search for neighbouring partners of a given amino acid residue along the polypeptide chain and sequentially assigns a maximum possible stretch of residues on either side. While doing so, each assigned residue is tracked in an array called assig array, with the two-digit code assigned earlier. The assig_array is then mapped onto the pps array for sequence specific resonance assignment. The program has been tested using experimental data on a calcium binding protein from Entamoeba histolytica (Eh-CaBP, 15 kDa) having substantial internal sequence homology and using published data on four other proteins in the molecular weight range of 18-42 kDa. In all the cases, nearly complete sequence specific resonance assignments (> 95%) are obtained. Furthermore, the reliability of the program has been tested by deleting sets of chemical shifts randomly from the master list created for the test proteins.

Item Type:Article
Source:Copyright of this article belongs to Springer-Verlag.
Keywords:Automated NMR Assignments; Borrelia burgdoferi OspA; Drosophila Numb Phosphotyrosine-binding Domain; Eh-CaBP; Escherichia Coli Maltose Binding Protein; Fibroblast Collagenase; Sequence Specific Resonance Assignments; Triple Resonance Experiments
ID Code:15470
Deposited On:13 Nov 2010 08:58
Last Modified:17 May 2016 00:21

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