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Fig. 2 | Journal of Animal Science and Technology

Fig. 2

From: In silico characterisation, homology modelling and structure-based functional annotation of blunt snout bream (Megalobrama amblycephala) Hsp70 and Hsc70 proteins

Fig. 2

Ma-Hsp70 a and Ma-Hsc70 b protein tertiary structure model and validation results: a 3-D homology model rendered by the SWISS-MODEL program. b Ramachandran plot analysis, indicating residues in the favoured regions (red), allowed regions (yellow), generously allowed regions (light yellow) and disallowed regions (white). c Overall quality of the model evaluated by the ERRAT program. On the error axis, two lines (95 and 99 %) indicate the confidence with which it is possible to reject regions that exceed that error value. Regions of the structure highlighted in grey and black can be rejected at 95 % and 99 % confidence level, respectively. d Z-score (highlighted as a black dot) is displayed in a plot that contains the Z-scores of all experimentally determined protein chains currently available in the Protein Data Bank. Groups of structures from different sources (X-ray and NMR) are distinguished by different colours (light- and dark-blue, respectively). e Plot of single residue energies, where window sizes of 40 and 10 residues are distinguished by dark- and light-green lines, respectively. Positive values indicate problematic or erroneous parts of the structure

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