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Additional file 4: Figure S3. Ramachandran plot of modeled VP28 protein of WSSV. The number of residues in favored, allowed and outlier region are 96.4, 3.6 and 0%, respectively. On the X and Y axes, ϕ (phi) and ψ (psi) represent the torsion angles around Cα (alpha carbon) to amine and carboxyl group of different amino acids

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Additional file 3: Figure S2. The aligned protein sequence data of VP28 taking into consideration 66 sequences generated by BioEdit Sequence Alignment Editor. The left portion of the frame contained the isolate ids of the sequences. The digit in the upper portion of the figure represented the residue number of protein. The red bar indicates the unique mutation position along with the mutated amino acid

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Additional file 1: Table S1. qPCR profile of the studied samples by our designed and standardized method. Table S2. Accession no., sequence IDs, sources and collection time of the WSSVs sequences of dataset

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Additional file 2: Figure S1. Wu-Kabat protein variability index showed 13 unique mutations as observed from the protruded peaks’ positioned along with the amino acid residue of VP28 protein