Weighted and un-weighted protein residue networks can predict key functional residues in proteins based on the closeness centrality C and betweenness centrality B values for each residue. A static snapshot of the protein structure, and a cutoff distance, are used to define edges between the network nodes. In this work we apply the weighted network approach to study the xcexb2-Lactamase Inhibitory Protein (BLIP). Joint recurrences extracted from molecular dynamics MD trajectory positions of the protein residue carbon alpha atoms are used to define edge weights between nodes, and no cutoff distance is used. The results for B and C from our approach are compared with those extracted from an un-weighted network, and a weighted network that uses interatomic contacts to define edge weights between nodes, respectively.