Complete understanding of the connection between protein structure and protein sequence has been a major goal in bioinformatics. A strong correlation between sequence entropy, hydrophobicity, and flexibility has been shown in recent studies, but with anomalous regions of very high and low flexibility that needed more exploration. Using a set of 130 proteins and their aligning sequences, direct observations revealed high counts of small residues in the anomalous, low flexibility region, and high counts of gaps in the anomalous, high flexibility region. Additional investigations on the effect of packing radius and % bit score cutoff showed that 6 to 9 A radii gave the most reasonable sequence entropy data, and bit score cutoffs have no significant effect on the general trend of the sequence entropy.