## 1 Introduction  
Urinary tract infections (UTIs) are among the most prevalent infectious diseases, affecting millions of people annually [1]. An acute or chronic UTI can lead to a high chance of recurrence within a period of approximately 6 months [1]. Additionally, the increasing antibiotic resistance among uropathogens imposes a significant economic burden leading to a high rise in the annual global healthcare cost of UTI treatment [1]. According to a report by [PERSON] et al., in 2019, \(\sim\)404 million cases of UTs were estimated globally [2]. Hence there is an urgent need to design better therapeutics for UTI treatment and/or prevention. Gram-positive and Gram-negative bacteria and fungi are the primary microbial agents that cause UTs [1, 3, 4, 5, 6, 7, 8], among which uropathogenic _Escherichia coli_ (UPEC) is the most common [9, 10, 11]. UPEC expresses fibers known as chaperone-usher pathway (CUP) pili that are tipped with adhesions, which specifically bind to host receptors to colonize and invade various host tissues [1, 12, 13, 14]. UPEC uses F9 pili and their adhesin protein FmlH to bind to glycoproteins present on the host cell surfaces that are heavily glycosylated with terminal galactosides. Thereby, the bacteria are able to avoid being washed out by the urinary flow and can have a long residence time in the urinary tract, leading to chronic inflammation [15, 16, 17, 18, 19, 20]. The lectin domain (LD) of a type 1 pilus adhesin protein, FimH, binds to mannovylated glycoproteins on the epithelial cell surfaces in the kidney and bladder,and has been targeted by rationally developing high-affinity aryl mannosides [21; 22; 23; 24; 25; 26; 27; 28; 29] as an antivirulence strategy in UTI prevention. Another highly homologous pilus, F9/FmI, is one of the most common CUP pili in the _E. coli_ pan genome and is involved in UTIs [17; 19]. Previous work has demonstrated that UPEC upregulates F9 pili expression in response to bladder inflammation [17; 20]. The F9 pilus contains a FimH-like adhesin protein, known as FmIH, which binds to glycoproteins with terminal galactosides on kidneys and inflamed bladders. [PERSON] et al. observed that the deletion of FmIH from clinical UPEC isolates resulted in a competitive defect in the bacterial strain to maintain infection in the UTI mouse models. Since FmIH serves an important role in the UPEC pathogenesis cascade, it represents a promising target for antivirulence strategies for UTI prevention. Very little is known regarding compounds targeting FmIH [14; 17; 18], hence the use of cutting-edge computational modeling techniques can be an excellent starting point in the process of discovering novel chemical matter targeting FmIH. Traditional antibiotic treatment has led to the rise in various antibiotic-resistant strains of UPEC. The increasing antimicrobial resistance has rendered the antibiotic therapeutic strategy less effective, thus creating a greater need for alternate therapeutic strategies. One such alternative therapeutic approach is the anti-adhesion strategy [30]. This strategy aims at early-stage prevention of the adhesion of an infectious agent, thus preventing bacterial survival and pathogenesis. The underlying concept is that the anti-adhesive agents _competitively_ block bacterial adhesion [30]. The F9 pilus is a rod-like structure that is produced on the surface of the UPEC, formed by multiple protein domains non-covalently interacting with each other. The pilus consists of a tip adhesin lectin, FmIH, which specifically binds to glycoproteins that are glycosylated with galactose-containing structures and mediates adhesion to host cell surfaces initiating infections [19]. The tip adhesin FmIH forms the end of the pili containing two domains: the C-terminal domain (FmIH\({}_{\text{PD}}\)), which contains an immunoglobulin-like fold; and the N-terminal lectin domain (FmIH\({}_{\text{LD}}\)), which recognizes the galactose units on the target receptors present on the urinary tract epithelial cells [17; 18].