<|begin_of_text|><|start_header_id|>system<|end_header_id|>

You are an expert at identifying data availability statements in scientific text. A data availability statement describes where research data can be found or how it can be accessed.<|eot_id|><|start_header_id|>user<|end_header_id|>

Determine if the following text contains a data availability statement. Answer with 'yes' or 'no'.

Text: Theb iochemical data were in accordance with the data obtained from structural analysis of the mutants . I nt he H42Q - uridine complex ( Figure 3A , C ) , the critical interactions between 5 ' OH and Y55 and Y89 remained the same as in the WT - uridine structure , a dditionally the hydrogen bond between K16 and E108 with 2'-OH , as well as the p - stacking of the uracil ring with F103 are all preserved . Q42 appears to have the same distance from the 4 ' proton and the overall fold of the protein does not seem to be impacted , all of which suggests that the H42Q mutation affects the key catalytic step and not substrate binding . Similarly , onexamining the Y89Furidine complex ( Figure 3B , D ) and Y55F - uridine complex structures ( Figure S23 , Table S4 ) , we observed ah igh degree of similarity with the wt enzyme . A lthough there are subtle shifts in the position of both the ribose and uracil rings , ofthe substrate , a nd in the orientation of the 5 ' functionality , t hese changes are small and consistent with our hypothesis that decreased catalytic efficiencyo ft hese mutants is largely due to inability of the phenyl mutants to stabilize the transient 5 ' oxo - anion that forms during catalysis , r ather than having amajor effect on binding competency .<|eot_id|><|start_header_id|>assistant<|end_header_id|>

no<|eot_id|>