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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: Taking the results as a whole , we propose that the binding of NAD + to PhoDHS is regulated by the NAD + concentration , which might itself be linked to the requirement for IF5A modification and the subsequent participation in translation . One PhoDHS tetramer binds two NAD + s at a low concentration of NAD + , but may be able to bind two additional NAD + s when supplemented with higher NAD + concentrations . This new model for NAD + binding by DHS is shown in Figure 4 with PhoDHS existing in three states : no NAD + , one PhoDHS tetramer binding two NAD + s on one side ( molAD or molBC ) , and one PhoDHS tetramer binding four NAD + s. Our structural data definitively demonstrate the different conformations of loop V288 - P299 in each monomer of PhoDHS , with the significant structural stabilization induced by NAD + binding , which , with the help of a comparison to the human DHS : GC7 structure , is likely stabilized into the final closed conformation ( conf2 ) upon binding spermidine . Indeed , the different conformations of the active site " lid , " or binding loop , observed in our structure are likely to reflect the absence of stabilizing interactions that spermidine binding would provide . Our structure provides a potential explanation for the NAD + -dependent binding of spermidine to DHS [ 29 ] . The conformation diversity observed in this region in our structure is compatible with an independence of NAD + binding to each monomer , suggesting that monomers of DHS may behave equally whether in a tetramer , dimer or heterodimers . Strikingly , our structure presents a simultaneous combination of three different conformations at the spermidine binding site that are reflective of a three - state conformational regulation of DHS by NAD + : the apo form , the open form , and the closed / reaction form . The structure thus highlights the role of On the left , the spermidine binding loop is disordered when there is no NAD + binding to DHS . In the middle , the loop is partially stabilized and structured in either conf1 or conf2 when NAD + binds to DHS . The binding of one NAD + to DHS could promote a second NAD + to bind to another monomer of the dimer , and binding of both NAD + s would be stabilized via the formation of the hydrogen bond between them . The spermidine binding loop is still disordered in another dimer of the tetramer which remains NAD + -free . On the right , the spermidine binding loop of all four monomers of PhoDHS will be ordered in conf2 in the presence of abundant NAD + , based on the current structure and human DHS structure . Yellow lines : loop in conf1 away from NAD + ; blue lines : loop in conf2 towards NAD + ; N : NAD + molecules .<|eot_id|><|start_header_id|>assistant<|end_header_id|>

no<|eot_id|>