Data from "Shape memory controls multi-substrate affinity and hierarchical domain motions in adenylate kinase catalysis"

The following raw unfiltered traces used in the manuscript is accessible here:

These *.abl files can be opened with Clampfit (Molecular Devices)

Fig. 1C.- Full recording of the apo protein is attached. Figure is cut out of the last part, time in the x-scale is unmodified.

Fig. 2A. Full recording of apo protein is provided
Fig. 2D. Full blockade is provided of ADK + 1 mM ATP 
Fig. 2E. Longer part of the trace is provided; 2 protein blockades ADK + 1 mM ATP + 1 mM AMP
Fig. 2F. Longer part of the trace is provided; 2 protein blockades ADK + 1 mM ATP without mg2+
Fig. 2G. Full blockade is provided of ADK + 1 mM ATP + 1 mM AMP

Fig 3 A1 - Full blockade is provided of ADK + 0.1 mM ADP 
Fig 3 A2 - Longer part of the trace is provided; 2 protein blockades ADK + 1 mM ADP
Fig 3 A3 -  Full blockade is provided of ADK + 1 mM ADP without mg2+

Fig 3 B1 - Full blockade is provided of ADK + 0.1 mM ADP 
Fig 3 B2 - Full blockade is provided of ADK, followed by a type I blockade to show the difference
Fig 3 B3 -  Full blockade is provided of ADK + 1 mM ATP ADP without mg2+

For the supplementary data only traces are added with the conditions that were not yet shown in the main text:
Fig. SI 4 - trace of binding of Ap5A to AdK, multiple blockades visible. 
Fig. SI 6 - longer part of the trace is provided
Fig. SI 7 - longer part of the trace is provided
Fig. SI 15 - full blockade as depicted 
Fig. SI 16 - full blockade as depicted 
Fig. SI 25 - Trace providing both Type I and Type II blockades with AMP and ADP. The pore is was inserted from trans instead of cis, hence the current is positive rather than negative. Recording was done at 90 mV. 


