These data relate to the work published in Biochemical Journal DOI: 10.1042/BCJ20210812

The peptides investigated had the following sequences:
1	Ac-AAQAAARQApSAAQKAY-NH2
2	Ac-AAQAAARQA SAAQKAY-NH2
3	Ac-AAQARAAQApSAAQAKY-NH2
4	Ac-AAQARAAQA SAAQAKY-NH2
5	Ac-AAQAAARQApSAAQAKY-NH2
6	Ac-AAQARAAQApSAAQKAY-NH2
7	Ac-AAQAAARQApTAAQKAY-NH2
8	Ac-AAQAAARQA TAAQKAY-NH2
9	Ac-AAQAAARQA AAAQKAY-NH2
10	Ac-AAQARAAQA AAAQAKY-NH2

where p denotes phosphorylation of the following S or T; Ac and NH2 are acetyl and amide capping groups.  

Circular dichroism: spectra were recorded at pH 7 and a temperature of 5 deg C using an APP Chirascan CD spectropolarimeter and 1 mm pathlength quartz cuvettes. Sample concentrations (shown in the spreadsheets) were typically 50-100 micromolar.

Nuclear magnetic resonance spectroscopy: 1H-15N HMQC, 1H-13C HSQC, 1H-1H TOCSY and 1H-1H NOESY NMR spectra were recorded for each peptide on a 600-MHz Bruker Avance spectrometer equipped with a quadruple resonance QCI-P cryoprobe, or a 950-MHz Bruker Ascend Aeon spectrometer equipped with a 5 mm TXO cryoprobe. Spectra were recorded at pH 6.5-7 and a temperature of 5 deg C.