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febs12588-sup-0001-FigS1-S10.zipZip archive3158KFig. S1. Histograms of CSD values between trans and cis conformers. Fig. S2. Heteronuclear values of Sp140-PHD. Fig. S3. Alignment showing the conservation of Sp140-PHD among species. Fig. S4. Superposition of AIRE-PHD1 and Sp140-PHD structures. Fig. S5. NMR titrations and Modified Histone Peptide Arrays showing lack of interaction between unmodified histone H3 tail and Sp140-PHD. Fig. S6. NMR titrations showing lack of interaction between modified histone H3 tail and Sp140-PHD. Fig. S7. Surface representation of AIRE-PHD1 and Sp140-PHD. Fig. S8. 15N HSQC spectra of 15N-Pin1 with EAERpTPWN and EAERTPWN. Fig. S9. 15N HSQC spectra of 15N-Pin1 with Sp140-PHDT726D. Fig. S10. Mapping of the interaction between 15N Sp140-PHD in cis conformation and Pin1.

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