SASBDB entries for UniProt ID: Q6PI79

SASDFL7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
GROMACS model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.4 nm
Dmax 10.5 nm

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 2.7 nm
Dmax 9.0 nm

SASDFN7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4, histone chaperones Asf1 and Vps75 (1-225aa) (acquired in 100% v/v D2O)

UniProt ID: P53853 (1-225) Vacuolar protein sorting-associated protein 75 (1-225 aa)

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Kratky plot
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.0 nm

SASDFP7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length

UniProt ID: P53853 (1-264) Vacuolar protein sorting-associated protein 75 full-length
Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Kratky plot
Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.5 nm

SASDFQ7 – Complex with 1H histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O

UniProt ID: Q07794 (1-436) Histone acetyltransferase RTT109

UniProt ID: P32447 (1-169) Histone chaperone ASF1

UniProt ID: P62799 (1-103) Histone H4

UniProt ID: Q6PI79 (1-136) Histone H3 full-length

UniProt ID: P53853 (1-264) Vacuolar protein sorting-associated protein 75 full-length
Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Kratky plot
Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.1 nm
Dmax 9.5 nm