SASBDB entries for UniProt ID: P62799

SASDFX3 – Semi-synthetic nucleosome core particle (NCP)

UniProt ID: None (2-136) Histone H3

UniProt ID: P62799 (2-103) Histone H4

UniProt ID: Q6AZJ8 (2-130) Histone H2a

UniProt ID: Q92130 (5-126) Histone H2b

UniProt ID: None (None-None) 147bp 601 Widom sequence
Histone H3Histone H4Histone H2aHistone H2b147bp 601 Widom sequence experimental SAS data
Histone H3 Histone H4 Histone H2a Histone H2b 147bp 601 Widom sequence Kratky plot
Sample: Histone H3 dimer, 31 kDa Xenopus laevis protein
Histone H4 dimer, 22 kDa Xenopus laevis protein
Histone H2a dimer, 28 kDa Xenopus laevis protein
Histone H2b dimer, 27 kDa Xenopus laevis protein
147bp 601 Widom sequence monomer, 45 kDa synthetic construct DNA
Buffer: 15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 11
A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Cell Rep 27(2):387-399.e7 (2019)
Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A
RgGuinier 4.4 nm
Dmax 12.8 nm
VolumePorod 353 nm3

SASDFY3 – Semi-synthetic nucleosome core particle (NCP) in complex with lysine-specific demethylase (LSD2) and the dehydrogenase domain plus linker of cytokine-like nuclear factor (NPAC delta-205)

UniProt ID: Q8NB78 (31-822) Lysyne-specific Demethylase LSD2

UniProt ID: Q49A26 (205-553) NPAC linker+DH (delta-205)

UniProt ID: None (2-136) Histone H3

UniProt ID: P62799 (2-103) Histone H4

UniProt ID: Q6AZJ8 (2-130) Histone H2a

UniProt ID: Q92130 (5-126) Histone H2b

UniProt ID: None (None-None) 147bp 601 Widom sequence
Lysyne-specific Demethylase LSD2NPAC linker+DH (delta-205)Histone H3Histone H4Histone H2aHistone H2b147bp 601 Widom sequence experimental SAS data
Lysyne-specific Demethylase LSD2 NPAC linker+DH (delta-205) Histone H3 Histone H4 Histone H2a Histone H2b 147bp 601 Widom sequence Kratky plot
Sample: Lysyne-specific Demethylase LSD2 monomer, 89 kDa Homo sapiens protein
NPAC linker+DH (delta-205) tetramer, 150 kDa Homo sapiens protein
Histone H3 dimer, 31 kDa Xenopus laevis protein
Histone H4 dimer, 22 kDa Xenopus laevis protein
Histone H2a dimer, 28 kDa Xenopus laevis protein
Histone H2b dimer, 27 kDa Xenopus laevis protein
147bp 601 Widom sequence monomer, 45 kDa synthetic construct DNA
Buffer: 15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 11
A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Cell Rep 27(2):387-399.e7 (2019)
Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A
RgGuinier 7.8 nm
Dmax 30.4 nm
VolumePorod 1100 nm3

SASDFK7 – Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone 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: P84233 (35-135) Histone H3.2 (35-135 aa)

UniProt ID: P62799 (1-103) Histone H4
Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK 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 H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 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 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 1.9 nm
Dmax 5.5 nm

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

SASDJ96 – Trinucleosomes from Xenopus laevis (African clawed frog)

UniProt ID: Q92133 (None-None) Histone H3

UniProt ID: P62799 (None-None) Histone H4

UniProt ID: P06897 (None-None) Histone H2A type 1

UniProt ID: Q92130 (None-None) Histone H2B

UniProt ID: None (None-None) Non-linker Ended Trinucleosome DNA
Histone H3Histone H4Histone H2A type 1Histone H2BNon-linker Ended Trinucleosome DNA experimental SAS data
Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA Kratky plot
Sample: Histone H3 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B monomer, 14 kDa Xenopus laevis protein
Non-linker Ended Trinucleosome DNA monomer, 172 kDa DNA
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 1 mM DTT 50% w/v sucrose, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Mar 11
Solution structure(s) of trinucleosomes from contrast variation SAXS Nucleic Acids Research (2021)
Mauney A, Muthurajan U, Luger K, Pollack L
RgGuinier 12.9 nm
Dmax 41.8 nm