SASBDB entries for UniProt ID:

SASDFQ3 – Complex with 1H histone acetyltransferase Rtt109 and histones H3 and H4, 2H histone chaperones Asf1 and Vps75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired 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: 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, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. 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

SASDFR3 – Complex with 1H histone chaperone Vps75 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Asf1 (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired 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: 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, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.1 nm
Dmax 10.5 nm

SASDFS3 – Murine transcription intermediary factor 1-beta, TRIM28 RBCC assembly-null mutation R184D

UniProt ID: Q62318 (58-418) Transcription intermediary factor 1-beta
Transcription intermediary factor 1-beta experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta dimer, 82 kDa Mus musculus protein
Buffer: 10 mM Tris 300 mM NaCl 0.1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Aug 10
A Dissection of Oligomerisation by the TRIM28 Tripartite Motif and the Interaction with Members of the Krab-ZFP Family. J Mol Biol (2019)
Sun Y, Keown JR, Black MM, Raclot C, Demarais N, Trono D, Turelli P, Goldstone DC
RgGuinier 7.0 nm
Dmax 23.2 nm
VolumePorod 232 nm3

SASDFT3 – Murine transcription intermediary factor 1-beta, TRIM28 RBCC assembly-null mutation R184D, complexed with the Krab domain of ZFP809 fused to an N-terminal MBP

UniProt ID: Q62318 (58-418) Transcription intermediary factor 1-beta

UniProt ID: G3X9G7 (1-74) Zinc finger protein 809 N-terminal MBP fusion
Transcription intermediary factor 1-betaZinc finger protein 809 N-terminal MBP fusion experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta dimer, 82 kDa Mus musculus protein
Zinc finger protein 809 N-terminal MBP fusion monomer, 52 kDa Mus musculus protein
Buffer: 10 mM Tris 300 mM NaCl 0.1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Aug 10
A Dissection of Oligomerisation by the TRIM28 Tripartite Motif and the Interaction with Members of the Krab-ZFP Family. J Mol Biol (2019)
Sun Y, Keown JR, Black MM, Raclot C, Demarais N, Trono D, Turelli P, Goldstone DC
RgGuinier 6.4 nm
Dmax 22.0 nm
VolumePorod 252 nm3

SASDFU3 – Lysine-specific Demethylase (LSD2)

UniProt ID: Q8NB78 (31-822) Lysyne-specific Demethylase LSD2
Lysyne-specific Demethylase LSD2 experimental SAS data
Lysyne-specific Demethylase LSD2 Kratky plot
Sample: Lysyne-specific Demethylase LSD2 monomer, 89 kDa Homo sapiens protein
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 3.4 nm
Dmax 10.6 nm
VolumePorod 124 nm3

SASDFV3 – Cytokine-like nuclear factor dehydrogenase domain, NPAC DH (NPAC delta-261)

UniProt ID: Q49A26 (261-553) NPAC dehydrogenase domain
NPAC dehydrogenase domain experimental SAS data
NPAC dehydrogenase domain Kratky plot
Sample: NPAC dehydrogenase domain tetramer, 125 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment: SAXS data collected at BM29, ESRF on 2018 Jan 26
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 3.5 nm
Dmax 11.0 nm
VolumePorod 167 nm3

SASDFW3 – Cytokine-like nuclear factor dehydrogenase domain, NPAC DH, plus native linker (NPAC delta-205)

UniProt ID: Q49A26 (205-553) NPAC linker+DH (delta-205)
NPAC linker+DH (delta-205) experimental SAS data
NPAC linker+DH (delta-205) Kratky plot
Sample: NPAC linker+DH (delta-205) tetramer, 150 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment: SAXS data collected at BM29, ESRF on 2018 Jan 26
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 4.0 nm
Dmax 11.4 nm
VolumePorod 240 nm3

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

SASDF24 – Full-length X-chromosome linked inhibitor of apoptosis protein (XIAP)

UniProt ID: P98170 (1-497) E3 ubiquitin-protein ligase XIAP
E3 ubiquitin-protein ligase XIAP experimental SAS data
HADDOCK model
Sample: E3 ubiquitin-protein ligase XIAP dimer, 113 kDa Homo sapiens protein
Buffer: Xiap buffer, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 15
Conformational characterization of full-length X-chromosome-linked inhibitor of apoptosis protein (XIAP) through an integrated approach. IUCrJ 6(Pt 5):948-957 (2019)
Polykretis P, Luchinat E, Bonucci A, Giachetti A, Graewert MA, Svergun DI, Banci L
RgGuinier 3.9 nm
Dmax 12.8 nm
VolumePorod 207 nm3