SASBDB entries for UniProt ID:

SASDPN3 – Vibrio cholerae ParD2:ParE2 antitoxin:toxin complex

UniProt ID: P58093 (1-80) Antitoxin ParD

UniProt ID: Q9KMJ0 (1-99) Toxin
Antitoxin ParDToxin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Antitoxin ParD hexamer, 54 kDa Vibrio cholerae serotype … protein
Toxin, 25 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Mar 6
Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module. Sci Adv 10(1):eadj2403 (2024)
Garcia-Rodriguez G, Girardin Y, Kumar Singh R, Volkov AN, Van Dyck J, Muruganandam G, Sobott F, Charlier D, Loris R
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 140 nm3

SASDPT3 – Histone-lysine N-methyltransferase multi protein complex: MLL1-WDR5-RBBP5-ASH2L

UniProt ID: Q03164 (3754-3969) Histone-lysine N-methyltransferase 2A

UniProt ID: P61964 (1-334) WD repeat-containing protein 5

UniProt ID: Q15291 (1-538) Retinoblastoma-binding protein 5

UniProt ID: Q9UBL3-3 (95-534) Set1/Ash2 histone methyltransferase complex subunit ASH2
Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Retinoblastoma-binding protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Retinoblastoma-binding protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 37 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TECP, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Feb 1
DPY30 acts as an ASH2L-specific stabilizer to stimulate the enzyme activity of MLL family methyltransferases on different substrates. iScience 25(9):104948 (2022)
Zhao L, Huang N, Mencius J, Li Y, Xu Y, Zheng Y, He W, Li N, Zheng J, Zhuang M, Quan S, Chen Y
RgGuinier 5.2 nm
Dmax 18.5 nm
VolumePorod 386 nm3

SASDPU3 – Histone-lysine N-methyltransferase multi protein complex bound to protein dpy-30 homologue: MLL1-WDR5-RBBP5-ASH2L-DPY30

UniProt ID: Q03164 (3754-3969) Histone-lysine N-methyltransferase 2A

UniProt ID: P61964 (1-334) WD repeat-containing protein 5

UniProt ID: Q15291 (1-538) Retinoblastoma-binding protein 5

UniProt ID: Q9UBL3-3 (95-534) Set1/Ash2 histone methyltransferase complex subunit ASH2

UniProt ID: Q9C005 (1-99) Protein dpy-30 homolog
Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Retinoblastoma-binding protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Protein dpy-30 homolog experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Retinoblastoma-binding protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Protein dpy-30 homolog Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 37 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Protein dpy-30 homolog dimer, 23 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM TECP, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Feb 1
DPY30 acts as an ASH2L-specific stabilizer to stimulate the enzyme activity of MLL family methyltransferases on different substrates. iScience 25(9):104948 (2022)
Zhao L, Huang N, Mencius J, Li Y, Xu Y, Zheng Y, He W, Li N, Zheng J, Zhuang M, Quan S, Chen Y
RgGuinier 5.4 nm
Dmax 17.5 nm
VolumePorod 411 nm3

SASDPV3 – Wild type oxalyl-CoA synthetase Pcs60p (2.5 mg/ml) - hexamer-tetramer equilibrium

UniProt ID: P38137 (1-543) Oxalate--CoA ligase
Oxalate--CoA ligase experimental SAS data
PYMOL model
Sample: Oxalate--CoA ligase, 363 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Dec 18
Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol Chem (2023)
Bürgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M
RgGuinier 4.7 nm
Dmax 13.2 nm
VolumePorod 565 nm3

SASDPW3 – Wild type oxalyl-CoA synthetase Pcs60p (0.5 mg/ml) - tetramer-hexamer equilibrium

UniProt ID: P38137 (1-543) Oxalate--CoA ligase
Oxalate--CoA ligase experimental SAS data
PYMOL model
Sample: Oxalate--CoA ligase, 363 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Dec 18
Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol Chem (2023)
Bürgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M
RgGuinier 4.5 nm
Dmax 13.7 nm
VolumePorod 432 nm3

SASDPX3 – Point mutant K352D oxalyl-CoA synthetase Pcs60p (2.5 mg/ml) - dimer

UniProt ID: P38137 (1-543) Oxalate--CoA ligase (K352D)
Oxalate--CoA ligase (K352D) experimental SAS data
PYMOL model
Sample: Oxalate--CoA ligase (K352D) dimer, 121 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Dec 18
Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol Chem (2023)
Bürgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M
RgGuinier 3.3 nm
Dmax 11.1 nm
VolumePorod 163 nm3

SASDPY3 – Point mutant K352D oxalyl-CoA synthetase Pcs60p (0.5 mg/ml) - dimer

UniProt ID: P38137 (1-543) Oxalate--CoA ligase (K352D)
Oxalate--CoA ligase (K352D) experimental SAS data
PYMOL model
Sample: Oxalate--CoA ligase (K352D) dimer, 121 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Dec 18
Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol Chem (2023)
Bürgi J, Lill P, Giannopoulou EA, Jeffries CM, Chojnowski G, Raunser S, Gatsogiannis C, Wilmanns M
RgGuinier 3.3 nm
Dmax 10.2 nm
VolumePorod 194 nm3

SASDPZ3 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 3’ss-ds DNA junction NER substrate

UniProt ID: P23025 (1-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (185-616) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: P15927 (45-270) Replication protein A 32 kDa subunit

UniProt ID: P35244 (1-121) Replication protein A 14 kDa subunit

UniProt ID: None (None-None) 3-prime ss-ds DNA junction NER model substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunitReplication protein A 14 kDa subunit3-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
3-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.3 nm
Dmax 14.7 nm
VolumePorod 189 nm3

SASDP24 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 5’ss-ds DNA junction NER substrate

UniProt ID: P35244 (1-121) Replication protein A 14 kDa subunit

UniProt ID: P23025 (1-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (185-616) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: P15927 (45-270) Replication protein A 32 kDa subunit

UniProt ID: None (None-None) 5-prime ss-ds DNA junction NER model substrate
Replication protein A 14 kDa subunitDNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunit5-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
5-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.6 nm
Dmax 16.5 nm
VolumePorod 220 nm3

SASDP34 – Ubiquitin-conjugating enzyme E2 conjugated to deuterated Ubiquitin (SANS data at 0% v/v D2O, plus additional SANS with contrast variation and SAXS datasets)

UniProt ID: P51668 (1-147) Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S)

UniProt ID: P0CG48 (1-76) Ubiquitin
Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S)Ubiquitin experimental SAS data
MONSA model
Sample: Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S) monomer, 17 kDa Homo sapiens protein
Ubiquitin monomer, 9 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2019 May 24
Production and characterisation of modularly deuterated UBE2D1–Ub conjugate by small angle neutron and X-ray scattering European Biophysics Journal (2022)
Pietras Z, Duff A, Morad V, Wood K, Jeffries C, Sunnerhagen M
RgGuinier 2.1 nm
Dmax 7.4 nm