SASBDB entries for UniProt ID:

SASDFA7 – Receptor binding BinB protein of mosquito-larvicidal Binary toxin in 100% D2O

UniProt ID: B1HQ59 (None-None) Lysinibacillus Mosquito-larvicidal receptor binding component
Lysinibacillus Mosquito-larvicidal receptor binding component experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysinibacillus Mosquito-larvicidal receptor binding component monomer, 53 kDa synthetic construct protein
Buffer: 25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH: 7.5
Experiment: SANS data collected at SANS-I facility, Dhruva Reactor, Bhabha Atomic Research Centre on 2019 Apr 24
Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization IUCrJ 7(2) (2020)
Sharma M, Aswal V, Kumar V, Chidambaram R
RgGuinier 3.3 nm
Dmax 9.9 nm

SASDFB7 – Human phenylalanine hydroxylase (hPAH)

UniProt ID: P00439 (1-452) Phenylalanine-4-hydroxylase
Phenylalanine-4-hydroxylase experimental SAS data
CORAL model
Sample: Phenylalanine-4-hydroxylase tetramer, 223 kDa Homo sapiens protein
Buffer: 0.02 mM Hepes, 0.2 M NaCl,, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 25
Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives Biomolecules 11(3):462 (2021)
Lopes R, Tomé C, Russo R, Paterna R, Leandro J, Candeias N, Gonçalves L, Teixeira M, Sousa P, Guedes R, Vicente J, Gois P, Leandro P
RgGuinier 4.3 nm
Dmax 14.8 nm
VolumePorod 336 nm3

SASDFC7 – Human phenylalanine hydroxylase (hPAH) + 1 mM L-Phe

UniProt ID: P00439 (1-452) Phenylalanine-4-hydroxylase
Phenylalanine-4-hydroxylase experimental SAS data
DAMMIN model
Sample: Phenylalanine-4-hydroxylase tetramer, 223 kDa Homo sapiens protein
Buffer: 0.02 mM Hepes, 0.2 M NaCl,, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 25
Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives Biomolecules 11(3):462 (2021)
Lopes R, Tomé C, Russo R, Paterna R, Leandro J, Candeias N, Gonçalves L, Teixeira M, Sousa P, Guedes R, Vicente J, Gois P, Leandro P
RgGuinier 4.0 nm
Dmax 12.3 nm
VolumePorod 367 nm3

SASDFD7 – Pseudomonas putida CBB5 NdmAB complex - static

UniProt ID: H9N289 (None-None) Methylxanthine N1-demethylase NdmA

UniProt ID: H9N290 (None-None) Methylxanthine N3-demethylase NdmB
Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.5 nm
Dmax 12.3 nm

SASDFE7 – Pseudomonas putida CBB5 mCherry-NdmA/NdmB complex - static

UniProt ID: H9N289 (None-None) Methylxanthine N1-demethylase NdmA

UniProt ID: H9N290 (None-None) Methylxanthine N3-demethylase NdmB
Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.4 nm
Dmax 13.8 nm

SASDFF7 – Pseudomonas putida CBB5 NdmA hexamer

UniProt ID: H9N289 (None-None) Methylxanthine N1-demethylase NdmA
Methylxanthine N1-demethylase NdmA experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA hexamer, 254 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 11.0 nm

SASDFG7 – Pseudomonas putida CBB5 NdmB hexamer

UniProt ID: H9N290 (None-None) Methylxanthine N3-demethylase NdmB
Methylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N3-demethylase NdmB hexamer, 258 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.3 nm
Dmax 12.2 nm

SASDFH7 – Pseudomonas putida CBB5 NdmAB complex

UniProt ID: H9N289 (None-None) Methylxanthine N1-demethylase NdmA

UniProt ID: H9N290 (None-None) Methylxanthine N3-demethylase NdmB
Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 10.9 nm

SASDFJ7 – Pseudomonas putida CBB5 mCherry-NdmA/ECFP-NdmB complex - static

UniProt ID: H9N289 (None-None) Methylxanthine N1-demethylase NdmA

UniProt ID: H9N290 (None-None) Methylxanthine N3-demethylase NdmB
Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 208 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.6 nm
Dmax 19.1 nm

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