SASBDB entries for UniProt ID:

SASDFT8 – The retinoic acid receptor (RAR-RXR heterodimer) bound to the DNA response element HoxB13 DR0

UniProt ID: P11416 (84-421) Retinoic acid receptor alpha, RAR

UniProt ID: P28700 (135-467) Retinoic acid receptor RXR-alpha

UniProt ID: None (None-None) DNA response element HoxB13 DR0
Retinoic acid receptor alpha, RARRetinoic acid receptor RXR-alphaDNA response element HoxB13 DR0 experimental SAS data
CORAL model
Sample: Retinoic acid receptor alpha, RAR monomer, 41 kDa Mus musculus protein
Retinoic acid receptor RXR-alpha monomer, 38 kDa Mus musculus protein
DNA response element HoxB13 DR0 monomer, 10 kDa DNA
Buffer: 20 mM Tris, pH 8, 150 mM NaCl, 5% v/v glycerol, 1 mM CHAPS, 4 mM MgSO4, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 19
Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR–RXR Nucleic Acids Research (2020)
Osz J, McEwen A, Bourguet M, Przybilla F, Peluso-Iltis C, Poussin-Courmontagne P, Mély Y, Cianférani S, Jeffries C, Svergun D, Rochel N
RgGuinier 3.8 nm
Dmax 14.5 nm
VolumePorod 132 nm3

SASDFU8 – The retinoic acid receptor (RAR-RXR heterodimer) bound to the DNA response element F11r DR5.

UniProt ID: P11416 (84-421) Retinoic acid receptor alpha, RAR

UniProt ID: P28700 (135-467) Retinoic acid receptor RXR-alpha

UniProt ID: None (None-None) DNA response element F11r DR5
Retinoic acid receptor alpha, RARRetinoic acid receptor RXR-alphaDNA response element F11r DR5 experimental SAS data
CORAL model
Sample: Retinoic acid receptor alpha, RAR monomer, 41 kDa Mus musculus protein
Retinoic acid receptor RXR-alpha monomer, 38 kDa Mus musculus protein
DNA response element F11r DR5 monomer, 13 kDa DNA
Buffer: 20 mM Tris, pH 8, 150 mM NaCl, 5% v/v glycerol, 1 mM CHAPS, 4 mM MgSO4, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 19
Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR–RXR Nucleic Acids Research (2020)
Osz J, McEwen A, Bourguet M, Przybilla F, Peluso-Iltis C, Poussin-Courmontagne P, Mély Y, Cianférani S, Jeffries C, Svergun D, Rochel N
RgGuinier 4.0 nm
Dmax 13.5 nm
VolumePorod 130 nm3

SASDFV8 – Apolipoprotein E2 (ApoE2) bound to 4 µg/mL heparin

UniProt ID: P02649 (19-317) Apolipoprotein E2

UniProt ID: None (None-None) Heparin
Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.2 nm
Dmax 20.7 nm
VolumePorod 504 nm3

SASDFW8 – Apolipoprotein E2 (ApoE2) bound to 12 µg/mL heparin

UniProt ID: P02649 (19-317) Apolipoprotein E2

UniProt ID: None (None-None) Heparin
Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.4 nm
Dmax 21.7 nm
VolumePorod 531 nm3

SASDFX8 – Apolipoprotein E2 (ApoE2) bound to 37 µg/mL heparin

UniProt ID: P02649 (19-317) Apolipoprotein E2

UniProt ID: None (None-None) Heparin
Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.5 nm
Dmax 23.4 nm
VolumePorod 584 nm3

SASDFY8 – Apolipoprotein E2 (ApoE2) bound to 110 µg/mL heparin

UniProt ID: P02649 (19-317) Apolipoprotein E2

UniProt ID: None (None-None) Heparin
Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 7.1 nm
Dmax 24.0 nm
VolumePorod 666 nm3

SASDFZ8 – Apolipoprotein E2 (ApoE2) bound to 330 µg/mL heparin

UniProt ID: P02649 (19-317) Apolipoprotein E2

UniProt ID: None (None-None) Heparin
Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 7.2 nm
Dmax 24.5 nm
VolumePorod 696 nm3

SASDF29 – Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4 - in complex with STAU1 binding site within the ADP-ribosylation factor1

UniProt ID: O95793 (286-355) Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4

UniProt ID: None (None-None) ADP-ribosylation factor1 - short
Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4ADP-ribosylation factor1 - short experimental SAS data
OTHER model
Sample: Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4 monomer, 8 kDa Homo sapiens protein
ADP-ribosylation factor1 - short monomer, 11 kDa Homo sapiens RNA
Buffer: 50 mM potassium phosphate, 100 mM NaCl, 3.5 mM 2-mercaptoethanol, pH: 6.8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2015 Dec 10
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res (2019)
Yadav DK, Zigáčková D, Zlobina M, Klumpler T, Beaumont C, Kubíčková M, Vaňáčová Š, Lukavsky PJ
RgGuinier 1.7 nm
Dmax 6.0 nm
VolumePorod 21 nm3

SASDF39 – Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 - in complex with STAU1 binding site within the ADP-ribosylation factor1

UniProt ID: None (None-None) ADP-ribosylation factor1 - short

UniProt ID: O95793 (183-355) Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4
ADP-ribosylation factor1 - shortDouble-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 experimental SAS data
OTHER model
Sample: ADP-ribosylation factor1 - short monomer, 11 kDa Homo sapiens RNA
Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 monomer, 20 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate buffer, 300 mM NaCl, 500 mM imidazole, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2018 May 29
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res (2019)
Yadav DK, Zigáčková D, Zlobina M, Klumpler T, Beaumont C, Kubíčková M, Vaňáčová Š, Lukavsky PJ
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDF49 – Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 - in complex with STAU1 binding site within the ADP-ribosylation factor1 - long

UniProt ID: O95793 (183-355) Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4

UniProt ID: None (None-None) ADP-ribosylation factor1 - long
Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4ADP-ribosylation factor1 - long experimental SAS data
Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 ADP-ribosylation factor1 - long Kratky plot
Sample: Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 monomer, 20 kDa Homo sapiens protein
ADP-ribosylation factor1 - long monomer, 16 kDa Homo sapiens RNA
Buffer: 50 mM potassium phosphate, 100 mM NaCl, 3.5 mM 2-mercaptoethanol, pH: 6.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Sep 20
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res (2019)
Yadav DK, Zigáčková D, Zlobina M, Klumpler T, Beaumont C, Kubíčková M, Vaňáčová Š, Lukavsky PJ
RgGuinier 2.5 nm
Dmax 7.0 nm
VolumePorod 53 nm3