SASBDB entries for UniProt ID:

SASDGV4 – Model of the RH1-LZ1 domains of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

UniProt ID: Q9UPT6 (22-187) C-Jun-amino-terminal kinase-interacting protein 3
C-Jun-amino-terminal kinase-interacting protein 3 experimental SAS data
OTHER model
Sample: C-Jun-amino-terminal kinase-interacting protein 3 dimer, 40 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH: 7.1
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Sep 22
Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif. Sci Rep 9(1):16036 (2019)
Vilela F, Velours C, Chenon M, Aumont-Nicaise M, Campanacci V, Thureau A, Pylypenko O, Andreani J, Llinas P, Ménétrey J
RgGuinier 6.3 nm
Dmax 23.1 nm
VolumePorod 140 nm3

SASDGW4 – Model of the LZ1 domain of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

UniProt ID: Q9UPT6 (22-187) C-Jun-amino-terminal kinase-interacting protein 3
C-Jun-amino-terminal kinase-interacting protein 3 experimental SAS data
OTHER model
Sample: C-Jun-amino-terminal kinase-interacting protein 3 dimer, 40 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH: 7.1
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Sep 22
Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif. Sci Rep 9(1):16036 (2019)
Vilela F, Velours C, Chenon M, Aumont-Nicaise M, Campanacci V, Thureau A, Pylypenko O, Andreani J, Llinas P, Ménétrey J
RgGuinier 5.0 nm
Dmax 19.8 nm
VolumePorod 84 nm3

SASDGX4 – Aryl-hydrocarbon-interacting protein-like 1

UniProt ID: Q9NZN9 (None-None) Aryl-hydrocarbon-interacting protein-like 1(1-316)
Aryl-hydrocarbon-interacting protein-like 1(1-316) experimental SAS data
Aryl-hydrocarbon-interacting protein-like 1(1-316) Kratky plot
Sample: Aryl-hydrocarbon-interacting protein-like 1(1-316) monomer, 37 kDa Homo sapiens protein
Buffer: 50 mM Tris, 100 mM NaCl, 2.5 % glycerol and 6 mM DTT, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jul 17
Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory Pγ subunit of phosphodiesterase 6. J Biol Chem 294(43):15795-15807 (2019)
Yadav RP, Boyd K, Yu L, Artemyev NO
RgGuinier 2.6 nm
Dmax 9.1 nm
VolumePorod 60 nm3

SASDGY4 – Beta-amylase 2, chloroplastic (AtBAM2)

UniProt ID: O65258 (56-542) Beta-amylase 2, chloroplastic
Beta-amylase 2, chloroplastic experimental SAS data
YASARA model
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 308 nm3

SASDGZ4 – Beta-amylase 2, chloroplastic (AtBAM2) Ndel1

UniProt ID: O65258 (86-542) Beta-amylase 2, chloroplastic
Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 215 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.4 nm
Dmax 11.0 nm
VolumePorod 272 nm3

SASDG25 – DNA repair protein Rad5 (with 6xhis and twin-strep tags)

UniProt ID: P32849 (2-1169) DNA repair protein RAD5
DNA repair protein RAD5 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: DNA repair protein RAD5 monomer, 138 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris, 150 mM KCl, 5 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 6
Conformational flexibility of fork-remodeling helicase Rad5 shown by full-ensemble hybrid methods. PLoS One 14(10):e0223875 (2019)
Gildenberg MS, Washington MT
RgGuinier 4.7 nm
Dmax 17.8 nm
VolumePorod 254 nm3

SASDG35 – Mothers against decapentaplegic homolog 2, S2MH1E3

UniProt ID: Q15796 (10-174) Mothers against decapentaplegic homolog 2
Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Jul 2
Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. Genes Dev 33(21-22):1506-1524 (2019)
Aragón E, Wang Q, Zou Y, Morgani SM, Ruiz L, Kaczmarska Z, Su J, Torner C, Tian L, Hu J, Shu W, Agrawal S, Gomes T, Márquez JA, Hadjantonakis AK, Macias MJ, Massagué J
RgGuinier 1.9 nm
Dmax 7.4 nm
VolumePorod 35 nm3

SASDG45 – Mothers against decapentaplegic homolog 2, S2MH1noE3

UniProt ID: Q15796-2 (10-143) Mothers against decapentaplegic homolog 2
Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 monomer, 16 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Jul 2
Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. Genes Dev 33(21-22):1506-1524 (2019)
Aragón E, Wang Q, Zou Y, Morgani SM, Ruiz L, Kaczmarska Z, Su J, Torner C, Tian L, Hu J, Shu W, Agrawal S, Gomes T, Márquez JA, Hadjantonakis AK, Macias MJ, Massagué J
RgGuinier 1.7 nm
Dmax 6.6 nm
VolumePorod 31 nm3

SASDG55 – Deglycosylated latency associated peptide, LAP (TGFB-1)

UniProt ID: P01137 (30-277) Latency associated peptide
Latency associated peptide experimental SAS data
Latency associated peptide Kratky plot
Sample: Latency associated peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 20
Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states IUCrJ 7(2) (2020)
Stachowski T, Snell M, Snell E
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 129 nm3

SASDG85 – Wild-type full-length Liver Receptor Homolog-1/Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha peptide complex bound to the CYP7A1 promoter oligonucleotide duplex.

UniProt ID: O00482 (1-541) Liver Receptor Homolog-1

UniProt ID: None (None-None) Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha

UniProt ID: None (None-None) CYP7A1 Promoter Forward

UniProt ID: None (None-None) CYP7A1 Promoter Reverse
Liver Receptor Homolog-1Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 AlphaCYP7A1 Promoter ForwardCYP7A1 Promoter Reverse experimental SAS data
Liver Receptor Homolog-1 Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha CYP7A1 Promoter Forward CYP7A1 Promoter Reverse Kratky plot
Sample: Liver Receptor Homolog-1 monomer, 64 kDa Homo sapiens protein
Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha monomer, 2 kDa Homo sapiens protein
CYP7A1 Promoter Forward monomer, 4 kDa Homo sapiens DNA
CYP7A1 Promoter Reverse monomer, 4 kDa Homo sapiens DNA
Buffer: 20 mM TRIS, 150 mM NaCl, 2% v/v glycerol, 0.5 mM CHAPS, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 26
Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function. Structure (2020)
Seacrist CD, Kuenze G, Hoffmann RM, Moeller BE, Burke JE, Meiler J, Blind RD
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 76 nm3