SASBDB entries for UniProt ID:

SASDVT5 – Marchantia polymorpha Auxin Response Factor 3

UniProt ID: A0A0G3FJH3 (52-470) Auxin response factor
Auxin response factor experimental SAS data
GASBOR model
Sample: Auxin response factor monomer, 46 kDa Marchantia polymorpha protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Dec 3
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1. Structure (2025)
Crespo I, Malfois M, Rienstra J, Tarrés-Solé A, van den Berg W, Weijers D, Boer DR
RgGuinier 2.6 nm
Dmax 6.2 nm
VolumePorod 59 nm3

SASDVU5 – Marchantia polymorpha Auxin Response Factor 3 in complex with high affinity DNA

UniProt ID: A0A0G3FJH3 (52-470) Auxin response factor

UniProt ID: None (None-None) High Affinity ARF binding sequence inverted repeat with 6 nucleotide spacing
Auxin response factorHigh Affinity ARF binding sequence inverted repeat with 6 nucleotide spacing experimental SAS data
SWISSMODEL model
Sample: Auxin response factor monomer, 46 kDa Marchantia polymorpha protein
High Affinity ARF binding sequence inverted repeat with 6 nucleotide spacing dimer, 12 kDa DNA
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Dec 3
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1. Structure (2025)
Crespo I, Malfois M, Rienstra J, Tarrés-Solé A, van den Berg W, Weijers D, Boer DR
RgGuinier 3.1 nm
Dmax 8.4 nm
VolumePorod 67 nm3

SASDVV5 – Arabidopsis thaliana Auxin Response Factor 1 in complex with high affinity DNA

UniProt ID: Q8L7G0 (1-355) Auxin response factor 1

UniProt ID: None (None-None) High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing
Auxin response factor 1High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing experimental SAS data
Auxin response factor 1 High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing Kratky plot
Sample: Auxin response factor 1 dimer, 81 kDa Arabidopsis thaliana protein
High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing dimer, 13 kDa DNA
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Dec 3
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1. Structure (2025)
Crespo I, Malfois M, Rienstra J, Tarrés-Solé A, van den Berg W, Weijers D, Boer DR
RgGuinier 3.6 nm
Dmax 10.5 nm
VolumePorod 136 nm3

SASDVW5 – alpha-amylase AMY3

UniProt ID: Q94A41 (57-887) Alpha-amylase 3, chloroplastic
Alpha-amylase 3, chloroplastic experimental SAS data
BILBOMD model
Sample: Alpha-amylase 3, chloroplastic dimer, 187 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 5.1 nm
Dmax 21.5 nm
VolumePorod 444 nm3

SASDVX5 – pseudoamylase BAM9

UniProt ID: Q8VYW2 (73-536) Inactive beta-amylase 9
Inactive beta-amylase 9 experimental SAS data
ALPHAFOLD model
Sample: Inactive beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 2.4 nm
Dmax 8.7 nm
VolumePorod 87 nm3

SASDVY5 – pseudoamylase BAM9 bound to alpha-amylase AMY3

UniProt ID: Q8VYW2 (73-536) Inactive beta-amylase 9

UniProt ID: Q94A41 (57-887) Alpha-amylase 3, chloroplastic
Inactive beta-amylase 9Alpha-amylase 3, chloroplastic experimental SAS data
BILBOMD model
Sample: Inactive beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein
Alpha-amylase 3, chloroplastic monomer, 94 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 5.0 nm
Dmax 25.5 nm
VolumePorod 380 nm3

SASDVZ5 – Human DNA repair protein RAD52 homolog (amino acids 1-212)

UniProt ID: P43351 (1-212) DNA repair protein RAD52 homolog
DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog decamer, 234 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% glycerol, 400 mM NaCl, 100 mM KCl, 1 mM EDTA, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS 1000, Eppley Structural Biology Facility, University of Nebraska Medical Center on 2014 Jul 25
A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52 Journal of Structural Biology 216(3):108115 (2024)
Struble L, Lovelace J, Borgstahl G
RgGuinier 4.1 nm
Dmax 11.8 nm
VolumePorod 375 nm3

SASDV26 – Human DNA repair protein RAD52 homolog (amino acids 1-303)

UniProt ID: P43351 (1-303) DNA repair protein RAD52 homolog
DNA repair protein RAD52 homolog experimental SAS data
DAMMIF model
Sample: DNA repair protein RAD52 homolog nonamer, 300 kDa Homo sapiens protein
Buffer: 20 mM Bis-Tris, 10% GLycerol, 400 mM NaCl, 100 mM KCl, 1mM EDTA, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS 1000, Eppley Structural Biology Facility, University of Nebraska Medical Center on 2014 Jul 25
A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52 Journal of Structural Biology 216(3):108115 (2024)
Struble L, Lovelace J, Borgstahl G
RgGuinier 4.8 nm
Dmax 18.3 nm
VolumePorod 782 nm3

SASDV46 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 33 nm3

SASDV56 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317

UniProt ID: P10636-8 (244-372) Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)

UniProt ID: A0A091E260 (1-77) Polyubiquitin-B
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B experimental SAS data
Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317 Rg histogram
Sample: Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A) monomer, 14 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Fukomys damarensis protein
Buffer: 100 mM NaCl, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain. Proc Natl Acad Sci U S A 122(15):e2425831122 (2025)
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
RgGuinier 3.3 nm
Dmax 13.3 nm
VolumePorod 41 nm3