SASBDB entries for UniProt ID:

SASDVC5 – SEC-SAXS data of phosphorylated estrogen receptor alpha (pSer118), N-terminal domain (NTD) at pH 7.4

UniProt ID: P03372 (1-184) Estrogen receptor
Estrogen receptor experimental SAS data
Estrogen receptor Kratky plot
Sample: Estrogen receptor monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 0.05 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2024 Jul 17
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.6 nm
Dmax 16.0 nm
VolumePorod 70 nm3

SASDVL5 – Small EDRK-rich factor 1 (SERF1a)

UniProt ID: O75920-2 (1-62) Isoform Short of Small EDRK-rich factor 1
Isoform Short of Small EDRK-rich factor 1 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Mar 11
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 9 nm3

SASDVR5 – Small EDRK-rich factor 1 (SERF1a) bound to NT17 peptide

UniProt ID: O75920-2 (1-62) Isoform Short of Small EDRK-rich factor 1

UniProt ID: None (None-None) NT17
Isoform Short of Small EDRK-rich factor 1NT17 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
NT17 dimer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm

SASDVS5 – Small EDRK-rich factor 1 (SERF1a) bound to HTT-3 peptide

UniProt ID: O75920-2 (1-62) Isoform Short of Small EDRK-rich factor 1

UniProt ID: None (None-None) HTT3
Isoform Short of Small EDRK-rich factor 1HTT3 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 9 nm3

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