SASBDB entries for UniProt ID:

SASDQE5 – Nucleoside triphosphate pyrophosphohydrolase (1–185)

UniProt ID: P96379 (1-185) Nucleoside triphosphate pyrophosphohydrolase
Nucleoside triphosphate pyrophosphohydrolase experimental SAS data
DAMMIF model
Sample: Nucleoside triphosphate pyrophosphohydrolase dimer, 41 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2020 Dec 11
Structural analysis of the housecleaning nucleoside triphosphate pyrophosphohydrolase MazG from Mycobacterium tuberculosis Frontiers in Microbiology 14 (2023)
Wang S, Gao B, Chen A, Zhang Z, Wang S, Lv L, Zhao G, Li J
RgGuinier 2.7 nm
Dmax 8.4 nm
VolumePorod 64 nm3

SASDQF5 – Zinc finger protein 410 (ZNF410 full length)

UniProt ID: Q86VK4 (1-478) Zinc finger protein 410
Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.6 nm
Dmax 12.3 nm
VolumePorod 108 nm3

SASDQH5 – Zinc finger protein 410 (ZNF410 full length) bound to DNA

UniProt ID: Q86VK4 (1-478) Zinc finger protein 410

UniProt ID: None (None-None) DNA (Zinc finger protein 410 recognition sequence)
Zinc finger protein 410DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 4.4 nm
Dmax 14.3 nm
VolumePorod 76 nm3

SASDQJ5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers

UniProt ID: Q86VK4 (1-366) Zinc finger protein 410
Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 78 nm3

SASDQK5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers bound to DNA

UniProt ID: None (None-None) DNA (Zinc finger protein 410 recognition sequence)

UniProt ID: Q86VK4 (1-366) Zinc finger protein 410
DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Apr 25
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 14.1 nm
VolumePorod 63 nm3

SASDQL5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers

UniProt ID: Q86VK4 (217-478) Zinc finger protein 410
Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.0 nm
Dmax 9.6 nm
VolumePorod 58 nm3

SASDQM5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers bound to DNA

UniProt ID: None (None-None) DNA (Zinc finger protein 410 recognition sequence)

UniProt ID: Q86VK4 (217-478) Zinc finger protein 410
DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 11.9 nm
VolumePorod 52 nm3

SASDQN5 – Candida glabrata Metacaspase in 10 mM CaCl2

UniProt ID: Q6FPX9 (1-392) Metacaspase-1
Metacaspase-1 experimental SAS data
Metacaspase-1 Kratky plot
Sample: Metacaspase-1 monomer, 46 kDa Candida glabrata (strain … protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1% glycerol, 10 mM CaCl2, pH: 7.6
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 26
Structural and molecular determinants of Candida glabrata metacaspase maturation and activation by calcium. Commun Biol 5(1):1158 (2022)
Conchou L, Doumèche B, Galisson F, Violot S, Dugelay C, Diesis E, Page A, Bienvenu AL, Picot S, Aghajari N, Ballut L
RgGuinier 1.9 nm
Dmax 5.4 nm
VolumePorod 43 nm3

SASDQP5 – Phosphoprotein of Borna disease virus

UniProt ID: P0C799 (1-201) Phosphoprotein
Phosphoprotein experimental SAS data
Phosphoprotein of Borna disease virus Rg histogram
Sample: Phosphoprotein tetramer, 90 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 6.1 nm
Dmax 21.5 nm
VolumePorod 225 nm3

SASDQQ5 – Oligomerisation domain of phosphoprotein from Borna disease virus

UniProt ID: P0C799 (65-172) Phosphoprotein
Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 47 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.5 nm
Dmax 17.0 nm
VolumePorod 66 nm3