SASBDB entries for UniProt ID:

SASDXD6 – Ubiquitin C-terminal hydrolase (UCH) domain of BAP1

UniProt ID: Q92560 (1-238) Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type experimental SAS data
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type Kratky plot
Sample: Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type monomer, 27 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Jun 23
Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR
Yong-Sheng Wang
RgGuinier 2.1 nm
Dmax 8.0 nm
VolumePorod 35 nm3

SASDXE6 – Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 point mutation (L49V)

UniProt ID: Q92560 (1-238) Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V experimental SAS data
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V Kratky plot
Sample: Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V monomer, 27 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Jun 23
Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR
Yong-Sheng Wang
RgGuinier 2.2 nm
Dmax 8.7 nm
VolumePorod 36 nm3

SASDXF3 – Multi-domain human O-GlcNAcase

UniProt ID: O60502 (11-766) Protein O-GlcNAcase
Protein O-GlcNAcase experimental SAS data
ALPHAFOLD model
Sample: Protein O-GlcNAcase dimer, 163 kDa Homo sapiens protein
Buffer: 25 mM Tris buffer, 150 mM NaCl, and 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2023 Jun 22
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms Nature Communications 16(1) (2025)
Hansen S, Bartual S, Yuan H, Raimi O, Gorelik A, Ferenbach A, Lytje K, Pedersen J, Drace T, Boesen T, van Aalten D
RgGuinier 5.4 nm
Dmax 18.9 nm
VolumePorod 443 nm3

SASDXL6 – Histone deacetylase 5 (HDAC5)

UniProt ID: Q9UQL6 (655-1122) Histone deacetylase 5
Histone deacetylase 5 experimental SAS data
Histone deacetylase 5 Kratky plot
Sample: Histone deacetylase 5 monomer, 51 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM KCl, 1 mM DTT,, pH: 7.5
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2024 Feb 29
In vitro characterization of the catalytic domain of human histone deacetylase 5 Scientific Reports (2026)
Mammen C, Hornung F, Anzenhofer C, Schumacher J, Reiners J, Li J, Mazzone F, Bilsing F, Kassack M, Kurz T, Smits S
RgGuinier 2.8 nm
Dmax 10.1 nm
VolumePorod 82 nm3

SASDX67 – Non Structural Protein 15 in complex with RNA 9mer

UniProt ID: P0DTD1 (6465-6798) Non structural Protein 15
Non structural Protein 15 experimental SAS data
Non structural Protein 15 Kratky plot
Sample: Non structural Protein 15 monomer, 251 kDa Severe acute respiratory … protein
Buffer: 20mM HEPES, 150mM Nacl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2024 Jun 14
Non Structural Protein 15 in Complex with RNA 9mer Oligo of SARS CoV 2
Hira Singh Gariya
RgGuinier 4.7 nm
Dmax 13.8 nm
VolumePorod 356 nm3

SASDX77 – Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker

UniProt ID: Q9ET54 (1022-1257) Palladin Ig3-45Linker_Ig4
Palladin Ig3-45Linker_Ig4 experimental SAS data
Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker Rg histogram
Sample: Palladin Ig3-45Linker_Ig4 monomer, 22 kDa Mus musculus protein
Buffer: HEPES, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
The role of linker length and composition in actin binding and bundling by palladin. Biochem J 483(3):301-318 (2026)
Sargent RA, Bradford CW, Hughes LM, Ta NH, Limpiado MJ, Vattepu R, Beck MR
RgGuinier 2.9 nm
Dmax 10.4 nm
VolumePorod 27 nm3

SASDXU7 – N-Myc proto-oncogene protein residues 1-69

UniProt ID: P04198 (1-69) N-myc proto-oncogene protein, residues 1-69
N-myc proto-oncogene protein, residues 1-69 experimental SAS data
N-myc proto-oncogene protein, residues 1-69 Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-69 monomer, 8 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.4 nm
Dmax 11.0 nm
VolumePorod 12 nm3

SASDXV7 – N-Myc proto-oncogene protein, residues 1-100

UniProt ID: P04198 (1-100) N-myc proto-oncogene protein, residues 1-100
N-myc proto-oncogene protein, residues 1-100 experimental SAS data
N-myc proto-oncogene protein, residues 1-100 Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-100 monomer, 11 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 3.0 nm
Dmax 13.0 nm
VolumePorod 22 nm3

SASDXW7 – Kinase domain of Aurora kinase A mutant C290A:C393A

UniProt ID: O14965 (122-403) Aurora kinase A mutant C290A:C393A
Aurora kinase A mutant C290A:C393A experimental SAS data
Aurora kinase A mutant C290A:C393A Kratky plot
Sample: Aurora kinase A mutant C290A:C393A monomer, 33 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.2 nm
Dmax 9.5 nm
VolumePorod 59 nm3

SASDXX7 – N-Myc proto-oncogene residues 1-69 in complex with Aurora kinase A mutant C290A:C393A

UniProt ID: P04198 (1-69) N-myc proto-oncogene protein, residues 1-69

UniProt ID: O14965 (122-403) Aurora kinase A mutant C290A:C393A
N-myc proto-oncogene protein, residues 1-69Aurora kinase A mutant C290A:C393A experimental SAS data
N-myc proto-oncogene protein, residues 1-69 Aurora kinase A mutant C290A:C393A Kratky plot
Sample: N-myc proto-oncogene protein, residues 1-69 monomer, 8 kDa Homo sapiens protein
Aurora kinase A mutant C290A:C393A monomer, 33 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Nov 28
The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A. Nat Commun (2026)
Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
RgGuinier 2.5 nm
Dmax 10.2 nm
VolumePorod 62 nm3