SASBDB entries for UniProt ID:

SASDJB5 – Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT)

UniProt ID: Q9IK91 (1-406) Phosphoprotein
Phosphoprotein experimental SAS data
Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT) Rg histogram
Sample: Phosphoprotein monomer, 45 kDa Nipah henipavirus protein
Buffer: 20 mM Tris-HCl, 0.3 M NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 May 3
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Sci Rep 10(1):19574 (2020)
Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S
RgGuinier 6.2 nm
Dmax 23.0 nm
VolumePorod 210 nm3

SASDJG5 – SARS-CoV-2 Main Protease

UniProt ID: P0DTC1 (3264-3569) 3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a
3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a dimer, 68 kDa Severe acute respiratory … protein
Buffer: 50 mM Tris, 1 mM DTT, 1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at Rigaku BioSAXS-2000, University of British Columbia on 2020 Jun 1
Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site. Nat Commun 11(1):5877 (2020)
Lee J, Worrall LJ, Vuckovic M, Rosell FI, Gentile F, Ton AT, Caveney NA, Ban F, Cherkasov A, Paetzel M, Strynadka NCJ
RgGuinier 2.7 nm
Dmax 8.8 nm
VolumePorod 93 nm3

SASDJJ5 – Histone H2A:H2B:H3:H4 complex with aprataxin and polynucleotide kinase like factor (APLF) acidic domain

UniProt ID: Q8IW19 (449-511) Aprataxin and PNK-like factor (acidic domain)

UniProt ID: P84051 (2-124) Histone H2A

UniProt ID: P02283 (2-123) Histone H2B

UniProt ID: P02299 (2-136) Histone H3

UniProt ID: P84040 (2-103) Histone H4
Aprataxin and PNK-like factor (acidic domain)Histone H2AHistone H2BHistone H3Histone H4 experimental SAS data
DAMMIF model
Sample: Aprataxin and PNK-like factor (acidic domain) dimer, 15 kDa Homo sapiens protein
Histone H2A dimer, 26 kDa Drosophila melanogaster protein
Histone H2B dimer, 27 kDa Drosophila melanogaster protein
Histone H3 dimer, 30 kDa Drosophila melanogaster protein
Histone H4 dimer, 23 kDa Drosophila melanogaster protein
Buffer: 25 mM NaPi, 300 mM NaCl, 3% v/v glycerol, 1 mM DTT,, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 10
Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF. Sci Adv 8(30):eabo0517 (2022)
Corbeski I, Guo X, Eckhardt BV, Fasci D, Wiegant W, Graewert MA, Vreeken K, Wienk H, Svergun DI, Heck AJR, van Attikum H, Boelens R, Sixma TK, Mattiroli F, van Ingen H
RgGuinier 3.7 nm
Dmax 10.8 nm
VolumePorod 260 nm3

SASDJK5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to TC1 DNA

UniProt ID: P31483-2 (93-274) Nucleolysin TIA-1 isoform p40

UniProt ID: None (None-None) TC1
Nucleolysin TIA-1 isoform p40TC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 TC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
TC1 monomer, 3 kDa synthetic construct DNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.2 nm
Dmax 15.1 nm
VolumePorod 78 nm3

SASDJL5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to UC1 RNA

UniProt ID: P31483-2 (93-274) Nucleolysin TIA-1 isoform p40

UniProt ID: None (None-None) UC1
Nucleolysin TIA-1 isoform p40UC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 UC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
UC1 monomer, 3 kDa synthetic construct RNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 14.4 nm
VolumePorod 77 nm3

SASDJN5 – Isolated translocation domain of tetanus nerotoxin (TeNT/iHn)

UniProt ID: P04958 (459-863) Tetanus toxin (C467S)
Tetanus toxin (C467S) experimental SAS data
Isolated translocation domain of tetanus nerotoxin (TeNT/iHn) Rg histogram
Sample: Tetanus toxin (C467S) monomer, 46 kDa Clostridium tetani protein
Buffer: 10 mM HEPES 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL45XU, SPring-8 on 2018 Oct 20
Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses. J Struct Biol X 5:100045 (2021)
Zhang CM, Imoto Y, Hikima T, Inoue T
RgGuinier 3.0 nm
Dmax 12.1 nm
VolumePorod 54 nm3

SASDJP5 – Beltless isolated translocation domain of tetanus nerotoxin (TeNT/blHn)

UniProt ID: P04958 (564-864) Tetanus toxin
Tetanus toxin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tetanus toxin monomer, 35 kDa Clostridium tetani protein
Buffer: 10 mM HEPES 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL45XU, SPring-8 on 2018 Oct 20
Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses. J Struct Biol X 5:100045 (2021)
Zhang CM, Imoto Y, Hikima T, Inoue T
RgGuinier 2.9 nm
Dmax 11.3 nm
VolumePorod 42 nm3

SASDJS5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-monomer

UniProt ID: P36056 (17-628) Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial
Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data
DAMMIN model
Sample: Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial monomer, 70 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 1
Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae Acta Crystallographica Section D Structural Biology 77(6) (2021)
Alam J, Rahman F, Sah-Teli S, Venkatesan R, Koski M, Autio K, Hiltunen J, Kastaniotis A
RgGuinier 3.8 nm
Dmax 13.9 nm
VolumePorod 160 nm3

SASDJT5 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-dimer

UniProt ID: P36056 (17-628) dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial
dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data
DAMMIN model
Sample: Dimeric Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial dimer, 141 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 1
Expression and analysis of the SAM-dependent RNA methyltransferase Rsm22 from Saccharomyces cerevisiae Acta Crystallographica Section D Structural Biology 77(6) (2021)
Alam J, Rahman F, Sah-Teli S, Venkatesan R, Koski M, Autio K, Hiltunen J, Kastaniotis A
RgGuinier 5.0 nm
Dmax 18.2 nm
VolumePorod 516 nm3

SASDJW5 – Plasminogen activator inhibitor-1 (PAI-1) W175F bound to nanobody Nb93

UniProt ID: P05121 (24-402) Plasminogen activator inhibitor 1

UniProt ID: None (None-None) VHH-s-a93 (Ig module Nb93)
Plasminogen activator inhibitor 1VHH-s-a93 (Ig module Nb93) experimental SAS data
OTHER model
Sample: Plasminogen activator inhibitor 1 monomer, 43 kDa Homo sapiens protein
VHH-s-a93 (Ig module Nb93) monomer, 13 kDa Vicugna pacos protein
Buffer: 30 mM BIS-TRIS pH 5.5, 300 mM sodium chloride, 5% v/v glycerol, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Dec 5
Structural Insights into the Mechanism of a Nanobody That Stabilizes PAI-1 and Modulates Its Activity International Journal of Molecular Sciences 21(16):5859 (2020)
Sillen M, Weeks S, Strelkov S, Declerck P
RgGuinier 2.9 nm
Dmax 9.7 nm
VolumePorod 80 nm3