SASBDB entries for UniProt ID:

SASDJ42 – Pentameric assembly of condensin complex subunits 1 and 2 (Ycs4-Brn1L-Brn1C) with subunits of the SMC hinge domain-containing protein (Smc4hd)

UniProt ID: G0SB82 (3-1222) Condensin complex subunit 1

UniProt ID: G0SBJ6 (225-418) Condensin complex subunit 2, 225-418

UniProt ID: G0SBJ6 (776-898) Condensin complex subunit 2, 776-898

UniProt ID: G0S2G2 (263-466) SMC hinge domain-containing protein, 263-466

UniProt ID: G0S2G2 (1367-1542) SMC hinge domain-containing protein, 1367-1542
Condensin complex subunit 1Condensin complex subunit 2, 225-418Condensin complex subunit 2, 776-898SMC hinge domain-containing protein, 263-466SMC hinge domain-containing protein, 1367-1542 experimental SAS data
MONSA model
Sample: Condensin complex subunit 1 monomer, 137 kDa Chaetomium thermophilum protein
Condensin complex subunit 2, 225-418 monomer, 21 kDa Chaetomium thermophilum protein
Condensin complex subunit 2, 776-898 monomer, 14 kDa Chaetomium thermophilum protein
SMC hinge domain-containing protein, 263-466 monomer, 22 kDa Chaetomium thermophilum protein
SMC hinge domain-containing protein, 1367-1542 monomer, 20 kDa Chaetomium thermophilum protein
Buffer: 25 mM Tris, 300 mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Nov 20
Molecular flexibility of the condensin subunit Ycs4 is modulated by kleisin binding
Karen Manalastas-Cantos
RgGuinier 5.1 nm
Dmax 17.9 nm
VolumePorod 355 nm3

SASDJ52 – DNA repair protein XRCC1ΔN monomer/dimer

UniProt ID: P18887 (294-633) DNA repair protein XRCC1ΔN
DNA repair protein XRCC1ΔN experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1ΔN dimer, 76 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Jul 15
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 170 nm3

SASDJ62 – DNA repair protein XRCC1 monomer /dimer

UniProt ID: P18887 (1-633) DNA repair protein XRCC1
DNA repair protein XRCC1 experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1, 69 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 19
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.3 nm
Dmax 26.9 nm
VolumePorod 330 nm3

SASDJ72 – DNA Ligase IIIα monomer/dimer

UniProt ID: P49916 (88-1009) DNA ligase 3 (DNA ligase III alpha)
DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA ligase 3 (DNA ligase III alpha), Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Mar 31
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.1 nm
Dmax 21.0 nm
VolumePorod 240 nm3

SASDJ82 – DNA repair protein XRCC1 - DNA Ligase IIIα complex

UniProt ID: P18887 (1-633) DNA repair protein XRCC1

UniProt ID: P49916 (88-1009) DNA ligase 3 (DNA ligase III alpha)
DNA repair protein XRCC1DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1, 69 kDa Homo sapiens protein
DNA ligase 3 (DNA ligase III alpha), Homo sapiens protein
Buffer: 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM MgCl₂,  0.2 mM PMSF, 1 mM benzamidine, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Aug 18
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.2 nm
Dmax 27.9 nm
VolumePorod 675 nm3

SASDJ92 – S. epidermidis extracellular matrix binding protein (Embp) F-repeats

UniProt ID: Q5HPA2 (None-None) Extracellular matrix binding protein F-repeats
Extracellular matrix binding protein F-repeats experimental SAS data
SASREF model
Sample: Extracellular matrix binding protein F-repeats, 70 kDa Staphylococcus epidermidis protein
Buffer: 50 mM MES, 150 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 15
A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism. mBio 11(5) (2020)
Büttner H, Perbandt M, Kohler T, Kikhney A, Wolters M, Christner M, Heise M, Wilde J, Weißelberg S, Both A, Betzel C, Hammerschmidt S, Svergun D, Aepfelbacher M, Rohde H
RgGuinier 7.0 nm
Dmax 28.0 nm

SASDJA2 – S. epidermidis extracellular matrix binding protein (Embp) FG-repeats

UniProt ID: Q5HPA2 (None-None) Extracellular matrix binding protein FG-repeats
Extracellular matrix binding protein FG-repeats experimental SAS data
EOM/RANCH model
Sample: Extracellular matrix binding protein FG-repeats, 85 kDa Staphylococcus epidermidis protein
Buffer: PBS, 136.5 mM NaCl, 2.65 mM KCl, 8.3 mM Na2HPO4, 2.65 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 14
A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism. mBio 11(5) (2020)
Büttner H, Perbandt M, Kohler T, Kikhney A, Wolters M, Christner M, Heise M, Wilde J, Weißelberg S, Both A, Betzel C, Hammerschmidt S, Svergun D, Aepfelbacher M, Rohde H
RgGuinier 10.7 nm
Dmax 40.0 nm

SASDJB2 – Restriction endonuclease R.AgeI in apo form, monomeric

UniProt ID: Q9KHV6 (1-278) Type-2 restriction enzyme AgeI
Type-2 restriction enzyme AgeI experimental SAS data
DAMMIN model
Sample: Type-2 restriction enzyme AgeI monomer, 31 kDa Thalassobius gelatinovorus protein
Buffer: 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl₂, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 14
Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA. Nucleic Acids Res 45(6):3547-3558 (2017)
Tamulaitiene G, Jovaisaite V, Tamulaitis G, Songailiene I, Manakova E, Zaremba M, Grazulis S, Xu SY, Siksnys V
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 53 nm3

SASDJC2 – Restriction endonuclease R.AgeI complex with cognate DNA

UniProt ID: Q9KHV6 (1-278) Type-2 restriction enzyme AgeI

UniProt ID: None (None-None) Cognate DNA oligoduplex with 5'-T overhang
Type-2 restriction enzyme AgeICognate DNA oligoduplex with 5'-T overhang experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Type-2 restriction enzyme AgeI dimer, 61 kDa Thalassobius gelatinovorus protein
Cognate DNA oligoduplex with 5'-T overhang dimer, 8 kDa DNA
Buffer: 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl₂, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 14
Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA. Nucleic Acids Res 45(6):3547-3558 (2017)
Tamulaitiene G, Jovaisaite V, Tamulaitis G, Songailiene I, Manakova E, Zaremba M, Grazulis S, Xu SY, Siksnys V
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 69 nm3

SASDJD2 – Human respiratory syncytial virus A (RSV) phosphoprotein oligomerization domain

UniProt ID: P12579 (127-163) Phosphoprotein
Phosphoprotein experimental SAS data
MULTIFOXS model
Sample: Phosphoprotein tetramer, 18 kDa Respiratory syncytial virus protein
Buffer: 20 mM Na phosphate 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Jun 21
A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein Biomolecules 11(8):1225 (2021)
Cardone C, Caseau C, Bardiaux B, Thureaux A, Galloux M, Bajorek M, Eléouët J, Litaudon M, Bontems F, Sizun C
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 33 nm3