SASBDB entries for UniProt ID:

SASDU67 – The C-terminal region of DNA repair protein XRCC4

UniProt ID: Q13426 (201-336) DNA repair protein XRCC4
DNA repair protein XRCC4 experimental SAS data
DNA repair protein XRCC4 Kratky plot
Sample: DNA repair protein XRCC4 monomer, 15 kDa Homo sapiens protein
Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Oct 20
Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. Nat Struct Mol Biol (2024)
Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F
RgGuinier 3.4 nm
Dmax 11.1 nm
VolumePorod 41 nm3

SASDU87 – Deglycosylated Fc gamma receptor IIb (CD32b) extracellular domain in complex with human IgG1 5C05 F(ab')

UniProt ID: P31994 (43-217) Low affinity immunoglobulin gamma Fc region receptor II-b

UniProt ID: None (None-None) Human IgG1 F(ab') 5C05
Low affinity immunoglobulin gamma Fc region receptor II-bHuman IgG1 F(ab') 5C05 experimental SAS data
MOLECULAR DYNAMICS FRAME model
Sample: Low affinity immunoglobulin gamma Fc region receptor II-b monomer, 20 kDa Homo sapiens protein
Human IgG1 F(ab') 5C05 monomer, 46 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 May 18
Antibody binding geometry and affinity control inhibitory FcγRIIB receptor signaling
Hayden Fisher
RgGuinier 3.5 nm
Dmax 14.0 nm
VolumePorod 95 nm3

SASDUA7 – Fc gamma receptor IIb (CD32b) extracellular domain in complex with human IgG1 6C11 F(ab')

UniProt ID: P31994 (43-217) Low affinity immunoglobulin gamma Fc region receptor II-b

UniProt ID: None (None-None) Human IgG1 F(ab') 6C11
Low affinity immunoglobulin gamma Fc region receptor II-bHuman IgG1 F(ab') 6C11 experimental SAS data
Low affinity immunoglobulin gamma Fc region receptor II-b Human IgG1 F(ab') 6C11 Kratky plot
Sample: Low affinity immunoglobulin gamma Fc region receptor II-b monomer, 20 kDa Homo sapiens protein
Human IgG1 F(ab') 6C11 monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 May 9
Antibody binding geometry and affinity control inhibitory FcγRIIB receptor signaling
Hayden Fisher
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 110 nm3

SASDUC7 – Deglycosylated Fc gamma receptor IIb (CD32b) extracellular domain in complex with human IgG1 6G11 F(ab')

UniProt ID: P31994 (43-217) Low affinity immunoglobulin gamma Fc region receptor II-b

UniProt ID: None (None-None) Human IgG1 F(ab') 6G11
Low affinity immunoglobulin gamma Fc region receptor II-bHuman IgG1 F(ab') 6G11 experimental SAS data
MOLECULAR DYNAMICS FRAME model
Sample: Low affinity immunoglobulin gamma Fc region receptor II-b monomer, 20 kDa Homo sapiens protein
Human IgG1 F(ab') 6G11 monomer, 25 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 9
Antibody binding geometry and affinity control inhibitory FcγRIIB receptor signaling
Hayden Fisher
RgGuinier 3.5 nm
Dmax 13.5 nm
VolumePorod 97 nm3

SASDUE7 – Fc gamma receptor IIb (CD32b) extracellular domain in complex with human IgG1 7C07 F(ab')

UniProt ID: P31994 (43-217) Low affinity immunoglobulin gamma Fc region receptor II-b

UniProt ID: None (None-None) Human IgG1 F(ab') 7C07
Low affinity immunoglobulin gamma Fc region receptor II-bHuman IgG1 F(ab') 7C07 experimental SAS data
Low affinity immunoglobulin gamma Fc region receptor II-b Human IgG1 F(ab') 7C07 Kratky plot
Sample: Low affinity immunoglobulin gamma Fc region receptor II-b monomer, 20 kDa Homo sapiens protein
Human IgG1 F(ab') 7C07 monomer, 25 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 5
Antibody binding geometry and affinity control inhibitory FcγRIIB receptor signaling
Hayden Fisher
RgGuinier 3.6 nm
Dmax 13.5 nm
VolumePorod 110 nm3

SASDUF7 – Deglycosylated Fc gamma receptor IIb (CD32b) extracellular domain in complex with human IgG1 6G08 F(ab')

UniProt ID: P31994 (43-217) Low affinity immunoglobulin gamma Fc region receptor II-b

UniProt ID: None (None-None) Human IgG1 F(ab') 6G08
Low affinity immunoglobulin gamma Fc region receptor II-bHuman IgG1 F(ab') 6G08 experimental SAS data
MOLECULAR DYNAMICS FRAME model
Sample: Low affinity immunoglobulin gamma Fc region receptor II-b monomer, 20 kDa Homo sapiens protein
Human IgG1 F(ab') 6G08 monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 14
Antibody binding geometry and affinity control inhibitory FcγRIIB receptor signaling
Hayden Fisher
RgGuinier 3.3 nm
Dmax 12.0 nm
VolumePorod 96 nm3

SASDUG7 – Wild type Lcl C-terminal domain

UniProt ID: E7BLH6 (387-536) HbP1
HbP1 experimental SAS data
HbP1 Kratky plot
Sample: HbP1 trimer, 56 kDa Legionella pneumophila protein
Buffer: 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA, pH:
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans. Nat Commun 15(1):4912 (2024)
Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.8 nm
Dmax 9.7 nm
VolumePorod 105 nm3

SASDUH7 – Lcl C-terminal domain R477A mutant - trimer

UniProt ID: E7BLH6 (387-536) HbP1 (R477A)
HbP1 (R477A) experimental SAS data
HbP1 (R477A) Kratky plot
Sample: HbP1 (R477A) trimer, 55 kDa Legionella pneumophila protein
Buffer: 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA, pH:
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans. Nat Commun 15(1):4912 (2024)
Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 79 nm3

SASDUJ7 – Lcl C-terminal domain R477A mutant - monomer

UniProt ID: E7BLH6 (387-536) HbP1 (R477A)
HbP1 (R477A) experimental SAS data
HbP1 (R477A) Kratky plot
Sample: HbP1 (R477A) monomer, 18 kDa Legionella pneumophila protein
Buffer: 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA, pH:
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans. Nat Commun 15(1):4912 (2024)
Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 1.9 nm
Dmax 6.4 nm
VolumePorod 33 nm3

SASDUK7 – Lcl C-terminal domain E503A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (E503A)
HbP1 (E503A) experimental SAS data
HbP1 (E503A) Kratky plot
Sample: HbP1 (E503A) trimer, 56 kDa Legionella pneumophila protein
Buffer: 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA, pH:
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans. Nat Commun 15(1):4912 (2024)
Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA
RgGuinier 2.8 nm
Dmax 9.9 nm
VolumePorod 106 nm3