SASBDB entries for UniProt ID:

SASDUL7 – Lcl C-terminal domain K504A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K504A)
HbP1 (K504A) experimental SAS data
HbP1 (K504A) Kratky plot
Sample: HbP1 (K504A) 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 106 nm3

SASDUM7 – Lcl C-terminal domain K515A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K515A)
HbP1 (K515A) experimental SAS data
HbP1 (K515A) Kratky plot
Sample: HbP1 (K515A) 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 9.8 nm
VolumePorod 105 nm3

SASDUN7 – Lcl C-terminal domain K520A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K520A)
HbP1 (K520A) experimental SAS data
HbP1 (K520A) Kratky plot
Sample: HbP1 (K520A) 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 9.8 nm
VolumePorod 100 nm3

SASDUP7 – Lcl C-terminal domain D521A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (D521A)
HbP1 (D521A) experimental SAS data
HbP1 (D521A) Kratky plot
Sample: HbP1 (D521A) 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 9.8 nm
VolumePorod 108 nm3

SASDUQ7 – Lcl C-terminal domain K526A mutant

UniProt ID: E7BLH6 (387-536) HbP1 (K526A)
HbP1 (K526A) experimental SAS data
HbP1 (K526A) Kratky plot
Sample: HbP1 (K526A) 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 9.5 nm
VolumePorod 104 nm3

SASDUR7 – Infectious Bursal Disease Virus VP3 (central domains at pH 8.0)

UniProt ID: P61825 (844-976) Structural polyprotein (Capsid protein VP3: K947R; Δ756-843; Δ977-1012)
Structural polyprotein (Capsid protein VP3: K947R; Δ756-843; Δ977-1012) experimental SAS data
Structural polyprotein (Capsid protein VP3: K947R; Δ756-843; Δ977-1012) Kratky plot
Sample: Structural polyprotein (Capsid protein VP3: K947R; Δ756-843; Δ977-1012) monomer, 18 kDa Infectious bursal disease … protein
Buffer: 50 mM TRIS, 500 mM NaCl, 2 mM DTT,, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
Infectious Bursal Disease Virus VP3
Diego Ferrero
RgGuinier 2.5 nm
Dmax 10.0 nm
VolumePorod 21 nm3

SASDUS7 – Infectious Bursal Disease Virus VP3 (C-terminal deleted at pH 8.0)

UniProt ID: P61825 (756-976) Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012)
Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) experimental SAS data
Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) Kratky plot
Sample: Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) dimer, 55 kDa Infectious bursal disease … protein
Buffer: 50 mM TRIS, 500 mM NaCl, 2 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 1
Infectious Bursal Disease Virus VP3
Diego Ferrero
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 110 nm3

SASDUT7 – The tandem SH2 domains of Tyrosine-protein kinase SYK

UniProt ID: P43405 (6-269) Tyrosine-protein kinase SYK
Tyrosine-protein kinase SYK experimental SAS data
Tyrosine-protein kinase SYK Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.2 nm
Dmax 6.9 nm
VolumePorod 49 nm3

SASDUU7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound FCER1G diphospho-ITAM peptide

UniProt ID: P43405 (6-269) Tyrosine-protein kinase SYK

UniProt ID: P30273 (62-81) High affinity immunoglobulin epsilon receptor subunit gamma
Tyrosine-protein kinase SYKHigh affinity immunoglobulin epsilon receptor subunit gamma experimental SAS data
Tyrosine-protein kinase SYK High affinity immunoglobulin epsilon receptor subunit gamma Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
High affinity immunoglobulin epsilon receptor subunit gamma monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 54 nm3

SASDUV7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound CD3G diphospho-ITAM peptide

UniProt ID: P43405 (6-269) Tyrosine-protein kinase SYK

UniProt ID: P09693 (157-176) T-cell surface glycoprotein CD3 gamma chain
Tyrosine-protein kinase SYKT-cell surface glycoprotein CD3 gamma chain experimental SAS data
Tyrosine-protein kinase SYK T-cell surface glycoprotein CD3 gamma chain Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
T-cell surface glycoprotein CD3 gamma chain monomer, 3 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 56 nm3