SASBDB entries for UniProt ID:

SASDKN2 – Matrix protein from Newcastle disease virus at neutral pH

UniProt ID: P11206 (None-None) Matrix protein
Matrix protein experimental SAS data
DAMMIN model
Sample: Matrix protein, 40 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.5 nm

SASDKP2 – Matrix protein from Newcastle disease virus at acidic pH

UniProt ID: P11206 (None-None) Matrix protein
Matrix protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Matrix protein dimer, 79 kDa Newcastle disease virus … protein
Buffer: STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11
Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A
RgGuinier 3.3 nm

SASDKK3 – SEC-SAXS of Presequence Protease (PreP)

UniProt ID: Q5JRX3 (33-1036) Presequence protease, mitochondrial
Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.2 nm
Dmax 9.1 nm
VolumePorod 170 nm3

SASDKL3 – SEC-SAXS of Presequence Protease (PreP) with inhibitor MitoBloCK-60 (MB-60)

UniProt ID: Q5JRX3 (33-1036) Presequence protease, mitochondrial
Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 9.1 nm
VolumePorod 165 nm3

SASDKM3 – SEC-SAXS of Presequence Protease (PreP) with pre-sequence of citrate synthase (1-27)

UniProt ID: Q5JRX3 (33-1036) Presequence protease, mitochondrial

UniProt ID: O75390 (1-27) Citrate synthase, mitochondrial
Presequence protease, mitochondrialCitrate synthase, mitochondrial experimental SAS data
Presequence protease, mitochondrial Citrate synthase, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Citrate synthase, mitochondrial monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 8.7 nm
VolumePorod 165 nm3

SASDKN3 – SEC-SAXS of Presequence Protease (PreP) with Amyloid beta precursor protein (1-40)

UniProt ID: Q5JRX3 (33-1036) Presequence protease, mitochondrial

UniProt ID: P05067 (688-711) Amyloid-beta precursor protein
Presequence protease, mitochondrialAmyloid-beta precursor protein experimental SAS data
Presequence protease, mitochondrial Amyloid-beta precursor protein Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Amyloid-beta precursor protein monomer, 4 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.0 nm
Dmax 8.5 nm
VolumePorod 175 nm3

SASDKQ3 – Alpha domain of autotransporter adhesin Ag43a from Escherichia coli

UniProt ID: None (53-551) Alpha domain of Ag43a
Alpha domain of Ag43a experimental SAS data
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 3
Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms npj Biofilms and Microbiomes 8(1) (2022)
Vo J, Ortiz G, Totsika M, Lo A, Hancock S, Whitten A, Hor L, Peters K, Ageorges V, Caccia N, Desvaux M, Schembri M, Paxman J, Heras B
RgGuinier 4.6 nm
Dmax 18.0 nm
VolumePorod 87 nm3

SASDKR3 – Deuterated calmodulin bound to the HIV-1 MA protein

UniProt ID: P0DP33 (2-149) Calmodulin-1

UniProt ID: None (None-None) calcium ions

UniProt ID: P12497 (1-133) Gag-Pol polyprotein
Calmodulin-1calcium ionsGag-Pol polyprotein experimental SAS data
MONSA model
Sample: Calmodulin-1 monomer, 17 kDa Xenopus laevis protein
Calcium ions tetramer, 0 kDa
Gag-Pol polyprotein monomer, 15 kDa Human immunodeficiency virus … protein
Buffer: 50 mM MOPS, 5 mM CaCl2, 2 mM TCEP, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2010 Jun 23
Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. Biophys J 103(3):541-549 (2012)
Taylor JE, Chow JYH, Jeffries CM, Kwan AH, Duff AP, Hamilton WA, Trewhella J
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 55 nm3

SASDKS3 – The dimeric ectodomain of the alkali-sensing insulin receptor–related receptor (ectoIRR) at pH7

UniProt ID: P14616 (28-918) Insulin receptor-related protein
Insulin receptor-related protein experimental SAS data
CORAL model
Sample: Insulin receptor-related protein dimer, 201 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM Tris, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 22
The dimeric ectodomain of the alkali-sensing insulin receptor-related receptor (ectoIRR) has a droplike shape. J Biol Chem 294(47):17790-17798 (2019)
Shtykova EV, Petoukhov MV, Mozhaev AA, Deyev IE, Dadinova LA, Loshkarev NA, Goryashchenko AS, Bocharov EV, Jeffries CM, Svergun DI, Batishchev OV, Petrenko AG
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 444 nm3

SASDKT3 – The dimeric ectodomain of the alkali-sensing insulin receptor–related receptor (ectoIRR) at pH9

UniProt ID: P14616 (28-918) Insulin receptor-related protein
Insulin receptor-related protein experimental SAS data
CORAL model
Sample: Insulin receptor-related protein dimer, 201 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM Tris, pH: 9
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 22
The dimeric ectodomain of the alkali-sensing insulin receptor-related receptor (ectoIRR) has a droplike shape. J Biol Chem 294(47):17790-17798 (2019)
Shtykova EV, Petoukhov MV, Mozhaev AA, Deyev IE, Dadinova LA, Loshkarev NA, Goryashchenko AS, Bocharov EV, Jeffries CM, Svergun DI, Batishchev OV, Petrenko AG
RgGuinier 5.3 nm
Dmax 19.0 nm
VolumePorod 430 nm3