SASBDB entries for UniProt ID:

SASDTY4 – F-actin - Skeletal muscle actin from Oryctolagus cuniculus: fibrillar actin

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
DAMMIF model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 1.0 mM ATP, 50 mM KCl, 2 mM MgCl2, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 1
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 15.7 nm
Dmax 60.0 nm
VolumePorod 4710 nm3

SASDTZ4 – I-actin - Skeletal muscle actin from Oryctolagus cuniculus: oligomer of time-inactivated actin (peak SEC fraction)

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris/Tris-HCl, 2.0 mM EDTA, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Nov 16
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 4.9 nm
Dmax 22.0 nm
VolumePorod 549 nm3

SASDT25 – G- / I-actin mixture - Skeletal muscle actin from Oryctolagus cuniculus: mixture of globular actin monomers and inactivated actin monomers and dimers

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 5
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 84 nm3

SASDT35 – N-cadherin extracellular domains EC1-EC5

UniProt ID: P15116 (160-714) Cadherin-2
Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 dimer, 123 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 8.8 nm
Dmax 40.0 nm
VolumePorod 496 nm3

SASDT45 – N-cadherin extracellular domains EC4-EC5

UniProt ID: P15116 (490-702) Cadherin-2
Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 monomer, 24 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 3.4 nm
Dmax 12.6 nm
VolumePorod 63 nm3

SASDT55 – Non-structural protein 1 (NS1B, C-terminal) with 5' PPP hairpin RNA

UniProt ID: X2C382 (141-281) Non-structural protein 1

UniProt ID: None (None-None) 5’ppp ds10 HP RNA
Non-structural protein 15’ppp ds10 HP RNA experimental SAS data
HADDOCK model
Sample: Non-structural protein 1 monomer, 16 kDa Influenza B virus protein
5’ppp ds10 HP RNA monomer, 8 kDa RNA
Buffer: 40 mM ammonium acetate, pH 5.5, 225 mM NaCl, 5 mM CaCl2, 0.02% NaN3, 50 mM arginine, pH: 5.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Aug 6
The NS1 protein of influenza B virus binds 5’-triphosphorylated dsRNA to suppress RIG-I activation and the host antiviral response (2024)
Woltz R, Schweibenz B, Tsutakawa S, Zhao C, Ma L, Shurina B, Hura G, John R, Vorobiev S, Swapna G, Solotchi M, Tainer J, Krug R, Patel S, Montelione G
RgGuinier 2.0 nm
Dmax 6.9 nm
VolumePorod 28 nm3

SASDT65 – Non-structural protein 1 (NS1B, C-terminal) plus double stranded RNA

UniProt ID: X2C382 (141-281) Non-structural protein 1

UniProt ID: None (None-None) RNA top strand

UniProt ID: None (None-None) RNA bottom strand
Non-structural protein 1RNA top strandRNA bottom strand experimental SAS data
HADDOCK model
Sample: Non-structural protein 1 monomer, 16 kDa Influenza B virus protein
RNA top strand monomer, 5 kDa RNA
RNA bottom strand monomer, 5 kDa RNA
Buffer: 40 mM ammonium acetate, pH 5.5, 450 mM NaCl, 5 mM CaCl2, 0.02% NaN3, 50 mM arginine, pH: 5.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 May 18
The NS1 protein of influenza B virus binds 5’-triphosphorylated dsRNA to suppress RIG-I activation and the host antiviral response (2024)
Woltz R, Schweibenz B, Tsutakawa S, Zhao C, Ma L, Shurina B, Hura G, John R, Vorobiev S, Swapna G, Solotchi M, Tainer J, Krug R, Patel S, Montelione G
RgGuinier 2.8 nm
Dmax 10.3 nm
VolumePorod 23 nm3

SASDTC5 – Full-length E3 ubiquitin-protein ligase HACE1

UniProt ID: Q8IYU2 (1-909) E3 ubiquitin-protein ligase HACE1
E3 ubiquitin-protein ligase HACE1 experimental SAS data
GASBOR model
Sample: E3 ubiquitin-protein ligase HACE1 dimer, 205 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1 Nature Structural & Molecular Biology (2024)
Düring J, Wolter M, Toplak J, Torres C, Dybkov O, Fokkens T, Bohnsack K, Urlaub H, Steinchen W, Dienemann C, Lorenz S
RgGuinier 5.2 nm
Dmax 16.4 nm
VolumePorod 379 nm3

SASDTD5 – N-terminally truncated E3 ubiquitin-protein ligase HACE1

UniProt ID: Q8IYU2 (22-909) E3 ubiquitin-protein ligase HACE1
E3 ubiquitin-protein ligase HACE1 experimental SAS data
MULTIFOXS model
Sample: E3 ubiquitin-protein ligase HACE1 monomer, 100 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1 Nature Structural & Molecular Biology (2024)
Düring J, Wolter M, Toplak J, Torres C, Dybkov O, Fokkens T, Bohnsack K, Urlaub H, Steinchen W, Dienemann C, Lorenz S
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 219 nm3

SASDTK5 – Heme acquisition system protein A (39.9 kDa dimer from Pseudomonas protegens PF-5)

UniProt ID: Q4K5N8 (1-183) Heme acquisition protein HasAp
Heme acquisition protein HasAp experimental SAS data
DAMMIN model
Sample: Heme acquisition protein HasAp dimer, 38 kDa Pseudomonas fluorescens (strain … protein
Buffer: 50 mM CHES, 5 % glycerol, pH: 9.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2023 Feb 24
Heme-substituted protein assembly bridged by synthetic porphyrin: achieving controlled configuration while maintaining rotational freedom RSC Advances 14(13):8829-8836 (2024)
Inaba H, Shisaka Y, Ariyasu S, Sakakibara E, Ueda G, Aiba Y, Shimizu N, Sugimoto H, Shoji O
RgGuinier 2.8 nm
Dmax 9.1 nm
VolumePorod 54 nm3