SASBDB entries for UniProt ID:

SASDXH4 – Mouse complex murine Immunoglobulin E (IgE) antibody with profilin (without HisTAG)

UniProt ID: None (None-None) Murine Immunoglobulin E (IgE) antibodies

UniProt ID: Q9STB6 (1-131) Profilin-2
Murine Immunoglobulin E (IgE) antibodiesProfilin-2 experimental SAS data
SREFLEX model
Sample: Murine Immunoglobulin E (IgE) antibodies monomer, 165 kDa Mus musculus protein
Profilin-2 monomer, 18 kDa Hevea brasiliensis protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 8.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2025 Apr 11
Allergen-induced structural rearrangements in IgE: insights from SAXS and molecular dynamics. Int J Biol Macromol :147658 (2025)
Gómez-Velasco H, García-Ramírez B, Siliqi D, Graewert MA, Quintero-Martinez A, Ortega E, Rodríguez-Romero A
RgGuinier 5.7 nm
Dmax 19.9 nm
VolumePorod 450 nm3

SASDBF6 – Deglycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

UniProt ID: P20917 (20-508) Myelin-associated glycoprotein Ig domains 1-5
Myelin-associated glycoprotein Ig domains 1-5 experimental SAS data
NONE model
Sample: Myelin-associated glycoprotein Ig domains 1-5 dimer, 108 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.3 nm
Dmax 25.5 nm
VolumePorod 166 nm3

SASDBP6 – Nucleolysin TIA-1 isoform p40 in complex with ACTCCTTTTT DNA

UniProt ID: P31483-2 (93-274) Nucleolysin TIA-1 isoform p40

UniProt ID: (None-None) DNA (ACTCCTTTTT)
Nucleolysin TIA-1 isoform p40DNA (ACTCCTTTTT) experimental SAS data
Nucleolysin TIA-1 isoform p40 DNA (ACTCCTTTTT) Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
DNA (ACTCCTTTTT) monomer, 1 kDa DNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
TIA-1 RRM23 binding and recognition of target oligonucleotides. Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 32 nm3

SASDBZ9 – Immunoglobulin domains 4,5,6,7 of Nucleoporin Pom152 (Pom152 Ig-4,5,6,7: amino acids 718-1148)

UniProt ID: P39685 (None-None) Nucleoporin POM152
Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 49 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 4.3 nm
Dmax 15.4 nm
VolumePorod 67 nm3

SASDCV4 – Collagenase ColG s2s3as3b at pCa 6

UniProt ID: Q9X721 (787-1118) Collagenase ColG segement s2s3as3b
Collagenase ColG segement s2s3as3b experimental SAS data
DAMMIF model
Sample: Collagenase ColG segement s2s3as3b monomer, 37 kDa Hathewaya histolytica protein
Buffer: 10mM HEPES 100mM NaCl 0.2mM EGTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ - Induced Structural Change of Multi-Domain Collagen Binding Segments of Collagenases ColG and ColH from Hathewaya histolytica University of Arkansas Dissertation - (2018)
Christopher E Ruth
RgGuinier 3.6 nm
Dmax 15.2 nm
VolumePorod 41 nm3

SASDEV3 – Senescence-associated E3 ubiquitin ligase 1, 0.6 mg/ml

UniProt ID: Q9LM76 (None-None) Senescence-associated E3 ubiquitin ligase 1
Senescence-associated E3 ubiquitin ligase 1 experimental SAS data
SASREF MX model
Sample: Senescence-associated E3 ubiquitin ligase 1 tetramer, 355 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 250 mM NaCl, pH: 9
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 2
Senescence-associated ubiquitin ligase 1 (SAUL1)
Haifa El Kilani, Al Kikhney
RgGuinier 4.6 nm
Dmax 17.2 nm
VolumePorod 230 nm3

SASDEX3 – DNA ligase A (MtbLigA) complexed with exodeoxyribonuclease III protein (MtbXthA) in presence of nicked ds DNA

UniProt ID: P9WNV1 (None-None) DNA ligase A

UniProt ID: A0A0T9L251 (1-291) Probable exodeoxyribonuclease III protein XthA

UniProt ID: None (None-None) Nicked DNA
DNA ligase AProbable exodeoxyribonuclease III protein XthANicked DNA experimental SAS data
DAMFILT model
Sample: DNA ligase A monomer, 76 kDa Mycobacterium tuberculosis protein
Probable exodeoxyribonuclease III protein XthA monomer, 33 kDa Mycobacterium tuberculosis protein
Nicked DNA monomer, 8 kDa DNA
Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 May 13
M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair. Nucleic Acids Res (2020)
Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R
RgGuinier 4.5 nm
Dmax 17.1 nm
VolumePorod 117 nm3

SASDEY5 – Albumin-insulin detemir 2:12 complex, P1 symmetry

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)

UniProt ID: P01308 (None-None) Insulin detemir (Levemir(R), Novo Nordisk A/S)
Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)Insulin detemir (Levemir(R), Novo Nordisk A/S) experimental SAS data
SASREF CV model
Sample: Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) monomer, 66 kDa protein
Insulin detemir (Levemir(R), Novo Nordisk A/S) dodecamer, 71 kDa protein
Buffer: 8.8 mM Na2HPO4, 10.6 mM m-cresol, 12.2 mM phenol, 140.9 mM glycerol, 56.9 mM NaCl, pH: 7.4
Experiment: SAXS data collected at I911-4, MAX IV on 2015 Sep 25
Solution structures of long-acting insulin analogues and their complexes with albumin. Acta Crystallogr D Struct Biol 75(Pt 3):272-282 (2019)
Ryberg LA, Sønderby P, Barrientos F, Bukrinski JT, Peters GHJ, Harris P
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 309 nm3

SASDE29 – Interleukin-1 receptor accessory protein ectodomain with RI linker

UniProt ID: Q9NPH3 (21-348) Interleukin-1 receptor accessory protein ectodomain with RI linker
Interleukin-1 receptor accessory protein ectodomain with RI linker experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor accessory protein ectodomain with RI linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Aug 11
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.0 nm
Dmax 10.4 nm
VolumePorod 76 nm3

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

UniProt ID: P11532 (1461-1973) Dystrophin (R11-15 human dystrophin fragment)
Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.1 nm
Dmax 29.6 nm
VolumePorod 231 nm3