SASBDB entries for UniProt ID:

SASDNU2 – Homodimerization of a membrane type 1 matrix metalloproteinase (MT1-MMP)

UniProt ID: P02790 (None-None) Hemopexin

UniProt ID: P02790 (None-None) Hemopexin
HemopexinHemopexin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Hemopexin monomer, 23 kDa Homo sapiens protein
Hemopexin dimer, 46 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM NaCl, 10 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 25
The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain Journal of Biological Chemistry 286(9):7587-7600 (2011)
Tochowicz A, Goettig P, Evans R, Visse R, Shitomi Y, Palmisano R, Ito N, Richter K, Maskos K, Franke D, Svergun D, Nagase H, Bode W, Itoh Y
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 48 nm3

SASDNV2 – The pro-convertase formed by human FB and cobra venom factor (CVF)

UniProt ID: Q91132 (None-None) Cobra venom factor
Cobra venom factor experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cobra venom factor monomer, 185 kDa Naja kaouthia protein
Buffer: 10 mM Tris 5 mM MgCl2 10 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 19
Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex The EMBO Journal 28(16):2469-2478 (2009)
Janssen B, Gomes L, Koning R, Svergun D, Koster A, Fritzinger D, Vogel C, Gros P
RgGuinier 4.6 nm
Dmax 15.0 nm
VolumePorod 384 nm3

SASDNZ2 – Tetrameric state of soluble endoglin receptor

UniProt ID: P17813 (27-256) Endoglin
Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin tetramer, 243 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
Le B, Franke D, Svergun D, Han T, Hwang H, Kim K
RgGuinier 7.6 nm
Dmax 26.0 nm
VolumePorod 434 nm3

SASDN23 – Homodimeric state of soluble endoglin receptor

UniProt ID: P17813 (27-256) Endoglin
Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin dimer, 121 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
Le B, Franke D, Svergun D, Han T, Hwang H, Kim K
RgGuinier 4.7 nm
Dmax 17.0 nm
VolumePorod 173 nm3

SASDN33 – Ternary Human Pex5p(C-terminal)-Pex14p(N)-PTS1 Complex (1:1:1 stoichiometry)

UniProt ID: P50542 (268-602) Peroxisomal targeting signal 1 receptor (C -terminal)

UniProt ID: O75381 (16-80) Peroxisomal membrane protein PEX14 (N-terminal)

UniProt ID: B4E0T2 (22-143) PTS1-BP
Peroxisomal targeting signal 1 receptor (C -terminal)Peroxisomal membrane protein PEX14 (N-terminal)PTS1-BP experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor (C -terminal) monomer, 48 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 (N-terminal) monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 14 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 3
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 110 nm3

SASDN43 – Full-length Human Pex5p protein

UniProt ID: P50542 (1-639) Peroxisomal targeting signal 1 receptor
Peroxisomal targeting signal 1 receptor experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 24
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 181 nm3

SASDN53 – Ternary Human Pex5p(full-length)-Pex14p(N)-PTS1 Protein Complex (1:7:1 stoichiometry)

UniProt ID: P50542 (None-None) Peroxisomal targeting signal 1 receptor

UniProt ID: O75381 (16-80) Peroxisomal membrane protein PEX14

UniProt ID: B4E0T2 (22-143) PTS1-BP
Peroxisomal targeting signal 1 receptorPeroxisomal membrane protein PEX14PTS1-BP experimental SAS data
SASREF model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 13 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Mar 18
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 6.0 nm
Dmax 20.0 nm
VolumePorod 267 nm3

SASDN63 – Microtubule affinity regulating kinase (isoform MARK2, T208E point mutant)

UniProt ID: Q7KZI7 (None-None) Serine/threonine-protein kinase MARK2
Serine/threonine-protein kinase MARK2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 61 nm3

SASDN73 – Microtubule affinity regulating kinase (isoform MARK2, wild type)

UniProt ID: Q7KZI7 (None-None) Serine/threonine-protein kinase MARK2
Serine/threonine-protein kinase MARK2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 62 nm3

SASDN83 – Microtubule affinity regulating kinase (isoform MARK1)

UniProt ID: Q9P0L2 (None-None) Serine/threonine-protein kinase MARK1
Serine/threonine-protein kinase MARK1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK1 monomer, 37 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 64 nm3