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- PDB-6szw: Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6szw | ||||||
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Title | Asymmetric complex of Factor XII and kininogen with gC1qR/C1QBP/P32 is governed by allostery | ||||||
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![]() | BLOOD CLOTTING / Contact activation | ||||||
Function / homology | ![]() adrenergic receptor binding / Apoptotic factor-mediated response / Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function / negative regulation of MDA-5 signaling pathway / kininogen binding / coagulation factor XIIa / plasma kallikrein-kinin cascade / negative regulation of RIG-I signaling pathway / deoxyribonuclease inhibitor activity / Factor XII activation ...adrenergic receptor binding / Apoptotic factor-mediated response / Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function / negative regulation of MDA-5 signaling pathway / kininogen binding / coagulation factor XIIa / plasma kallikrein-kinin cascade / negative regulation of RIG-I signaling pathway / deoxyribonuclease inhibitor activity / Factor XII activation / Defective SERPING1 causes hereditary angioedema / response to misfolded protein / negative regulation of defense response to virus / positive regulation of dendritic cell chemotaxis / hyaluronic acid binding / complement component C1q complex binding / positive regulation of plasminogen activation / positive regulation of trophoblast cell migration / blood coagulation, intrinsic pathway / mitochondrial ribosome binding / regulation of complement activation / misfolded protein binding / positive regulation of fibrinolysis / negative regulation of interleukin-12 production / positive regulation of mitochondrial translation / positive regulation of neutrophil chemotaxis / enzyme inhibitor activity / zymogen activation / RHOC GTPase cycle / Defective factor XII causes hereditary angioedema / negative regulation of mRNA splicing, via spliceosome / transcription factor binding / protein autoprocessing / negative regulation of type II interferon production / positive regulation of cell adhesion / RHOA GTPase cycle / positive regulation of blood coagulation / negative regulation of double-strand break repair via homologous recombination / positive regulation of substrate adhesion-dependent cell spreading / rough endoplasmic reticulum / fibrinolysis / Intrinsic Pathway of Fibrin Clot Formation / phosphatidylinositol 3-kinase/protein kinase B signal transduction / RNA splicing / complement activation, classical pathway / cytosolic ribosome assembly / protein processing / mRNA processing / transcription corepressor activity / blood coagulation / collagen-containing extracellular matrix / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / mitochondrial matrix / immune response / positive regulation of apoptotic process / serine-type endopeptidase activity / innate immune response / mRNA binding / calcium ion binding / DNA damage response / nucleolus / apoptotic process / negative regulation of transcription by RNA polymerase II / cell surface / mitochondrion / extracellular space / extracellular exosome / extracellular region / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kaira, B.G. / Emsley, J. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Factor XII and kininogen asymmetric assembly with gC1qR/C1QBP/P32 is governed by allostery. Authors: Kaira, B.G. / Slater, A. / McCrae, K.R. / Dreveny, I. / Sumya, U. / Mutch, N.J. / Searle, M. / Emsley, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.2 KB | Display | ![]() |
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PDB format | ![]() | 102.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8os5C ![]() 1p32S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: GLN / End label comp-ID: GLN / Refine code: _ / Auth seq-ID: 74 - 282 / Label seq-ID: 1 - 209
NCS ensembles :
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Components
#1: Protein | Mass: 23826.105 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | | Mass: 8461.517 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.31 % |
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Crystal grow | Temperature: 283.15 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.1 M sodium cacodylate, 0.1 M calcium acetate, 12% (w/v) PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 8, 2015 | |||||||||
Radiation | Protocol: LAUE / Monochromatic (M) / Laue (L): L / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 3.14→90.99 Å / Num. obs: 14379 / % possible obs: 99.8 % / Redundancy: 3.1 % / CC1/2: 0.953 / Rmerge(I) obs: 0.109 / Net I/σ(I): 6.4 | |||||||||
Reflection shell | Resolution: 3.14→3.36 Å / Num. unique obs: 2571 / CC1/2: 0.793 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1P32 Resolution: 3.14→90.99 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.866 / SU B: 25.916 / SU ML: 0.432 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.472 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 182.26 Å2 / Biso mean: 76.668 Å2 / Biso min: 33.92 Å2
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Refinement step | Cycle: final / Resolution: 3.14→90.99 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05
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LS refinement shell | Resolution: 3.14→3.221 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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