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Open data
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Basic information
| Entry | Database: PDB / ID: 7mrn | ||||||
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| Title | Mouse CNTN5 APP complex | ||||||
Components |
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Keywords | CELL ADHESION / Ig superfamily / amyloid precursor protein | ||||||
| Function / homology | Function and homology informationregulation of response to calcium ion / positive regulation of protein import / Formyl peptide receptors bind formyl peptides and many other ligands / regulation of neurotransmitter uptake / regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway / positive regulation of response to endoplasmic reticulum stress / negative regulation of presynapse assembly / Advanced glycosylation endproduct receptor signaling / Post-translational modification: synthesis of GPI-anchored proteins / positive regulation of gene expression, epigenetic ...regulation of response to calcium ion / positive regulation of protein import / Formyl peptide receptors bind formyl peptides and many other ligands / regulation of neurotransmitter uptake / regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway / positive regulation of response to endoplasmic reticulum stress / negative regulation of presynapse assembly / Advanced glycosylation endproduct receptor signaling / Post-translational modification: synthesis of GPI-anchored proteins / positive regulation of gene expression, epigenetic / cytosolic mRNA polyadenylation / endosome to plasma membrane transport vesicle / low-density lipoprotein particle mediated signaling / ECM proteoglycans / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / regulation of dendritic spine maintenance / negative regulation of blood circulation / positive regulation of endothelin production / synaptic assembly at neuromuscular junction / positive regulation of Toll signaling pathway / TRAF6 mediated NF-kB activation / Lysosome Vesicle Biogenesis / phospholipase D-activating G protein-coupled receptor signaling pathway / positive regulation of G protein-coupled receptor internalization / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / protein trimerization / smooth endoplasmic reticulum calcium ion homeostasis / TAK1-dependent IKK and NF-kappa-B activation / G alpha (q) signalling events / dendrite self-avoidance / presynapse assembly / positive regulation of amyloid precursor protein catabolic process / lipoprotein particle / regulation of amyloid-beta clearance / intermediate-density lipoprotein particle / Platelet degranulation / cell-cell adhesion mediator activity / response to yeast / ciliary rootlet / RAGE receptor binding / G alpha (i) signalling events / antifungal humoral response / regulation of amyloid fibril formation / positive regulation of G protein-coupled receptor signaling pathway / Mitochondrial protein degradation / low-density lipoprotein particle / COPII-coated ER to Golgi transport vesicle / high-density lipoprotein particle / very-low-density lipoprotein particle / acetylcholine receptor binding / frizzled binding / amyloid-beta complex / heparan sulfate proteoglycan binding / growth cone lamellipodium / cellular response to norepinephrine stimulus / collateral sprouting in absence of injury / growth cone filopodium / suckling behavior / microglia development / positive regulation of monocyte chemotaxis / axo-dendritic transport / axon midline choice point recognition / positive regulation of membrane protein ectodomain proteolysis / regulation of synapse structure or activity / hippocampal neuron apoptotic process / astrocyte activation involved in immune response / presynaptic active zone / regulation of spontaneous synaptic transmission / mating behavior / positive regulation of extrinsic apoptotic signaling pathway / growth factor receptor binding / negative regulation of protein localization to nucleus / peptidase activator activity / neuromuscular process controlling balance / PTB domain binding / positive regulation of amyloid fibril formation / Golgi-associated vesicle / regulation of toll-like receptor signaling pathway / astrocyte projection / neuron remodeling / negative regulation of neuron differentiation / spindle midzone / chemoattractant activity / nuclear envelope lumen / forebrain development / homophilic cell-cell adhesion / intracellular vesicle / smooth endoplasmic reticulum / dendrite development / positive regulation of protein metabolic process / positive regulation of cAMP/PKA signal transduction / signaling receptor activator activity / negative regulation of long-term synaptic potentiation / transition metal ion binding / apolipoprotein binding / regulation of multicellular organism growth / main axon / modulation of excitatory postsynaptic potential / intracellular copper ion homeostasis Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Bouyain, S. / Karuppan, S.J. | ||||||
| Funding support | United States, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2021Title: Members of the vertebrate contactin and amyloid precursor protein families interact through a conserved interface. Authors: Karuppan, S.J. / Vogt, A. / Fischer, Z. / Ladutska, A. / Swiastyn, J. / McGraw, H.F. / Bouyain, S. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7mrn.cif.gz | 381.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7mrn.ent.gz | 281.2 KB | Display | PDB format |
| PDBx/mmJSON format | 7mrn.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mr/7mrn ftp://data.pdbj.org/pub/pdb/validation_reports/mr/7mrn | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 7mqyC ![]() 7mrkC ![]() 7mrmC ![]() 7mroC ![]() 7mrqC ![]() 7mrsC ![]() 3ktmS ![]() 5e52S S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 33395.023 Da / Num. of mol.: 2 / Fragment: FN1-FN3 domains Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 19730.727 Da / Num. of mol.: 2 / Fragment: E1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.28 Å3/Da / Density % sol: 62.45 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 100mM Na-citrate pH 5.5, 10% Isopropanol, 25% (w/v) PEG 400 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å |
| Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 21, 2018 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 3.5→74.79 Å / Num. obs: 17993 / % possible obs: 100 % / Redundancy: 9.7 % / Biso Wilson estimate: 114.08 Å2 / CC1/2: 0.983 / Rmerge(I) obs: 0.216 / Rpim(I) all: 0.073 / Rrim(I) all: 0.229 / Net I/σ(I): 8.8 |
| Reflection shell | Resolution: 3.5→3.83 Å / Redundancy: 9.8 % / Rmerge(I) obs: 1.323 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 4233 / CC1/2: 0.728 / Rpim(I) all: 0.444 / Rrim(I) all: 1.396 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 3KTM, 5E52 Resolution: 3.5→64.64 Å / SU ML: 0.4177 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 28.6588 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 136.01 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.5→64.64 Å
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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About Yorodumi





X-RAY DIFFRACTION
United States, 1items
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