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Yorodumi- PDB-1ten: STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED B... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ten | ||||||
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Title | STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN | ||||||
Components | TENASCIN | ||||||
Keywords | CELL ADHESION PROTEIN | ||||||
Function / homology | Function and homology information perisynaptic extracellular matrix / tenascin complex / interstitial matrix / mesenchymal-epithelial cell signaling involved in prostate gland development / peripheral nervous system axon regeneration / bud outgrowth involved in lung branching / cellular response to prostaglandin D stimulus / syndecan binding / response to fibroblast growth factor / cellular response to vitamin D ...perisynaptic extracellular matrix / tenascin complex / interstitial matrix / mesenchymal-epithelial cell signaling involved in prostate gland development / peripheral nervous system axon regeneration / bud outgrowth involved in lung branching / cellular response to prostaglandin D stimulus / syndecan binding / response to fibroblast growth factor / cellular response to vitamin D / prostate gland epithelium morphogenesis / negative regulation of cell adhesion / extracellular matrix structural constituent / Syndecan interactions / neuromuscular junction development / odontogenesis of dentin-containing tooth / basement membrane / ECM proteoglycans / Integrin cell surface interactions / regulation of cell adhesion / response to mechanical stimulus / cellular response to retinoic acid / regulation of cell migration / morphogenesis of an epithelium / regulation of cell growth / Post-translational protein phosphorylation / response to wounding / osteoblast differentiation / integrin binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / regulation of inflammatory response / collagen-containing extracellular matrix / response to ethanol / cell adhesion / endoplasmic reticulum lumen / focal adhesion / positive regulation of cell population proliferation / positive regulation of gene expression / extracellular space / extracellular region / membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Leahy, D.J. / Hendrickson, W.A. / Aukhil, I. / Erickson, H.P. | ||||||
Citation | Journal: Science / Year: 1992 Title: Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Authors: Leahy, D.J. / Hendrickson, W.A. / Aukhil, I. / Erickson, H.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ten.cif.gz | 36.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ten.ent.gz | 25.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ten.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ten_validation.pdf.gz | 357.7 KB | Display | wwPDB validaton report |
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Full document | 1ten_full_validation.pdf.gz | 357.6 KB | Display | |
Data in XML | 1ten_validation.xml.gz | 3.2 KB | Display | |
Data in CIF | 1ten_validation.cif.gz | 4.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/1ten ftp://data.pdbj.org/pub/pdb/validation_reports/te/1ten | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 841, 871, 880, 888, AND 890 ARE DISORDERED. | ||||||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 10061.064 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P24821 |
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#2: Water | ChemComp-HOH / |
Sequence details | RESIDUES ARE NUMBERED ACCORDING TO NIES ET AL. (1991), J. BIOL. CHEM., 266, P. 2818. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.73 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 3 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 30 Å / Num. obs: 7950 / Observed criterion σ(F): 3 / Rmerge(I) obs: 0.067 |
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-Processing
Software |
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Refinement | Resolution: 1.8→10 Å / Rfactor Rwork: 0.196 / Rfactor obs: 0.196 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 10 Å / σ(F): 2 / Rfactor obs: 0.196 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.9 |