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Yorodumi- PDB-1kun: SOLUTION STRUCTURE OF THE HUMAN ALPHA3-CHAIN TYPE VI COLLAGEN C-T... -
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Basic information
| Entry | Database: PDB / ID: 1kun | ||||||
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| Title | SOLUTION STRUCTURE OF THE HUMAN ALPHA3-CHAIN TYPE VI COLLAGEN C-TERMINAL KUNITZ DOMAIN, NMR, 20 STRUCTURES | ||||||
Components | ALPHA3-CHAIN TYPE VI COLLAGEN | ||||||
Keywords | EXTRACELLULAR MATRIX / COLLAGEN TYPE VI FRAGMENT / KUNITZ-TYPE DOMAIN / CONNECTIVE TISSUE | ||||||
| Function / homology | Function and homology informationcollagen type VI trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / Assembly of collagen fibrils and other multimeric structures / muscle organ development / Collagen degradation / ECM proteoglycans ...collagen type VI trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / Assembly of collagen fibrils and other multimeric structures / muscle organ development / Collagen degradation / ECM proteoglycans / Integrin cell surface interactions / response to glucose / response to UV / extracellular matrix / phosphatidylinositol 3-kinase/protein kinase B signal transduction / serine-type endopeptidase inhibitor activity / sarcolemma / extracellular vesicle / : / neuron apoptotic process / cell adhesion / endoplasmic reticulum lumen / extracellular space / extracellular exosome / extracellular region Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Sorensen, M.D. / Bjorn, S. / Norris, K. / Olsen, O. / Petersen, L. / James, T.L. / Led, J.J. | ||||||
Citation | Journal: Biochemistry / Year: 1997Title: Solution structure and backbone dynamics of the human alpha3-chain type VI collagen C-terminal Kunitz domain,. Authors: Sorensen, M.D. / Bjorn, S. / Norris, K. / Olsen, O. / Petersen, L. / James, T.L. / Led, J.J. #1: Journal: J.Biomol.NMR / Year: 1996Title: Elucidation of the Origin of Multiple Conformations of the Human Alpha 3-Chain Type Vi Collagen C-Terminal Kunitz Domain. The Reorientation of the Trp21 Ring Authors: Sorensen, M.D. / Kristensen, S.M. / Bjorn, S. / Norris, K. / Olsen, O. / Led, J.J. | ||||||
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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 | 1kun.cif.gz | 356.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1kun.ent.gz | 292.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1kun.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1kun_validation.pdf.gz | 351.4 KB | Display | wwPDB validaton report |
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| Full document | 1kun_full_validation.pdf.gz | 512 KB | Display | |
| Data in XML | 1kun_validation.xml.gz | 29.2 KB | Display | |
| Data in CIF | 1kun_validation.cif.gz | 44.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ku/1kun ftp://data.pdbj.org/pub/pdb/validation_reports/ku/1kun | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 6639.508 Da / Num. of mol.: 1 / Fragment: C-TERMINAL KUNITZ DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / Production host: ![]() |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Sample conditions | pH: 3 / Temperature: 303 K |
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| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| NMR spectrometer | Type: Bruker AM500 / Manufacturer: Bruker / Model: AM500 / Field strength: 500.13 MHz |
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Processing
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| NMR software |
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| Refinement | Software ordinal: 1 Details: THREE-DIMENSIONAL STRUCTURE IN AQUEOUS SOLUTION AS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND SIMULATED ANNEALING. | ||||||||||||
| NMR ensemble | Conformers calculated total number: 50 / Conformers submitted total number: 20 |
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