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Open data
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Basic information
Entry | Database: PDB / ID: 1uvg | ||||||
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Title | Solution structure of the 15th Domain of LEKTI | ||||||
![]() | SERINE PROTEINASE INHIBITOR KAZAL TYPE 5![]() | ||||||
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Function / homology | ![]() negative regulation of antibacterial peptide production / epidermal lamellar body / regulation of timing of anagen / epidermal cell differentiation / hair cell differentiation / Formation of the cornified envelope / negative regulation of immune response / regulation of T cell differentiation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vitzithum, K. / Roesch, P. / Marx, U.C. | ||||||
![]() | ![]() Title: The Solution Structure of a Chimeric Lekti Domain Reveals a Chameleon Sequence Authors: Tidow, H. / Lauber, T. / Vitzithum, K. / Sommerhoff, C. / Roesch, P. / Marx, U.C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 682.9 KB | Display | ![]() |
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PDB format | ![]() | 598.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 8585.635 Da / Num. of mol.: 1 / Fragment: LEKTI-DOMAIN15, RESIDUES 989-1064 Source method: isolated from a genetically manipulated source Details: DISULPHIDE BONDS BETWEEN CYS5 AND CYS40, BETWEEN CYS18 AND CYS37, BETWEEN CYS26 AND CYS58 Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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Compound details | FUNCTION: SERINE PROTEASE INHIBITOR, PROBABLY IMPORTANT FOR THE ANTI-INFLAMMATORY AND/OR ...FUNCTION: SERINE PROTEASE INHIBITOR, PROBABLY IMPORTANT FOR THE ANTI-INFLAMMATO |
-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED USING STANDARD NMR-TECHNIQUES ON 15N-LABELED AND UNLABELED PROTEIN |
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Sample preparation
Details | Contents: 90% H2O/10% D2O | |||||||||||||||||||||
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Sample conditions |
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-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model![]() |
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Processing
NMR software |
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Refinement | Method: ![]() | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY, LEAST RESTRAINT VIOLATION Conformers calculated total number: 200 / Conformers submitted total number: 31 |