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Yorodumi- PDB-1tlk: X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN O... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1tlk | ||||||
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| Title | X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN OF MYOSIN LIGHT CHAIN KINASE, AT 2.8 ANGSTROMS RESOLUTION | ||||||
Components | TELOKIN | ||||||
Keywords | CALMODULIN-BINDING | ||||||
| Function / homology | Function and homology informationtonic smooth muscle contraction / myosin light chain kinase activity / cleavage furrow / stress fiber / lamellipodium / calmodulin binding / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Holden, H.M. / Rayment, I. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992Title: X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. Authors: Holden, H.M. / Ito, M. / Hartshorne, D.J. / Rayment, I. | ||||||
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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 | 1tlk.cif.gz | 32.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1tlk.ent.gz | 21.4 KB | Display | PDB format |
| PDBx/mmJSON format | 1tlk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1tlk_validation.pdf.gz | 375.9 KB | Display | wwPDB validaton report |
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| Full document | 1tlk_full_validation.pdf.gz | 383 KB | Display | |
| Data in XML | 1tlk_validation.xml.gz | 4.5 KB | Display | |
| Data in CIF | 1tlk_validation.cif.gz | 6.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tl/1tlk ftp://data.pdbj.org/pub/pdb/validation_reports/tl/1tlk | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| Unit cell |
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| Atom site foot note | 1: RESIDUE PRO 69 IS A CIS PROLINE. |
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Components
| #1: Protein | Mass: 16960.326 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.5 % | |||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS Temperature: 4 ℃ / Method: batch method / PH range low: 7 / PH range high: 4.5 | |||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 30 Å / Num. obs: 4061 / Num. measured all: 15144 / Rmerge(I) obs: 0.05 |
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Processing
| Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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| Refinement | Resolution: 2.8→8 Å / Rfactor obs: 0.184 | ||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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| Refine LS restraints |
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| Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8 Å / Num. reflection obs: 3722 / Rfactor obs: 0.184 | ||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS
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