[English] 日本語
Yorodumi- PDB-1lkj: NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lkj | ||||||
---|---|---|---|---|---|---|---|
Title | NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae | ||||||
Components | Calmodulin | ||||||
Keywords | METAL BINDING PROTEIN / yeast calmodulin / saccharomyces cerevisiae / EF-hand | ||||||
Function / homology | Function and homology information regulation of membrane tubulation / spindle pole body organization / cell budding / myosin I complex / central plaque of spindle pole body / regulation of microtubule nucleation / cellular bud / positive regulation of Arp2/3 complex-mediated actin nucleation / myosin V complex / karyogamy involved in conjugation with cellular fusion ...regulation of membrane tubulation / spindle pole body organization / cell budding / myosin I complex / central plaque of spindle pole body / regulation of microtubule nucleation / cellular bud / positive regulation of Arp2/3 complex-mediated actin nucleation / myosin V complex / karyogamy involved in conjugation with cellular fusion / vacuole fusion, non-autophagic / microautophagy / actin cortical patch / incipient cellular bud site / cellular bud tip / cellular bud neck / mating projection tip / vesicle transport along actin filament / phosphatidylinositol biosynthetic process / mitogen-activated protein kinase binding / enzyme regulator activity / cytoskeleton organization / Neutrophil degranulation / receptor-mediated endocytosis / endocytosis / protein import into nucleus / calcium-dependent protein binding / calcium ion binding Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Ishida, H. / Nakashima, K. / Kumaki, Y. / Nakata, M. / Hikichi, K. / Yazawa, M. | ||||||
Citation | Journal: Biochemistry / Year: 2002 Title: The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property. Authors: Ishida, H. / Nakashima, K. / Kumaki, Y. / Nakata, M. / Hikichi, K. / Yazawa, M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1lkj.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1lkj.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1lkj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lk/1lkj ftp://data.pdbj.org/pub/pdb/validation_reports/lk/1lkj | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 16016.603 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: pET30b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P06787 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 50mM KCl / pH: 7.0 / Pressure: ambient / Temperature: 303 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 31 |