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Yorodumi- PDB-1f55: SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f55 | ||||||
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Title | SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULIN | ||||||
Components | CALMODULIN | ||||||
Keywords | TRANSPORT PROTEIN / EF-hand / helix-loop-helix | ||||||
Function / homology | Function and homology information regulation of membrane tubulation / cell budding / spindle pole body organization / 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 / cell budding / spindle pole body organization / 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 / microautophagy / vacuole fusion, non-autophagic / cell tip / incipient cellular bud site / cellular bud tip / vesicle transport along actin filament / actin cortical patch / cellular bud neck / mating projection tip / phosphatidylinositol biosynthetic process / cellular hyperosmotic response / mitogen-activated protein kinase binding / enzyme regulator activity / cytoskeleton organization / 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. / Takahashi, K. / Nakashima, K. / Kumaki, Y. / Nakata, M. / Hikichi, K. / Yazawa, M. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Solution Structures of the N-terminal Domain of Yeast Calmodulin: Ca2+-Dependent Conformational Change and Its Functional Implication Authors: Ishida, H. / Takahashi, K. / Nakashima, K. / Kumaki, Y. / Nakata, M. / Hikichi, K. / Yazawa, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f55.cif.gz | 689.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f55.ent.gz | 574.3 KB | Display | PDB format |
PDBx/mmJSON format | 1f55.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f5/1f55 ftp://data.pdbj.org/pub/pdb/validation_reports/f5/1f55 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8546.367 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Details: INTRACELLULAR CALCIUM SENSOR Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: PET-30B(+) AND PIC10 / Production host: Escherichia coli (E. coli) / References: UniProt: P06787 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using double-resonance NMR spectroscopy on 15N-labeled protein |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50mM KCl / pH: 6.8 / Pressure: ambient / Temperature: 303 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 920 restraints, 863 are NOE-derived distance constraints, 17 dihedral angle restraints, 28 distance restraints from hydrogen bonds, 12 calcium-ligand distance restraints | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 30 |