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Yorodumi- PDB-2glh: Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulf... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2glh | ||||||
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Title | Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles | ||||||
Components | Calcitonin-1 | ||||||
Keywords | HORMONE/GROWTH FACTOR / a-helix / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information calcitonin receptor binding / sperm capacitation / regulation of cytosolic calcium ion concentration / activation of adenylate cyclase activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / extracellular space Similarity search - Function | ||||||
Method | SOLUTION NMR / restrained simulated annealing, energy minimization, unrestrained molecular dynamics | ||||||
Authors | Andreotti, G. / Lopez-Mendez, B. / Amodeo, P. / Morelli, M.A. / Nakamuta, H. / Motta, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic alpha-helix. Authors: Andreotti, G. / Mendez, B.L. / Amodeo, P. / Morelli, M.A. / Nakamuta, H. / Motta, A. #1: Journal: J.Biomol.NMR / Year: 1999 Title: Conformational flexibility in calcitonin: The dynamic properties of human and salmon calcitonin in solution Authors: Amodeo, P. / Motta, A. / Strazzullo, G. / Castiglione-Morelli, M.A. #2: Journal: Biochemistry / Year: 1991 Title: Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculations Authors: Motta, A. / Pastore, A. / Goud, N.A. / Castiglione-Morelli, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2glh.cif.gz | 889.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2glh.ent.gz | 793.6 KB | Display | PDB format |
PDBx/mmJSON format | 2glh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gl/2glh ftp://data.pdbj.org/pub/pdb/validation_reports/gl/2glh | 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/peptide | Mass: 3436.894 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: peptide synthesis / References: UniProt: P01263 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 5 mM sCT; 20 mM phosphate buffer; 600 mM SDS; 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: restrained simulated annealing, energy minimization, unrestrained molecular dynamics Software ordinal: 1 | |||||||||||||||
NMR ensemble | Conformer selection criteria: periodically sampled unrestrained molecular dynamics structures Conformers calculated total number: 100 / Conformers submitted total number: 100 |