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- PDB-2glh: Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulf... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2glh | ||||||
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Title | Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles | ||||||
![]() | Calcitonin-1 | ||||||
![]() | HORMONE/GROWTH FACTOR / a-helix / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | ![]() calcitonin receptor binding / sperm capacitation / activation of adenylate cyclase activity / hormone activity / extracellular space Similarity search - Function | ||||||
Method | SOLUTION NMR / restrained simulated annealing, energy minimization, unrestrained molecular dynamics | ||||||
![]() | Andreotti, G. / Lopez-Mendez, B. / Amodeo, P. / Morelli, M.A. / Nakamuta, H. / Motta, A. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 892.5 KB | Display | ![]() |
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PDB format | ![]() | 767.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 346 KB | Display | ![]() |
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Full document | ![]() | 584.9 KB | Display | |
Data in XML | ![]() | 39.1 KB | Display | |
Data in CIF | ![]() | 76.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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/peptide | Mass: 3436.894 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: peptide synthesis / References: UniProt: P01263 |
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Has protein modification | Y |
-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 |
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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 |