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Open data
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Basic information
Entry | Database: PDB / ID: 2glg | ||||||
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Title | NMR structure of the [L23,A24]-sCT mutant | ||||||
![]() | Calcitonin-1 | ||||||
![]() | HORMONE/GROWTH FACTOR / a-helix / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | ![]() 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 | ||||||
![]() | 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: Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculation Authors: Motta, A. / Pastore, A. / Goud, N.A. / Morelli, M.A.C. #2: ![]() Title: Conformational flexibility in calcitonin: The dynamic properties of human and salmon calcitonin Authors: Amodeo, P. / Motta, A. / Strazullo, G. / Morelli, M.A.C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 875.3 KB | Display | ![]() |
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PDB format | ![]() | 777.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 345.6 KB | Display | ![]() |
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Full document | ![]() | 668.3 KB | Display | |
Data in XML | ![]() | 36.8 KB | Display | |
Data in CIF | ![]() | 74.1 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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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3366.821 Da / Num. of mol.: 1 / Mutation: P23L, R24A / Source method: obtained synthetically Details: synthesis on polyoxyethylenepolystyrene graft resin 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: 1mM [L23,A24]-sCT; 120mM SDS; 90% H2O, 10% D2O / Solvent system: 90% H2O/10% 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: 600 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 |