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- PDB-1sy9: Structure of calmodulin complexed with a fragment of the olfactor... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sy9 | ||||||
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Title | Structure of calmodulin complexed with a fragment of the olfactory CNG channel | ||||||
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![]() | CALCIUM-BINDING PROTEIN / 4 helix-turn-helix | ||||||
Function / homology | ![]() response to stimulus / enzyme regulator activity / cAMP binding / sensory perception of smell / monoatomic ion channel activity / membrane => GO:0016020 / calmodulin binding / signaling receptor binding / calcium ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
![]() | Contessa, G.M. / Orsale, M. / Melino, S. / Torre, V. / Paci, M. / Desideri, A. / Cicero, D.O. | ||||||
![]() | ![]() Title: Structure of calmodulin complexed with an olfactory CNG channel fragment and role of the central linker: residual dipolar couplings to evaluate calmodulin binding modes outside the kinase family. Authors: Contessa, G.M. / Orsale, M. / Melino, S. / Torre, V. / Paci, M. / Desideri, A. / Cicero, D.O. #1: ![]() Title: Two distinct Ca2+-Calmodulin interactions with N-terminal regions of the olfactory and rod cyclic nucleotide gated channels characterized by NMR spectroscopy Authors: Orsale, M. / Melino, S. / Contessa, G.M. / Torre, V. / Andreotti, G. / Motta, A. / Paci, M. / Desideri, A. / Cicero, D.O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1011.7 KB | Display | ![]() |
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PDB format | ![]() | 846.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 352.8 KB | Display | ![]() |
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Full document | ![]() | 587.1 KB | Display | |
Data in XML | ![]() | 62.7 KB | Display | |
Data in CIF | ![]() | 86.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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 | Mass: 16721.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 3269.817 Da / Num. of mol.: 1 / Fragment: Residues 151-176 / Source method: obtained synthetically Details: The protein was chemically synthesized. The sequence of the protein is naturally found in Bos Taurus (bovine). References: UniProt: Q03041 |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
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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 AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: The structures are based on a total of 3935 restraints: 3050 are NOE-derived distance constraints, 591 are dihedral angle restraints, 133 are distance restraints from hydrogen bonds. 68 ...Details: The structures are based on a total of 3935 restraints: 3050 are NOE-derived distance constraints, 591 are dihedral angle restraints, 133 are distance restraints from hydrogen bonds. 68 scalar J coupling constants and 93 Residual Dipolar Coupling constants were included as experimental restraints necessary to obtain the final structures. | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 20 |