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Yorodumi- PDB-1sy9: Structure of calmodulin complexed with a fragment of the olfactor... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sy9 | ||||||
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Title | Structure of calmodulin complexed with a fragment of the olfactory CNG channel | ||||||
Components |
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Keywords | CALCIUM-BINDING PROTEIN / 4 helix-turn-helix | ||||||
Function / homology | Function and homology information response to stimulus / 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 | Xenopus laevis (African clawed frog) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Contessa, G.M. / Orsale, M. / Melino, S. / Torre, V. / Paci, M. / Desideri, A. / Cicero, D.O. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2005 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: Journal: FEBS Lett. / Year: 2003 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sy9.cif.gz | 1008.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sy9.ent.gz | 872.4 KB | Display | PDB format |
PDBx/mmJSON format | 1sy9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sy/1sy9 ftp://data.pdbj.org/pub/pdb/validation_reports/sy/1sy9 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Xenopus laevis (African clawed frog) / Production host: Escherichia coli (E. coli) / References: UniProt: P62155, UniProt: P0DP33*PLUS |
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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
Details |
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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 |
-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 |