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- PDB-1y49: Solution Structure of CCAP (Crustacean Cardioactive Peptide) from... -
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Basic information
Entry | Database: PDB / ID: 1y49 | ||||||
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Title | Solution Structure of CCAP (Crustacean Cardioactive Peptide) from Drosophila melanogaster | ||||||
![]() | Cardioactive peptide | ||||||
![]() | NEUROPEPTIDE / disulfide bond | ||||||
Function / homology | Crustacean cardioactive peptide / Arthropod cardioacceleratory peptide 2a / neuropeptide receptor binding / neuropeptide hormone activity / positive regulation of heart rate / neuropeptide signaling pathway / extracellular space / Cardioactive peptide![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Nagata, K. / Tanokura, M. | ||||||
![]() | ![]() Title: Solution Structure of CCAP (Crustacean Cardioactive Peptide) from Drosophila melanogaster Authors: Nagata, K. / Tanokura, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 23.9 KB | Display | ![]() |
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PDB format | ![]() | 17.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 327.9 KB | Display | ![]() |
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Full document | ![]() | 350.6 KB | Display | |
Data in XML | ![]() | 3.7 KB | Display | |
Data in CIF | ![]() | 5.1 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/peptide | Mass: 959.099 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence occurs naturally in fruit flies. / References: UniProt: Q9VCW0 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
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Sample preparation
Details | Contents: 2mM CCAP / Solvent system: 50%(v/v) DMSO-d6, 50%(v/v) H2O |
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Sample conditions | pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: The structures are based on a total of 81 restraints, 75 are NOE-derived upper-bound distance restraints and 6 are upper- and lower-bound distance restraints from a disulfide bond. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10 |