+Open data
-Basic information
Entry | Database: PDB / ID: 2oon | ||||||
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Title | Structure of Ala14-PYY in aqueous solution | ||||||
Components | Peptide YY | ||||||
Keywords | HORMONE / peptide YY / PYY / neurohormone / folding of helical hairpins | ||||||
Function / homology | Function and homology information neuropeptide Y receptor binding / hormone activity / extracellular region Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | SOLUTION NMR / AMBER energy minimization in explicit water | ||||||
Authors | Zerbe, O. / Neumoin, A. / Mares, J. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2007 Title: Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin. Authors: Neumoin, A. / Mares, J. / Lerch-Bader, M. / Bader, R. / Zerbe, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2oon.cif.gz | 234 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2oon.ent.gz | 194 KB | Display | PDB format |
PDBx/mmJSON format | 2oon.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oo/2oon ftp://data.pdbj.org/pub/pdb/validation_reports/oo/2oon | HTTPS FTP |
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-Related structure data
Related structure data | 2oopC 2rlkC 2ooo C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4219.653 Da / Num. of mol.: 1 / Mutation: P14A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: PYY / Production host: Escherichia coli (E. coli) / Strain (production host): DH5a / References: UniProt: P68005 |
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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: 2mM solution at pH 4.1 in 20mM acetate buffer / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0 / pH: 4.1 / Pressure: 1 atm / Temperature: 301 K |
-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: AMBER energy minimization in explicit water / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |