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- PDB-2n2f: Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Re... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n2f | ||||||
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Title | Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor | ||||||
![]() | Dynorphin A(1-13) | ||||||
![]() | HORMONE RECEPTOR / GPCR | ||||||
Function / homology | ![]() opioid receptor binding / opioid peptide activity / Opioid Signalling / sensory perception / neuronal dense core vesicle / neuropeptide signaling pathway / axon terminus / hippocampal mossy fiber to CA3 synapse / Peptide ligand-binding receptors / G-protein activation ...opioid receptor binding / opioid peptide activity / Opioid Signalling / sensory perception / neuronal dense core vesicle / neuropeptide signaling pathway / axon terminus / hippocampal mossy fiber to CA3 synapse / Peptide ligand-binding receptors / G-protein activation / G alpha (i) signalling events / chemical synaptic transmission / neuronal cell body / dendrite / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Model details | fewest violations, model2 | ||||||
![]() | O'Connor, C. / White, K. / Doncescu, N. / Didenko, T. / Roth, B.L. / Czaplicki, G. / Stevens, R.C. / Wuthrich, K. / Milon, A. | ||||||
![]() | ![]() Title: NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. Authors: O'Connor, C. / White, K.L. / Doncescu, N. / Didenko, T. / Roth, B.L. / Czaplicki, G. / Stevens, R.C. / Wuthrich, K. / Milon, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51 KB | Display | ![]() |
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PDB format | ![]() | 35.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 432.3 KB | Display | ![]() |
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Full document | ![]() | 502.2 KB | Display | |
Data in XML | ![]() | 10.2 KB | Display | |
Data in CIF | ![]() | 10.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Other databases |
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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: 1608.995 Da / Num. of mol.: 1 / Fragment: residues 207-219 / Source method: obtained synthetically Details: SYNTHESIS OF THE PEPTIDE WAS PERFORMED BY A SOLID PHASE METHOD USING FMOC CHEMISTRY. Source: (synth.) ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | pH: 6.1 / Pressure: ambient / Temperature: 280 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 56 / NOE medium range total count: 14 / NOE sequential total count: 42 / Protein phi angle constraints total count: 2 / Protein psi angle constraints total count: 2 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 1000 / Conformers submitted total number: 10 | ||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.2 Å |