+Open data
-Basic information
Entry | Database: PDB / ID: 2d2p | ||||||
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Title | The solution structure of micelle-bound peptide | ||||||
Components | Pituitary adenylate cyclase activating polypeptide-38Pituitary adenylate cyclase-activating peptide | ||||||
Keywords | HORMONE/GROWTH FACTOR / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information pituitary adenylate cyclase activating polypeptide activity / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of growth hormone secretion / NGF-independant TRKA activation / neuropeptide hormone activity / regulation of G protein-coupled receptor signaling pathway / insulin secretion / peptide hormone receptor binding / cAMP-mediated signaling / negative regulation of cell cycle ...pituitary adenylate cyclase activating polypeptide activity / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of growth hormone secretion / NGF-independant TRKA activation / neuropeptide hormone activity / regulation of G protein-coupled receptor signaling pathway / insulin secretion / peptide hormone receptor binding / cAMP-mediated signaling / negative regulation of cell cycle / neuropeptide signaling pathway / positive regulation of protein kinase activity / activation of adenylate cyclase activity / female pregnancy / adenylate cyclase-activating G protein-coupled receptor signaling pathway / Glucagon-type ligand receptors / positive regulation of GTPase activity / neuron projection development / regulation of protein localization / cell-cell signaling / positive regulation of cold-induced thermogenesis / positive regulation of cytosolic calcium ion concentration / perikaryon / G alpha (s) signalling events / positive regulation of ERK1 and ERK2 cascade / neuron projection / signaling receptor binding / positive regulation of transcription by RNA polymerase II / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, MOLECULAR DYNAMICS, ENERGY MINIMIZATION | ||||||
Authors | Tateishi, Y. / Jee, J.G. / Inooka, H. / Tochio, H. / Hiroaki, H. / Shirakawa, M. | ||||||
Citation | Journal: To be Published Title: The solution structure of micelle-bound peptide Authors: Tateishi, Y. / Jee, J.G. / Inooka, H. / Tochio, H. / Hiroaki, H. / Shirakawa, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d2p.cif.gz | 258.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d2p.ent.gz | 224.6 KB | Display | PDB format |
PDBx/mmJSON format | 2d2p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d2/2d2p ftp://data.pdbj.org/pub/pdb/validation_reports/d2/2d2p | 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/peptide | Mass: 4545.344 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET21b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P18509 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 0.5mM PACAP38 U-15N,13C; 20mM potassium phosphate buffer; 200mM DPC; 93% H2O, 5% D2O, 2% Glycerol-1,1,2,3,3-d5 Solvent system: 93% H2O, 5% D2O, 2% Glycerol-1,1,2,3,3-d5 |
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Sample conditions | Ionic strength: 20mM potassium phosphate / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, MOLECULAR DYNAMICS, ENERGY MINIMIZATION Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |