+Open data
-Basic information
Entry | Database: PDB / ID: 8h0u | |||||||||
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Title | AQEE-30 in a DPC solution | |||||||||
Components | AQEE-30 | |||||||||
Keywords | NEUROPEPTIDE / VGF / DPC | |||||||||
Function / homology | Function and homology information carbohydrate homeostasis / synaptic signaling via neuropeptide / sexual reproduction / neuropeptide hormone activity / NGF-stimulated transcription / insulin secretion / regulation of neuronal synaptic plasticity / response to dietary excess / ovarian follicle development / transport vesicle ...carbohydrate homeostasis / synaptic signaling via neuropeptide / sexual reproduction / neuropeptide hormone activity / NGF-stimulated transcription / insulin secretion / regulation of neuronal synaptic plasticity / response to dietary excess / ovarian follicle development / transport vesicle / response to cAMP / response to cold / generation of precursor metabolites and energy / Post-translational protein phosphorylation / growth factor activity / response to insulin / regulation of synaptic plasticity / hormone activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / glucose homeostasis / cytoplasmic vesicle / defense response to bacterium / endoplasmic reticulum lumen / intracellular membrane-bounded organelle / neuronal cell body / glutamatergic synapse / Golgi apparatus / extracellular space Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Park, O.-S. / Jeon, Y.H. / Cheong, C. | |||||||||
Funding support | Korea, Republic Of, 2items
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Citation | Journal: Int J Mol Sci / Year: 2022 Title: Structure of AQEE-30 of VGF Neuropeptide in Membrane-Mimicking Environments. Authors: Park, O.S. / Bang, J.K. / Cheong, C. / Jeon, Y.H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8h0u.cif.gz | 234 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8h0u.ent.gz | 201.1 KB | Display | PDB format |
PDBx/mmJSON format | 8h0u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8h0u_validation.pdf.gz | 390 KB | Display | wwPDB validaton report |
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Full document | 8h0u_full_validation.pdf.gz | 491.9 KB | Display | |
Data in XML | 8h0u_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 8h0u_validation.cif.gz | 16.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h0/8h0u ftp://data.pdbj.org/pub/pdb/validation_reports/h0/8h0u | HTTPS FTP |
-Related structure data
Related structure data | 8h0gC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
Other databases |
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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: 3800.084 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VGF / Production host: Escherichia coli (E. coli) / References: UniProt: O15240 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution / Contents: 1 mM [U-13C; U-15N] AQEE-30, 90% H2O/10% D2O Details: 400 mM DPC was added to provide a membrane-mimicking environment. Label: 15N, 13C / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: AQEE-30 / Isotopic labeling: [U-13C; U-15N] |
Sample conditions | Ionic strength: 0 mM / Label: conditions_1 / pH: 6.0 / Pressure: 1 atm / Temperature: 288 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 2 | ||||||||||||
NMR representative | Selection criteria: medoid | ||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |