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- PDB-7s3o: NMR Solution Structure of hGal(2-12)KK, a solubility-tagged trunc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7s3o | ||||||
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Title | NMR Solution Structure of hGal(2-12)KK, a solubility-tagged truncation of the human neuropeptide galanin | ||||||
![]() | Galanin | ||||||
![]() | NEUROPEPTIDE / binding epitope / synthetic peptide | ||||||
Function / homology | ![]() galanin receptor binding / type 1 galanin receptor binding / type 2 galanin receptor binding / type 3 galanin receptor binding / galanin receptor activity / positive regulation of large conductance calcium-activated potassium channel activity / positive regulation of timing of catagen / positive regulation of cortisol secretion / regulation of glucocorticoid metabolic process / negative regulation of lymphocyte proliferation ...galanin receptor binding / type 1 galanin receptor binding / type 2 galanin receptor binding / type 3 galanin receptor binding / galanin receptor activity / positive regulation of large conductance calcium-activated potassium channel activity / positive regulation of timing of catagen / positive regulation of cortisol secretion / regulation of glucocorticoid metabolic process / negative regulation of lymphocyte proliferation / neuropeptide hormone activity / feeding behavior / insulin secretion / neuropeptide signaling pathway / response to immobilization stress / protein kinase A signaling / cAMP-mediated signaling / Peptide ligand-binding receptors / secretory granule / response to insulin / response to estrogen / G alpha (i) signalling events / response to xenobiotic stimulus / positive regulation of apoptotic process / neuronal cell body / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Kraichely, K.N. / Clinkscales, S.E. / Parnham, S. / Giuliano, M.W. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Minimal Increments of Hydrophobic Collapse within the N-Terminus of the Neuropeptide Galanin. Authors: Kraichely, K.N. / Clinkscales, S.E. / Hendy, C.M. / Mendoza, E.A. / Parnham, S. / Giuliano, M.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94 KB | Display | ![]() |
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PDB format | ![]() | 65.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7s3qC ![]() 7s3rC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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: 1450.705 Da / Num. of mol.: 1 / Mutation: P45K, H46K / Source method: obtained synthetically / 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
Details | Type: solution Contents: 5 mM hGal(2-12)KK, 4.14 mM D3 sodium acetate, 5.86 mM D4 acetic acid, 95% H2O/5% D2O Details: 5 mM hGal(2-12)KK peptide 10 mM deuterated (d3/d4) sodium acetate/acetic acid buffer pH 4.6 Label: SEC-I-072A / Solvent system: 95% H2O/5% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Details: 5 mM hGal(2-12)KK peptide 10 mM deuterated (d3/d4) sodium acetate/acetic acid buffer pH 4.6 Ionic strength: 4.14 mM sodium acetate-d3 mM / Label: 1 / pH: 4.6 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 400 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 25 |