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- PDB-8dhz: NMR Structure of Ac-hGal(17-30)NH2, an N-terminally acetylated fr... -

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Basic information

Entry
Database: PDB / ID: 8dhz
TitleNMR Structure of Ac-hGal(17-30)NH2, an N-terminally acetylated fragment of the C-terminus of human galanin
ComponentsGalanin
KeywordsNEUROPEPTIDE / fragment
Function / homology
Function and homology information


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 / response to immobilization stress / neuropeptide signaling pathway / 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
Galanin / Galanin precursor / Galanin message associated peptide (GMAP) / Galanin / Galanin message associated peptide (GMAP) / Galanin signature. / Galanin
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsKraichely, K.N. / Hendy, C.M. / Parnham, S. / Giuliano, M.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P20GM103499-20 United States
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2022
Title: The neuropeptide galanin adopts an irregular secondary structure.
Authors: Wilkinson, R.E. / Kraichely, K.N. / Hendy, C.M. / Buchanan, L.E. / Parnham, S. / Giuliano, M.W.
History
DepositionJun 28, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 24, 2022Provider: repository / Type: Initial release
Revision 1.1Sep 7, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Galanin


Theoretical massNumber of molelcules
Total (without water)1,5471
Polymers1,5471
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: assay for oligomerization, 1D 1H NMR spectra were analyzed between 0.1 mM and 5 mM, a fifty-fold range of concentrations. All spectra were identical (free of dispersion and line-broadening ...Evidence: assay for oligomerization, 1D 1H NMR spectra were analyzed between 0.1 mM and 5 mM, a fifty-fold range of concentrations. All spectra were identical (free of dispersion and line-broadening effects), independent of concentration below and inclusive of a peptide concentration of 2mM, which was selected for structure analysis.
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 1000structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Galanin /


Mass: 1546.647 Da / Num. of mol.: 1 / Fragment: C-terminal residues, 49-62 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P22466
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic11D 1H NMR
121isotropic12D COSY
131isotropic12D TOCSY
141isotropic12D ROESY

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Sample preparation

DetailsType: lyophilized powder
Contents: 2 mM Ac-hGal(17-30)-NH2, 4.14 mM [U-2H] sodium acetate, 5.86 mM [U-2H] acetic acid, 95% H2O/5% D2O
Details: peptide was suspended and dissolved into deuterated acetate buffer, which had been prepared in 95:5 H2O:D2O to within 0.02 units of pH 4.6.
Label: Ac-hGal(17-30)-NH2 / Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
2 mMAc-hGal(17-30)-NH2natural abundance1
4.14 mMsodium acetate[U-2H]1
5.86 mMacetic acid[U-2H]1
Sample conditionsIonic strength: sample was dissolved in 10 mM sodium acetate-d3/acetic acid-d4 buffer at pH 4.6; no additional additives were present. Not defined
Label: 1 / pH: 4.6 / PH err: 0.02 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
CNSBrunger, Adams, Clore, Gros, Nilges and Readstructure calculation
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
MestreLab (Mnova / MestReNova / MestReC)MestreLabchemical shift assignment
MestreLab (Mnova / MestReNova / MestReC)MestreLabdata analysis
MestreLab (Mnova / MestReNova / MestReC)MestreLabpeak picking
RefinementMethod: simulated annealing / Software ordinal: 2
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 1000 / Conformers submitted total number: 25

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