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.
Type
Name
Symmetry operation
Number
identity operation
1_555
1
NMR ensembles
Data
Criteria
Number of conformers (submitted / calculated)
25 / 1000
structures with the lowest energy
Representative
Model #1
lowest energy
-
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 interest
N
-
Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
1
isotropic
1
1D1HNMR
1
2
1
isotropic
1
2D COSY
1
3
1
isotropic
1
2D TOCSY
1
4
1
isotropic
1
2D ROESY
-
Sample preparation
Details
Type: 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)
Component
Isotopic labeling
Solution-ID
2mM
Ac-hGal(17-30)-NH2
naturalabundance
1
4.14mM
sodiumacetate
[U-2H]
1
5.86mM
aceticacid
[U-2H]
1
Sample conditions
Ionic 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
-
NMR measurement
NMR spectrometer
Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 600 MHz
-
Processing
NMR software
Name
Developer
Classification
CNS
Brunger, Adams, Clore, Gros, NilgesandRead
structurecalculation
CNS
Brunger, Adams, Clore, Gros, NilgesandRead
refinement
MestreLab (Mnova / MestReNova / MestReC)
MestreLab
chemicalshiftassignment
MestreLab (Mnova / MestReNova / MestReC)
MestreLab
dataanalysis
MestreLab (Mnova / MestReNova / MestReC)
MestreLab
peakpicking
Refinement
Method: simulated annealing / Software ordinal: 2
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
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