Mass: 1293.470 Da / Num. of mol.: 1 / Fragment: S2 Peptide, Residues 339-349 / Mutation: K340R, C346S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: GNAT1 / Plasmid: GEV-S2 / Production host: Escherichia coli (E. coli) / References: UniProt: P04695
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D NOESY
1
2
1
2D 1H-15N HSQC (w/o 1H decoupling)
1
3
2
2D 1H-13C CT-HSQC (w/o 1H decoupling)
NMR details
Text: sample was studied in dark adapted state and after photo activation of rhodopsin by illuminating the sample for 60s with a focussed microscope light, chemical shifts of S2 peptide are identical ...Text: sample was studied in dark adapted state and after photo activation of rhodopsin by illuminating the sample for 60s with a focussed microscope light, chemical shifts of S2 peptide are identical in both states, TrNOEs and TrDCs are difference values between the dark and light-activated states. orientation of the bound peptide relative to the membrane normal was determined from residual dipolar couplings. the membrane normal that belongs to model 1 runs parallel to the y-axis of the coordinate frame in which the deposited s2 peptide coordinates are specified.
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
2.6mM S2 peptide U-15N, 0.063mM rhodopsin as part of intact disk membranes from bovine retina; buffer: 10 mM HEPES, 20mM KCl, 0.05mM DTPA
90% H2O/10% D2O
2
2.6mM S2 peptide U-15N, 13C, 0.063mM rhodopsin as part of intact disk membranes from bovine retina; buffer: 10 mM HEPES, 20mM KCl, 0.05mM DTPA
90% H2O/10% D2O
Sample conditions
Ionic strength: 10 mM HEPES, 20 mM KCl / pH: 6.6 / Pressure: ambient / Temperature: 283 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker DMX
Bruker
DMX
750
1
Bruker DMX
Bruker
DMX
600
2
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Processing
NMR software
Name
Version
Developer
Classification
NMRPipe
2.1
Delaglio
processing
X-PLOR
NIH
A.T. Brunger
structuresolution
X-PLOR
NIH
A.T. Brunger, N. Tjandra, C.D. Schwieters, J. Kuszewski, G.M. Clore
refinement
Refinement
Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: the structures are based on a total of 121 NOE-derived distance constraints, 12 NOE-derived dihedral angle restraints, and 38 residual dipolar couplings
NMR representative
Selection criteria: lowest energy structure
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20
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