S1P4FirstExtracellularLoopPeptidomimetic / Arfaptin-2 / ADP-ribosylation factor-interacting protein 2 / Partner of RAC1 / Protein ...Arfaptin-2 / ADP-ribosylation factor-interacting protein 2 / Partner of RAC1 / Protein POR1phingosine 1-phosphate receptor Edg-6 / S1P receptor Edg-6 / Endothelial differentiation G-protein coupled receptor 6 / Sphingosine 1-phosphate receptor 4 / S1P4
Mass: 3891.223 Da / Num. of mol.: 1 / Fragment: Extracellular Loop 1 / Mutation: L10C/A28C Source method: isolated from a genetically manipulated source Details: This protein is a fusion protein. Residues 13-26 and 29-30 are from the first extracellular loop of S1P4 receptor. The rest, residues 3-12, 27-28, and 31-34 are from Arfatin (PDB entry 1I49) ...Details: This protein is a fusion protein. Residues 13-26 and 29-30 are from the first extracellular loop of S1P4 receptor. The rest, residues 3-12, 27-28, and 31-34 are from Arfatin (PDB entry 1I49) segments 139-148, 164-164, 168-171 of 1I49 that we designed to be in the sequence. Source: (gene. exp.) Homo sapiens (human) / Gene: S1P4 / Plasmid: pET-32a, CCE1a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P53365, UniProt: O95977
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
2
1
2
3D 15N-separated NOESY
2
2
2
3D 13C-separated NOESY
NMR details
Text: The structure was determined using triple-resonance NMR spectroscopy.
Method: simulated annealing, matrix relaxation, torsion angle dynamics, energy minimization Software ordinal: 1 Details: the structures are based on a total of 748 NOE-derived distance constraints
NMR representative
Selection criteria: extended first helix
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 10
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