Backbone 1H and 15N Chemical Shift Assignments for the Phosphotyrosine Binding Domain of Insulin Receptor Substrate 1 in the Apo and Phosphopeptide Bound Forms
GPAFKEVWQV ILKPKGLGQT KNLIGIYRLC LTSKTISFVK LNSEAAAVVL QLMNIRRCGH SENFFFIEVG RSAVTGPGEF WMQVDDSVVA QNMHETILEA MRAMSDEFRP R
Polymer type: polypeptide(L)
Total | 1H | 15N | |
---|---|---|---|
All | 23.3 % (202 of 868) | 14.1 % (104 of 739) | 76.0 % (98 of 129) |
Backbone | 53.6 % (194 of 362) | 39.8 % (98 of 246) | 82.8 % (96 of 116) |
Sidechain | 1.6 % (8 of 506) | 1.2 % (6 of 493) | 15.4 % (2 of 13) |
Aromatic | 7.0 % (4 of 57) | 3.6 % (2 of 55) | 100.0 % (2 of 2) |
Methyl | 0.0 % (0 of 73) | 0.0 % (0 of 73) |
1. Phosphotyrosine-Binding Domain of Insulin Receptor Substrate-1
GPAFKEVWQV ILKPKGLGQT KNLIGIYRLC LTSKTISFVK LNSEAAAVVL QLMNIRRCGH SENFFFIEVG RSAVTGPGEF WMQVDDSVVA QNMHETILEA MRAMSDEFRP R2. Interleukin-4 Receptor Phosphopeptide
LVIAGNPAXR SSolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.5, Details A complex between IRS-PTB and the IL-4 receptor peptide was formed by addition of peptide under the same buffer conditions to the protein to obtain a stoichiometery of 1:1.5 (protein:peptide).
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | Phosphotyrosine-Binding Domain of Insulin Receptor Substrate-1 | [U-15N] | 200 uM |