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Solution NMR Structure of Insulin A-chain peptide
Authors
Sharma, A.K., Zhang, Y., Ling, Y., Greer, A.B., Hafler, D.A., Kent, S.C., Rigby, A.C.
Assembly
Human Insulin A-chain peptide
Entity
1. Human Insulin A-chain peptide (polymer, Thiol state: all free), 15 monomers, 1646.903 Da Detail

GIVEQCCTSI CSLYQ


Formula weight
1646.903 Da
Source organism
Homo sapiens
Exptl. method
SOLUTION NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 77.4 %, Completeness (bb): 62.2 % Detail

Polymer type: polypeptide(L)

Total1H13C
All77.4 % (113 of 146)100.0 % (83 of 83)47.6 % (30 of 63)
Backbone62.2 % (46 of 74)100.0 % (30 of 30)36.4 % (16 of 44)
Sidechain89.5 % (77 of 86)100.0 % (53 of 53)72.7 % (24 of 33)
Aromatic50.0 % (4 of 8)100.0 % (4 of 4) 0.0 % (0 of 4)
Methyl100.0 % (18 of 18)100.0 % (9 of 9)100.0 % (9 of 9)

1. Human Insulin A-chain peptide

GIVEQCCTSI CSLYQ

Sample

Solvent system 80%DMSO-d6/20%H2O, Temperature 288 K, pH 6.0, Details 80%DMSO-d6/20%H2O co-solvent system


#NameIsotope labelingTypeConcentration
1Human Insulin A-chain peptidenatural abundance3.03 mM
2DMSO-d6[U-99% 2H]80 %
3H2Onatural abundance20 %

Release date
2010-02-28
Citation
Evaluating the intrinsic cysteine redox-dependent states of the A-chain of human insulin using NMR spectroscopy, quantum chemical calculations, and mass spectrometry
Sharma, A.K., Ling, Y., Greer, A.B., Hafler, D.A., Kent, S.C., Zhang, Y., Rigby, A.C.
J. Phys. Chem. B (2010), 114, 585-591, PubMed 19954153 , DOI 10.1021/jp908729h ,
Related entities 1. Human Insulin A-chain peptide, : 1 : 109 : 9 : 4 : 37 entities Detail
Interaction partners 1. Human Insulin A-chain peptide, : 2 interactors Detail
Experiments performed 4 experiments Detail
Keywords cyana-2.1, ensemble of 20 structures, insulin A-chain analog, least target function value, NMR structure, torsion angle dynamics