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Solution NMR structure of Insulin A-chain variant peptide
Authors
Sharma, A.K., Zhang, Y., Ling, Y., Greer, A.B., Hafler, D.A., Kent, S.C., Rigby, A.C.
Assembly
Insulin A-chain variant peptide
Entity
1. Insulin A-chain variant peptide (polymer, Thiol state: all free), 17 monomers, 1931.261 Da Detail

KRGIVEQCCT SICSLYQ


Formula weight
1931.261 Da
Source organism
Homo sapiens
Exptl. method
SOLUTION NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 83.5 %, Completeness (bb): 70.2 % Detail

Polymer type: polypeptide(L)

Total1H13C
All83.5 % (147 of 176)99.0 % (101 of 102)62.2 % (46 of 74)
Backbone70.2 % (59 of 84)97.1 % (33 of 34)52.0 % (26 of 50)
Sidechain96.3 % (104 of 108)100.0 % (68 of 68)90.0 % (36 of 40)
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. Insulin A-chain variant peptide

KRGIVEQCCT SICSLYQ

Sample

Solvent system 80%DMSO-d6/20%H2O, Temperature 288 K, pH 5.5, Details 80%DMSO-d6/20%H2O


#NameIsotope labelingTypeConcentration
1Insulin A-chain variant peptidenatural abundance2.16 mM
2DMSO-d6natural abundance80 %
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. Insulin A-chain variant peptide, : 1 : 10 : 6 : 98 : 58 entities Detail
Interaction partners 1. Insulin A-chain variant peptide, : 2 interactors Detail
Experiments performed 5 experiments Detail
Keywords cyana-2.1, ensemble of 20 structures, KR-A1-15, Insulin A-chain variant, NMR structure