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Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure
Authors
Kristensen, S.M., Jorgensen, A.MARIE.M., Led, J.J., Balschmidt, P., Hansen, F.B.
Assembly
insulin A chain
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 95.2 %, Completeness: 91.5 %, Completeness (bb): 95.0 % Detail

Polymer type: polypeptide(L)

Total1H
All91.5 % (107 of 117)91.5 % (107 of 117)
Backbone95.0 % (38 of 40)95.0 % (38 of 40)
Sidechain87.0 % (67 of 77)87.0 % (67 of 77)
Aromatic100.0 % (8 of 8)100.0 % (8 of 8)
Methyl90.9 % (10 of 11)90.9 % (10 of 11)

1. insulin A chain

XIVEQCCTSI CSLYQLENYC N

Sample

Temperature 295 K, pH 1.85



Release date
1995-07-30
Citation
Proton nuclear magnetic resonance study of the B9(Asp) mutant of human insulin. Sequential assignment and secondary structure
Kristensen, S.M., Jorgensen, A.MARIE.M., Led, J.J., Balschmidt, P., Hansen, F.B.
J. Mol. Biol. (1991), 218, 221-231, PubMed 2002506 , DOI 10.1016/0022-2836(91)90886-b ,
Related entities 1. insulin A chain, : 1 : 117 : 83 entities Detail
Interaction partners 1. insulin A chain, : 2 interactors Detail
Experiments performed 1 experiments Detail