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Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design
Authors
Weiss, M.A., Hua, Q., Lynch, C.S., Frank, B.H., Shoelson, S.E.
Assembly
insulin A chain
Entity
1. insulin A chain (polymer), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N


Formula weight
2383.696 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 23.8 %, Completeness: 14.2 %, Completeness (bb): 7.1 % Detail

Polymer type: polypeptide(L)

Total1H
All14.2 % (17 of 120)14.2 % (17 of 120)
Backbone 7.1 % (3 of 42) 7.1 % (3 of 42)
Sidechain17.9 % (14 of 78)17.9 % (14 of 78)
Aromatic100.0 % (8 of 8)100.0 % (8 of 8)
Methyl 0.0 % (0 of 11) 0.0 % (0 of 11)

1. insulin A chain

GIVEQCCTSI CSLYQLENYC N

Sample

Temperature 310 K, pH 8



Release date
1995-07-30
Citation
Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design
Weiss, M.A., Hua, Q., Lynch, C.S., Frank, B.H., Shoelson, S.E.
Biochemistry (1991), 30, 7373-7389, PubMed 1906742 , DOI 10.1021/bi00244a004 ,
Related entities 1. insulin A chain, : 1 : 110 : 9 : 7 : 74 entities Detail
Interaction partners 1. insulin A chain, : 2 interactors Detail
Experiments performed 1 experiments Detail