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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 B chain
Entity
1. insulin B chain (polymer), 30 monomers, 3407.868 Da Detail

FVNQHLCGSD LVEALYLVCG ERGFFYTKPT


Formula weight
3407.868 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 40.0 %, Completeness: 39.4 %, Completeness (bb): 20.3 % Detail

Polymer type: polypeptide(L)

Total1H
All39.4 % (71 of 180)39.4 % (71 of 180)
Backbone20.3 % (12 of 59)20.3 % (12 of 59)
Sidechain48.8 % (59 of 121)48.8 % (59 of 121)
Aromatic100.0 % (25 of 25)100.0 % (25 of 25)
Methyl 5.9 % (1 of 17) 5.9 % (1 of 17)

1. insulin B chain

FVNQHLCGSD LVEALYLVCG ERGFFYTKPT

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 B chain, : 1 : 10 : 112 : 75 entities Detail
Interaction partners 1. insulin B chain, : 7 interactors Detail
Experiments performed 1 experiments Detail