Search

NMR and circular dichroic studies on the solution conformation of a synthetic peptide derived from the calmodulin-binding domain of Bordetella pertussis adenylate cyclase
Authors
Precheur, B., Siffert, O., Barzu, O., Craescu, C.T.
Assembly
adenylate cyclase
Entity
1. adenylate cyclase (polymer), 20 monomers, 2238.595 Da Detail

RERIDLLWKI ARAGARSAVG


Formula weight
2238.595 Da
Source organism
Bordetella pertussis
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 99.2 %, Completeness (bb): 97.6 % Detail

Polymer type: polypeptide(L)

Total1H
All99.2 % (120 of 121)99.2 % (120 of 121)
Backbone97.6 % (41 of 42)97.6 % (41 of 42)
Sidechain100.0 % (79 of 79)100.0 % (79 of 79)
Aromatic100.0 % (6 of 6)100.0 % (6 of 6)
Methyl100.0 % (14 of 14)100.0 % (14 of 14)

1. adenylate cyclase

RERIDLLWKI ARAGARSAVG

Sample

Temperature 278 K, pH 3.5



Release date
1995-07-30
Citation
NMR and circular dichroic studies on the solution conformation of a synthetic peptide derived from the calmodulin-binding domain of Bordetella pertussis adenylate cyclase
Precheur, B., Siffert, O., Barzu, O., Craescu, C.T.
Eur. J. Biochem. (1991), 196, 67-72, PubMed 2001708 , DOI 10.1111/j.1432-1033.1991.tb15786.x ,
Related entities 1. adenylate cyclase, : 1 : 5 : 1 entities Detail
Interaction partners 1. adenylate cyclase, : 1 interactors Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail