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Proton chemical shift assignments for CP-11
Authors
Rozek, A., Powers, J.S., Friedrich, C.L., Hancock, R.E.W.
Assembly
CP-11in DPC micelles
Entity
1. CP-11in DPC micelles (polymer, Thiol state: not present), 14 monomers, 1878.294 Da Detail

ILKKWPWWPW RRKX


Formula weight
1878.294 Da
Source organism
Bos taurus
Exptl. method
NMR
Refine. method
DISTANCE GEOMETRY AND SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 92.9 %, Completeness: 97.4 %, Completeness (bb): 95.8 % Detail

Polymer type: polypeptide(L)

Total1H
All97.4 % (113 of 116)97.4 % (113 of 116)
Backbone95.8 % (23 of 24)95.8 % (23 of 24)
Sidechain97.8 % (90 of 92)97.8 % (90 of 92)
Aromatic100.0 % (24 of 24)100.0 % (24 of 24)
Methyl100.0 % (4 of 4)100.0 % (4 of 4)

1. indolicidin

ILKKWPWWPW RRKX

Sample

Pressure 1 atm, Temperature 310 (±1) K, pH 4.6 (±0.2)


#NameIsotope labelingTypeConcentration
1indolicidin2 mM
2DPC200 mM

Protein Blocks Logo
Calculated from 12 models in PDB: 1QXQ, Strand ID: A Detail


Release date
2003-10-15
Citation 1
Structure-based design of an indolicidin peptide analog with increased protease stability
Rozek, A., Powers, J.S., Friedrich, C.L., Hancock, R.E.W.
Biochemistry
Citation 2
Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
Rozek, A., Friedrich, C.L., Hancock, R.E.
Biochemistry (2000), 39, 15765-15774, PubMed 11123901 , DOI: ,
Related entities 1. CP-11in DPC micelles, : 1 : 1 entities Detail
Experiments performed 3 experiments Detail
Chemical shift validation 3 contents Detail
Keywords antimicrobial cationic peptide