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Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P25
Authors
Massiah, M.A., Ko, Y.H., Pedersen, P.L., Mildvan, A.S.
Assembly
cystic fibrosis transmembrane conductance regulator (CFTR)
Entity
1. cystic fibrosis transmembrane conductance regulator (CFTR) (polymer, Thiol state: not present), 25 monomers, 2903.313 Da Detail

MPGTIKENII GVSYDEYRYR SVIKA


Formula weight
2903.313 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
DISTANCE GEOMETRY
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 80.9 %, Completeness (bb): 96.1 % Detail

Polymer type: polypeptide(L)

Total1H
All80.9 % (127 of 157)80.9 % (127 of 157)
Backbone96.1 % (49 of 51)96.1 % (49 of 51)
Sidechain73.6 % (78 of 106)73.6 % (78 of 106)
Aromatic100.0 % (12 of 12)100.0 % (12 of 12)
Methyl100.0 % (14 of 14)100.0 % (14 of 14)

1. protein (cystic fibrosis transmembrane conductance regulator (CFTR))

MPGTIKENII GVSYDEYRYR SVIKA

Sample

Pressure 1 atm, Temperature 298 (±0.5) K, pH 4.0 (±0.1)


#NameIsotope labelingTypeConcentration
1protein (cystic fibrosis transmembrane conductance regulator (CFTR))1.4 mM
2Trifluroethanol43 %

Protein Blocks Logo
Calculated from 13 models in PDB: 1CKW, Strand ID: A Detail


Release date
2000-12-03
Citation
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation
Massiah, M.A., Ko, Y.H., Pedersen, P.L., Mildvan, A.S.
Biochemistry (1999), 38, 7453-7461, PubMed 10360942 , DOI 10.1021/bi9903603 ,
Related entities 1. cystic fibrosis transmembrane conductance regulator (CFTR), : 1 : 6 : 1 : 78 entities Detail
Interaction partners 1. cystic fibrosis transmembrane conductance regulator (CFTR), : 29 interactors Detail
Experiments performed 3 experiments Detail
nullKeywords P25 TFE, cystic fibrosis, peptides, NMR