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Three-Dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli
Authors
van Nuland, N.A.J., van Dijk, A.A., Dijkstra, K., van Hoesel, F.H.J., Scheek, R.M., Robillard, G.T.
Assembly
phosphocarrier protein HPr
Entity
1. phosphocarrier protein HPr (polymer), 85 monomers, 9119.249 Da Detail

MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV VTISAEGEDE QKAVEHLVKL MAELE


Formula weight
9119.249 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 36.7 %, Completeness (bb): 67.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All36.7 % (353 of 962)36.2 % (179 of 494)24.5 % (92 of 376)89.1 % (82 of 92)
Backbone67.6 % (338 of 500)99.4 % (167 of 168)35.7 % (89 of 249)98.8 % (82 of 83)
Sidechain 3.1 % (17 of 541) 3.7 % (12 of 326) 2.4 % (5 of 206) 0.0 % (0 of 9)
Aromatic 0.0 % (0 of 48) 0.0 % (0 of 24) 0.0 % (0 of 24)
Methyl 5.5 % (6 of 110) 5.5 % (3 of 55) 5.5 % (3 of 55)

1. phosphocarrier protein HPr

MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV VTISAEGEDE QKAVEHLVKL MAELE

Sample

Temperature 303 K, pH 6.5



Release date
1995-07-30
Citation
Three-dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignment of backbone resonances
van Nuland, N.A.J., van Dijk, A.A., Dijkstra, K., van Hoesel, F.H.J., Scheek, R.M., Robillard, G.T.
Eur. J. Biochem. (1992), 203, 483-491, PubMed 1735433 , DOI 10.1111/j.1432-1033.1992.tb16573.x ,
Related entities 1. phosphocarrier protein HPr, : 1 : 15 : 1 : 4 : 89 entities Detail
Interaction partners 1. phosphocarrier protein HPr, : 10 interactors Detail
Experiments performed 1 experiments Detail