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Structure of the coat protein in fd filamentous bacteriophage particles
Authors
Zeri, A.C., Mesleh, M.F., Nevzorov, A.A., Opella, S.J.
Assembly
Major coat protein
Entity
1. Major coat protein (polymer, Thiol state: not present), 50 monomers, 5206.980 Da Detail

AEGDDPAKAA FDSLQASATE MIGYAWAMVV VIVGATIGIK LFKKFTSKAS


Formula weight
5206.98 Da
Source organism
Filamentous phage
Exptl. method
NMR
Refine. method
SOLID-STATE NMR SPECTROSCOPY
Data set
assigned_chemical_shifts, RDCs
Chem. Shift Complete
Sequence coverage: 88.0 %, Completeness: 86.3 %, Completeness (bb): 89.8 % Detail

Polymer type: polypeptide(L)

Total15N
All86.3 % (44 of 51)86.3 % (44 of 51)
Backbone89.8 % (44 of 49)89.8 % (44 of 49)
Sidechain 0.0 % (0 of 2) 0.0 % (0 of 2)
Aromatic 0.0 % (0 of 1) 0.0 % (0 of 1)

1. bacteriophage fd major coat protein

AEGDDPAKAA FDSLQASATE MIGYAWAMVV VIVGATIGIK LFKKFTSKAS

Sample

Pressure 1 atm, Temperature 338 (±1) K, pH 8.0 (±0.2), Details bacteriophage particles were suspended in aqueous buffer


#NameIsotope labelingTypeConcentration
1bacteriophage fd major coat protein[U-15N]50 mg/mL
2sodium borate buffer5 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 1NH4, Strand ID: A Detail


RDC
43 RDC values in 1 lists
Field strength (1H) 550 MHz, Pressure 1 atm, Temperature 338 (±1) K, pH 8.0 (±0.2) Detail
Release date
2003-10-16
Citation
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
Zeri, A.C., Mesleh, M.F., Nevzorov, A.A., Opella, S.J.
Proc. Natl. Acad. Sci. U. S. A. (2003), 100, 6458-6463, PubMed 12750469 , DOI 10.1073/pnas.1132059100 ,
Related entities 1. Major coat protein, : 1 : 2 : 9 : 23 entities Detail
Experiments performed 2 experiments Detail
Keywords ALPHA HELIX, bacteriophage, solid-state NMR, PISEMA