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Ensemble Solution structure of the phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system
Authors
Venditti, V., Schwieters, C.D., Grishaev, A., Clore, G.
Assembly
phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system
Entity
1. phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system (polymer), 573 monomers, 63344.77 × 2 Da Detail

MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKT


Total weight
126689.54 Da
Max. entity weight
63344.77 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 20.6 %, Completeness: 7.4 %, Completeness (bb): 14.4 % Detail

Polymer type: polypeptide(L)

Total1H15N
All 7.4 % (298 of 4006) 5.4 % (183 of 3408)19.2 % (115 of 598)
Backbone14.4 % (248 of 1725)11.4 % (133 of 1167)20.6 % (115 of 558)
Sidechain 2.2 % (50 of 2281) 2.2 % (50 of 2241) 0.0 % (0 of 40)
Aromatic 0.0 % (0 of 156) 0.0 % (0 of 154) 0.0 % (0 of 2)
Methyl 2.1 % (8 of 378) 2.1 % (8 of 378)

1. entity

MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKT

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 7.4


#NameIsotope labelingTypeConcentration
1EIA[U-13C; U-15N; U-2H]0.4 mM
2TRISnatural abundance20 mM
3EDTAnatural abundance1 mM
4sodium chloridenatural abundance100 mM
5DTTnatural abundance2 mM
6D2Onatural abundance10 %
7H2Onatural abundance90 %

Protein Blocks Logo
Calculated from 11 models in PDB: 2N5T, Strand ID: A, B Detail


Release date
2015-08-30
Citation
Dynamic equilibrium between closed and partially-closed states of the Enzyme I-phosphoenolpyruvate complex from the bacterial phosphotransferase system uncovered by NMR residual dipolar couplings and solution X-ray scattering
Venditti, V., Schwieters, C.D., Grishaev, A., Clore, G.
Proc. Natl. Acad. Sci. U.S.A.
Related entities 1. phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system, : 1 : 4 : 2 : 52 entities Detail
Interaction partners 1. phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system, : 11 interactors Detail
Experiments performed 2 experiments Detail
NMR combined restraints 2 contents Detail
Keywords Multidomain protein, phosphotransferase system