BMRB: 1996

NMR Study of the Phosphate-Binding Elements of Escherichia coli Elongation Factor Tu Catalytic Domain

Authors

Lowry, D.F., Cool, R.H., Redfield, A.G., Parmeggiani, A.

Assembly

elongation factor Tu

Entity

1. elongation factor Tu (polymer), 200 monomers, 21837.42 Da Detail

SKEKFERTKP HVNVGTIGHV DHGKTTLTAA ITTVLAKTYG GAARAFDQID NAPEEKARGI TINTSHVEYD TPTRHYAHVD CPGGADYVKN MITGAAQMDG AILVVAATDG PMPQTREHIL LGRQVGVPYI IVFLNKCDMV DDEELLELVE MEVRELLSQY DFPGDDTPIV RGSALKALEG DAEWEAKILE LAGFLDSYIP

Formula weight

21837.42 Da

Source organism

Escherichia coli

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.5 %, Completeness: 1.4 %, Completeness (bb): 2.7 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	1.4 % (19 of 1347)	1.2 % (14 of 1146)	2.5 % (5 of 201)
Backbone	2.7 % (16 of 597)	2.7 % (11 of 407)	2.6 % (5 of 190)
Sidechain	0.5 % (4 of 750)	0.5 % (4 of 739)	0.0 % (0 of 11)
Aromatic	0.0 % (0 of 74)	0.0 % (0 of 73)	0.0 % (0 of 1)
Methyl	1.6 % (2 of 126)	1.6 % (2 of 126)

1. elongation factor Tu

SKEKFERTKP HVNVGTIGHV DHGKTTLTAA ITTVLAKTYG GAARAFDQID NAPEEKARGI TINTSHVEYD TPTRHYAHVD CPGGADYVKN MITGAAQMDG AILVVAATDG PMPQTREHIL LGRQVGVPYI IVFLNKCDMV DDEELLELVE MEVRELLSQY DFPGDDTPIV RGSALKALEG DAEWEAKILE LAGFLDSYIP

Show sample condition

Sample

Temperature 290 K, pH 7.6

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Release date

1995-07-30

Citation

NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain
Lowry, D.F., Cool, R.H., Redfield, A.G., Parmeggiani, A.
Biochemistry (1991), 30, 10872-10877, PubMed 1932010 , DOI 10.1021/bi00109a010 , Abstract

Related entities 1. elongation factor Tu, : 1 : 50 : 221 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail