BMRB: 2070

Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR

Authors

Meiering, E.M., Bycroft, M., Fersht, A.R.

Assembly

barnase

Entity

1. barnase (polymer), 110 monomers, 12382.59 Da Detail

AQVINTFDGV ADYLQTYHKL PDNYITKSEA QALGWVASKG NLADVAPGKS IGGDIFSNRE GKLPGKSGRT WREADINYTS GFRNSDRILY SSDWLIYKTT DHYQTFTKIR

Formula weight

12382.59 Da

Source organism

Bacillus amyloliquefaciens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 38.2 %, Completeness: 13.4 %, Completeness (bb): 22.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	13.4 % (89 of 662)	13.4 % (89 of 662)
Backbone	22.9 % (52 of 227)	22.9 % (52 of 227)
Sidechain	8.5 % (37 of 435)	8.5 % (37 of 435)
Aromatic	7.1 % (5 of 70)	7.1 % (5 of 70)
Methyl	16.4 % (9 of 55)	16.4 % (9 of 55)

1. barnase

AQVINTFDGV ADYLQTYHKL PDNYITKSEA QALGWVASKG NLADVAPGKS IGGDIFSNRE GKLPGKSGRT WREADINYTS GFRNSDRILY SSDWLIYKTT DHYQTFTKIR

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Sample

Temperature 300 K, pH 4.5

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Release date

1995-07-30

Citation

Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR
Meiering, E.M., Bycroft, M., Fersht, A.R.
Biochemistry (1991), 30, 11348-11356, PubMed 1958671 , Abstract

Related entities 1. barnase, : 1 : 15 : 9 : 26 : 12 entities Detail

Interaction partners 1. barnase, : 1 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail