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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: 32.7 %, Completeness: 13.0 %, Completeness (bb): 21.7 % Detail

Polymer type: polypeptide(L)

Total1H
All13.0 % (86 of 662)13.0 % (86 of 662)
Backbone21.7 % (47 of 217)21.7 % (47 of 217)
Sidechain 8.8 % (39 of 445) 8.8 % (39 of 445)
Aromatic15.7 % (11 of 70)15.7 % (11 of 70)
Methyl 3.6 % (2 of 55) 3.6 % (2 of 55)

1. barnase

AQVINTFDGV ADYLQTYHKL PDNYITKSEA QALGWVASKG NLADVAPGKS IGGDIFSNRE GKLPGKSGRT WREADINYTS GFRNSDRILY SSDWLIYKTT DHYQTFTKIR

Sample

Temperature 310 K, pH 4.5



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 , DOI 10.1021/bi00111a022 ,
Related entities 1. barnase, : 1 : 15 : 9 : 24 : 12 entities Detail
Interaction partners 1. barnase, : 1 interactors Detail
Experiments performed 1 experiments Detail