BMRB: 16171

Barnase bound to d(CGAC), low pressure

Authors

Williamson, M.P., Wilton, D.J.

Assembly

Barnase

Entity

1. Barnase (polymer, Thiol state: not present), 108 monomers, 12117.32 Da Detail

VINTFDGVAD YLQTYHKLPD NYITKSEAQA LGWVASKGNL ADVAPGKSIG GDIFSNREGK LPGKSGRTWR EADINYTSGF RNSDRILYSS DWLIYKTTDA YQTFTKIR

Formula weight

12117.32 Da

Source organism

Bacillus amyloliquefaciens

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.4 %, Completeness: 41.8 %, Completeness (bb): 61.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	41.8 % (271 of 648)	41.8 % (271 of 648)
Backbone	61.4 % (137 of 223)	61.4 % (137 of 223)
Sidechain	31.5 % (134 of 425)	31.5 % (134 of 425)
Aromatic	0.0 % (0 of 68)	0.0 % (0 of 68)
Methyl	90.9 % (50 of 55)	90.9 % (50 of 55)

1. barnase

VINTFDGVAD YLQTYHKLPD NYITKSEAQA LGWVASKGNL ADVAPGKSIG GDIFSNREGK LPGKSGRTWR EADINYTSGF RNSDRILYSS DWLIYKTTDA YQTFTKIR

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 30 atm, Temperature 298 K, pH 6.7

#	Name	Isotope labeling	Type	Concentration
1	barnase	[U-100% 13C; U-100% 15N]		1.1 mM
2	sodium phosphate	natural abundance		30 mM
3	d(CGAC)	natural abundance		4.7 mM
4	H2O	natural abundance		90 %
5	D2O	natural abundance		10 %

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Protein Blocks Logo

Calculated from 10 models in PDB: 2KF5, Strand ID: A Detail

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Release date

2009-09-03

Citation

Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations
Wilton, D.J., Kitahara, R., Akasaka, K., Pandya, M.J., Williamson, M.P.
Biophys. J. (2009), 97, 1482-1490, PubMed 19720037 , DOI 10.1016/j.bpj.2009.06.022 , Abstract

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. Barnase, : 1 : 5 : 36 : 21 entities Detail

Interaction partners 1. Barnase, : 1 interactors Detail

Experiments performed 2 experiments Detail