BMRB: 5769

Solution structure of apo-CopAS46V from Bacillus subtilis

Authors

Banci, L., Bertini, I., Ciofi-Baffoni, S., Gonnelli, L., Su, X.C.

Assembly

Potential copper-transporting ATPase

Entity

1. Potential copper-transporting ATPase (polymer, Thiol state: all free), 76 monomers, 8165.353 Da Detail

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVIEGR

Formula weight

8165.353 Da

Source organism

Bacillus subtilis

Exptl. method

NMR

Refine. method

distance geometry,

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.1 %, Completeness: 86.9 %, Completeness (bb): 96.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	86.9 % (445 of 512)	85.2 % (368 of 432)	96.2 % (77 of 80)
Backbone	96.1 % (221 of 230)	96.2 % (150 of 156)	95.9 % (71 of 74)
Sidechain	79.4 % (224 of 282)	79.0 % (218 of 276)	100.0 % (6 of 6)
Aromatic	50.0 % (5 of 10)	50.0 % (5 of 10)
Methyl	94.0 % (47 of 50)	94.0 % (47 of 50)

1. CPx-type ATPase CopA

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVIEGR

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Sample

Pressure 1 atm, Temperature 298 (±0.1) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	CPx-type ATPase CopA	[U-15N]		1.2 mM
2	phosphate			20 mM
3	DTT			2 mM
4	H2O			90 %
5	D2O			10 %

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Calculated from 30 models in PDB: 1OQ3, Strand ID: A Detail

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Release date

2003-09-07

Citation

A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis
Banci, L., Bertini, I., Ciofi-Baffoni, S., Gonnelli, L., Su, X.C.
J. Mol. Biol. (2003), 331, 473-484, PubMed 12888353 , DOI: , Abstract

Related entities 1. Potential copper-transporting ATPase, : 1 : 2 : 2 : 285 entities Detail

Interaction partners 1. Potential copper-transporting ATPase, : 2 interactors Detail

Experiments performed 5 experiments Detail