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BMRB: 5813

1P6T

The solution structure of the whole N-terminal domain of the ATPase CopA from Bacillus Subtilis. Implications for the function

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), 151 monomers, 16380.56 Da Detail

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVTEKAEFDI EGMTCAACAN RIEKRLNKIE GVANAPVNFA LETVTVEYNP KEASVSDLKE AVDKLGYKLK LKGEQDSIEG R

Formula weight

16380.56 Da

Source organism

Bacillus subtilis subsp. subtilis str. 168

Exptl. method

NMR

Refine. method

distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 90.4 %, Completeness (bb): 95.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	90.4 % (1529 of 1692)	91.3 % (801 of 877)	87.0 % (571 of 656)	98.7 % (157 of 159)
Backbone	95.2 % (855 of 898)	97.4 % (300 of 308)	92.6 % (410 of 443)	98.6 % (145 of 147)
Sidechain	86.3 % (807 of 935)	88.0 % (501 of 569)	83.1 % (294 of 354)	100.0 % (12 of 12)
Aromatic	30.4 % (17 of 56)	50.0 % (14 of 28)	10.7 % (3 of 28)
Methyl	93.5 % (174 of 186)	96.8 % (90 of 93)	90.3 % (84 of 93)

1. copper-transporting ATPase CopA

MLSEQKEIAM QVSGMTCAAC AARIEKGLKR MPGVTDANVN LATETVNVIY DPAETGTAAI QEKIEKLGYH VVTEKAEFDI EGMTCAACAN RIEKRLNKIE GVANAPVNFA LETVTVEYNP KEASVSDLKE AVDKLGYKLK LKGEQDSIEG R

Show sample condition

Sample

Pressure 1 (±0.01) atm, Temperature 298 (±0.1) K, pH 7.0 (±0.1)

#	Name	Isotope labeling	Concentration
1	copper-transporting ATPase CopA	[U-95% 13C; U-90% 15N]	1.5 mM
2	phosphate		20 mM
3	H2O		90 %
4	D2O		10 %
5	DTT		2.0 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	1.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: 2.65 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	1.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: 2.65 ppm, Outliers: 3 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	1.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 7 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	TMS	methyl protons	null	indirect	0.2514495
¹H	TMS	methyl protons	internal	direct	1.0
¹⁵N	TMS	methyl protons	null	indirect	0.1013291

Referencing offset: 2.92 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 30 models in PDB: 1P6T, Strand ID: A Detail

Release date

2003-12-17

Citation

Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis
Banci, L., Bertini, I., Ciofi-Baffoni, S., Gonnelli, L., Su, X.C.
J. Biol. Chem. (2003), 278, 50506-50513, PubMed 14514665 , DOI 10.1074/jbc.M307389200 , Abstract

Related entities 1. Potential copper-transporting ATPase, : 1 : 1 : 154 entities Detail

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

More details for 2 interactors identified by 2 citations

Experiments performed 10 experiments Detail

1 2D NOESY