000			01501 a2200421 4500
005			20250513202850.0
264		0	_c20000313
008			200003s 0 0 eng d
022			_a0006-2960
024	7		_a10.1021/bi992822i _2doi
040			_aNLM _beng _cNLM
100	1		_aLamb, A L
245	0	0	_aCrystal structure of the second domain of the human copper chaperone for superoxide dismutase. _h[electronic resource]
260			_bBiochemistry _cFeb 2000
300			_a1589-95 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
650	0	4	_aAmino Acid Sequence
650	0	4	_aBinding Sites
650	0	4	_aCopper _xmetabolism
650	0	4	_aCrystallization
650	0	4	_aCrystallography, X-Ray
650	0	4	_aDimerization
650	0	4	_aHumans
650	0	4	_aMolecular Chaperones _xchemistry
650	0	4	_aMolecular Sequence Data
650	0	4	_aPeptide Fragments _xchemistry
650	0	4	_aProtein Structure, Secondary
650	0	4	_aProtein Structure, Tertiary
650	0	4	_aSequence Homology, Amino Acid
650	0	4	_aSuperoxide Dismutase _xchemistry
650	0	4	_aZinc _xmetabolism
700	1		_aWernimont, A K
700	1		_aPufahl, R A
700	1		_aO'Halloran, T V
700	1		_aRosenzweig, A C
773	0		_tBiochemistry _gvol. 39 _gno. 7 _gp. 1589-95
856	4	0	_uhttps://doi.org/10.1021/bi992822i _zAvailable from publisher's website
999			_c10631550 _d10631550