000 01292 a2200361 4500
005 20250515043002.0
264 0 _c20070109
008 200701s 0 0 eng d
022 _a0925-2738
024 7 _a10.1007/s10858-006-9073-2
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aPagano, Katiuscia
245 0 0 _aNMR solution structure of the acylphosphatase from Escherichia coli.
_h[electronic resource]
260 _bJournal of biomolecular NMR
_cNov 2006
300 _a199-204 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAcid Anhydride Hydrolases
_xchemistry
650 0 4 _aAmino Acid Sequence
650 0 4 _aEscherichia coli
_xchemistry
650 0 4 _aModels, Molecular
650 0 4 _aNuclear Magnetic Resonance, Biomolecular
650 0 4 _aProtein Conformation
650 0 4 _aSequence Alignment
650 0 4 _aAcylphosphatase
700 1 _aRamazzotti, Matteo
700 1 _aViglino, Paolo
700 1 _aEsposito, Gennaro
700 1 _aDegl'Innocenti, Donatella
700 1 _aTaddei, Niccolò
700 1 _aCorazza, Alessandra
773 0 _tJournal of biomolecular NMR
_gvol. 36
_gno. 3
_gp. 199-204
856 4 0 _uhttps://doi.org/10.1007/s10858-006-9073-2
_zAvailable from publisher's website
999 _c16598956
_d16598956