Structure of the cyclohexapeptide cleromyrine II trihydrate

C29H40N6O7.3H2O, Mr = 638.7, trigonal, P3(1)21, a = 14.190 (2), c = 29.833 (4) A, V = 5202 (1) A3, Z = 6, Dx = 1.22 g cm-3, Cu K alpha, lambda = 1.54178 A, mu = 7.8 cm-1, F(000) = 2052, T = 291 K, R = 0.069 for 1942 observed reflections. The new cyclohexapeptide cleromyrine II was isolated from Cler...

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Veröffentlicht in:	Acta crystallographica. Section C, Crystal structure communications Crystal structure communications, 1990-07, Vol.46 (7), p.1259-1262
Hauptverfasser:	Declercq, J.-P., Tinant, B., Bashwira, S., Hootelé, C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Crystallization Fundamental and applied biological sciences. Psychology Magnetic Resonance Spectroscopy Mass Spectrometry Molecular Sequence Data Molecular Structure Peptides, Cyclic - isolation & purification Plants - analysis Proteins X-Ray Diffraction
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Zusammenfassung:	C29H40N6O7.3H2O, Mr = 638.7, trigonal, P3(1)21, a = 14.190 (2), c = 29.833 (4) A, V = 5202 (1) A3, Z = 6, Dx = 1.22 g cm-3, Cu K alpha, lambda = 1.54178 A, mu = 7.8 cm-1, F(000) = 2052, T = 291 K, R = 0.069 for 1942 observed reflections. The new cyclohexapeptide cleromyrine II was isolated from Clerodendrum myricoides. Its structure was established by spectroscopic and X-ray diffraction methods as cyclo(-Gly-Tyr-Gly-Pro-Leu-Pro-). The conformation essentially consists of two beta-turns including the Pro residues and one central very short antiparallel beta-sheet stabilized by two intramolecular hydrogen bonds: N(Tyr2)...O(Leu5) = 2.94 (2) A and N(Leu5)...O(Tyr2) = 3.02 (2) A.
ISSN:	0108-2701 1600-5759
DOI:	10.1107/S0108270189010656