[Journal logo]

Volume 69 
Part 5 
Page o660  
May 2013  

Received 12 March 2013
Accepted 27 March 2013
Online 5 April 2013

Key indicators
Single-crystal X-ray study
T = 173 K
Mean [sigma](C-C) = 0.003 Å
R = 0.038
wR = 0.087
Data-to-parameter ratio = 16.4
Details
Open access

L-Leucylglycylglycine

aInstitute of Radioisotope Research, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki, Kanagawa 216-8511, Japan,bDepartment of Molecular and Behavioral Neuroscience, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki, Kanagawa 216-8511, Japan, and cSchool of Science, Kitasato University, 1-15-1 Kitasato, Minami-ku, Sagamihara, Kanagawa 252-0373, Japan
Correspondence e-mail: m_ootaki@marianna-u.ac.jp

In the title compound, C10H19N3O4, the N- and C-termini are protonated and ionized, respectively, and the molecule forms a zwitterion. The main chain is in a folded form. In the crystal, the N-terminal -NH3+ group hydrogen bonds to three C-terminal -COO groups and one carbonyl O atom, forming a three-dimensional network. In addition, an N-H...O hydrogen bond between the amide groups of the middle glycine residue and a C-H...O interaction continue along the a-axis direction. The side chains of the leucyl residues form a hydrophobic region along the a axis.

Related literature

For related structures of L-leucylglycylglycine, see: Goswami et al. (1977[Goswami, K. N., Yadava, V. S. & Padmanabhan, V. M. (1977). Acta Cryst. B33, 1280-1283.]); Srikrishnan & Parthasarathy (1987[Srikrishnan, T. & Parthasarathy, R. (1987). Int. J. Pept. Protein Res. 30, 557-563.]); Kiyotani & Sugawara (2012[Kiyotani, T. & Sugawara, Y. (2012). Acta Cryst. C68, o498-o501.]).

[Scheme 1]

Experimental

Crystal data
  • C10H19N3O4

  • Mr = 245.28

  • Orthorhombic, P 21 21 21

  • a = 5.391 (5) Å

  • b = 11.742 (10) Å

  • c = 19.975 (16) Å

  • V = 1264.4 (19) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.10 mm-1

  • T = 173 K

  • 0.48 × 0.18 × 0.08 mm

Data collection
  • Rigaku Mercury CCD area-detecter diffractometer

  • 9374 measured reflections

  • 2887 independent reflections

  • 2200 reflections with I > 2[sigma](I)

  • Rint = 0.070

Refinement
  • R[F2 > 2[sigma](F2)] = 0.038

  • wR(F2) = 0.087

  • S = 0.96

  • 2887 reflections

  • 176 parameters

  • 3 restraints

  • H atoms treated by a mixture of independent and constrained refinement

  • [Delta][rho]max = 0.14 e Å-3

  • [Delta][rho]min = -0.17 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N1-H1...O3i 0.97 (3) 1.78 (3) 2.743 (2) 168 (2)
N1-H2...O4ii 0.92 (2) 1.94 (2) 2.822 (2) 160 (2)
N1-H2...O3ii 0.92 (2) 2.52 (2) 3.260 (2) 138 (2)
N1-H3...O1iii 0.89 (2) 2.45 (2) 3.031 (2) 123 (2)
N1-H3...O3iv 0.89 (2) 2.05 (2) 2.870 (2) 151 (2)
N2-H5...O2v 0.83 (2) 2.05 (2) 2.832 (2) 155 (2)
C1-H4...O1v 1.00 2.33 3.269 (2) 155
Symmetry codes: (i) [-x+{\script{1\over 2}}, -y+1, z-{\script{1\over 2}}]; (ii) [-x-{\script{1\over 2}}, -y+1, z-{\script{1\over 2}}]; (iii) [x-{\script{1\over 2}}, -y+{\script{3\over 2}}, -z+1]; (iv) [-x, y+{\script{1\over 2}}, -z+{\script{3\over 2}}]; (v) x-1, y, z.

Data collection: CrystalClear (Rigaku, 2006[Rigaku (2006). CrystalClear. Rigaku Corporation, Tokyo, Japan.]); cell refinement: CrystalClear; data reduction: CrystalClear; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: Mercury (Macrae et al., 2006[Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.]); software used to prepare material for publication: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]) and Yadokari-XG 2009 (Kabuto et al., 2009[Kabuto, C., Akine, S., Nemoto, T. & Kwon, E. (2009). J. Cryst. Soc. Jpn, 51, 218-224.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: IS5257 ).


Acknowledgements

This work was partially supported by the JSPS KAKENHI (grant Nos. 24659548 and 23540478) and MEXT KAKENHI (grant No. 23108003).

References

Goswami, K. N., Yadava, V. S. & Padmanabhan, V. M. (1977). Acta Cryst. B33, 1280-1283.  [CrossRef] [details] [ISI]
Kabuto, C., Akine, S., Nemoto, T. & Kwon, E. (2009). J. Cryst. Soc. Jpn, 51, 218-224.  [CrossRef]
Kiyotani, T. & Sugawara, Y. (2012). Acta Cryst. C68, o498-o501.  [CSD] [CrossRef] [ChemPort] [details]
Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.  [ISI] [CrossRef] [ChemPort] [details]
Rigaku (2006). CrystalClear. Rigaku Corporation, Tokyo, Japan.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [ChemPort] [details]
Srikrishnan, T. & Parthasarathy, R. (1987). Int. J. Pept. Protein Res. 30, 557-563.  [CrossRef] [ChemPort] [PubMed]


Acta Cryst (2013). E69, o660  [ doi:10.1107/S1600536813008490 ]

This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.