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Jones, E.V.10
Karoutchi, G.I.11
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Morley, A.D.13
Oldham, K.14
Rankine, N.15
Ryan, D.16
Wells, S.L.17
Wood, L.18
Augustin, M.19
Krapp, S.20
Simader, H.21
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12
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67749123530
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note
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There are four protein molecules in the asymmetric unit of the crystal structure of the complex of Cathepsin L with 2. The ranges for the H-H distance and angle between the NH vectors are 2.77 Å to 2.84 Å and 25° to 27°, respectively.
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13
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37049068888
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Abraham M.H., Duce P.D., Prior D.V., Barratt D.G., Morris J.J., and Taylor P.J. J. Chem. Soc., Perkin Trans. 2 (1989) 1355
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Abraham, M.H.1
Duce, P.D.2
Prior, D.V.3
Barratt, D.G.4
Morris, J.J.5
Taylor, P.J.6
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16
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67749138960
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note
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50/M).
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17
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67749117330
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note
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50 for inhibition of Cathepsins L, L2, S, K and B were determined from dose dependent inhibition of cleavage of fluorogenic, AMC-tagged, peptide substrates. See also Ref. 18.
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18
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0033920692
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Hulkower K.I., Butler C.C., Linebaugh B.E., Klaus J.L., Keppler D., Giranda V.L., and Sloane B.F. Eur. J. Biochem. 267 (2000) 4165
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Hulkower, K.I.1
Butler, C.C.2
Linebaugh, B.E.3
Klaus, J.L.4
Keppler, D.5
Giranda, V.L.6
Sloane, B.F.7
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20
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67749115530
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note
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Diffraction data for compound 35 were collected at 100 K on beamline PX at the Swiss Light Source (SLS, Villigen, Switzerland). The structure was solved by molecular replacement and refined to a final resolution of 2.33 Å and R-factor of 25.0% using the CCP4 (Ref. 21) and Coot (Ref. 22) software packages. This structure has been deposited in the RSB (home.rcsb.org) Protein Data Bank (www.rcsb.org/pdb/home/home.do) with reference code 3HWN.
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21
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33744820336
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Number 4; (http://www.ccp4.ac.uk)
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Collaborative Computational Project
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Collaborative Computational Project, Number 4; (http://www.ccp4.ac.uk) Acta Crystallogr. 1994, D50, 760.
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(1994)
Acta Crystallogr
, vol.D50
, pp. 760
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22
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67749117329
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Coot: http://www.ysbl.york.ac.uk/~emsley/coot.
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Coot: http
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