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The two independent EBP monomers of the dimer have a root mean square deviation (rmsd) of 0.52 A for all Cα.
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2-terminal D1 domain between strands C and C′. Thus, in the crystal structures of EBP with the smaller EMP peptide ligands (11) and the native EBP, L2 does not participate in ligand binding.
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31
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0345468736
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note
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91 hydroxyl (L3).
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32
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0344606675
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note
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Superposition of the individual D1 and D2 domains of the native and EBP-EMP1 structures gives rmsd's of 0.92 Å (90 pairs) and 1.2 Å (98 pairs), respectively, for the Cα atoms.
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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Acta Crystallgr.
, pp. 760
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Bailey, S.1
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58
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67651192516
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1991)
Acta Crystallgr.
, vol.A47
, pp. 195
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Brünger, A.T.1
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59
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Yale Univ. Press, New Haven, CT
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1992)
X-PLOR. Version 3.1: A System for X-ray and NMR
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Brünger, A.T.1
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1994)
J. Mol. Biol.
, vol.243
, pp. 100
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Jiang, J.S.1
Brünger, A.T.2
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1991)
Acta Crystallogr.
, vol.A47
, pp. 110
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Jones, T.A.1
Zou, J.Y.2
Cowan, S.W.3
Kjeldgaard, M.4
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1993)
J. Appl. Crystallogr.
, vol.26
, pp. 283
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Laskowski, R.A.1
MacArthur, M.W.2
Moss, D.S.3
Thornton, J.M.4
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63
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Crystallographic programs and methods. DENZO and SCALEPACK: Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997); AMoRE: J. Navaza, Acta Crystallgr. A50, 157 (1994); CCP4: S. Bailey, ibid., p. 760; X-PLOR: A. T. Brünger, ibid. A47, 195 (1991); A. T. Brünger, X-PLOR. Version 3.1: A system for x-ray and NMR (Yale Univ. Press, New Haven, CT 1992); bulk solvent: J. S. Jiang and A. T. Brünger, J. Mol. Biol. 243, 100 (1994); Program O: T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991); PROCHECK: R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26, 283 (1993); GRASP: A. Nicholls, R. Bharadwaj, B. Honig, Biophys. J. 64, 166 (1993).
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(1993)
Biophys. J.
, vol.64
, pp. 166
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Nicholls, A.1
Bharadwaj, R.2
Honig, B.3
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0344606671
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note
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sym = ΣΣ|li - (l)|/Σli, where (l) is the average of equivalent reflections and the sum is extended over all measured observations for all unique reflections.
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65
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0344606670
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note
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We thank J. Gately Luz for preparation of schematics in Fig. 1, K. Hotta for help with figures, S. Michnick and J. Kelly for helpful discussions, and R. Syed and R. Stroud for providing data for Fig. 2C Supported in part by NIH grant GM49497 (I.A.W.) and the Rueff-Wormser Scholarship Fund (O.L). This is publication 11901-MB from The Scripps Research Institute. The unliganded EBP coordinates have been deposited in the Protein Data Bank (PDB) with the accession code 1em.
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