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Volumn 366, Issue 3, 2007, Pages 916-932

Crystal Structures Reveal an Induced-fit Binding of a Substrate-like Aza-peptide Epoxide to SARS Coronavirus Main Peptidase

Author keywords

aza peptide epoxide; induced fit binding; SARS coronavirus main peptidase; structure based drug design; X ray crystallography

Indexed keywords

EPOXIDE; HETEROCYCLIC COMPOUND; PEPTIDASE;

EID: 33846637686     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.078     Document Type: Article
Times cited : (49)

References (54)
  • 2
    • 0038523806 scopus 로고    scopus 로고
    • Identification of a novel coronavirus in patients with severe acute respiratory syndrome
    • Drosten C., Gunther S., Preiser W., van der Werf S., Brodt H.R., Becker S., et al. Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N. Engl. J. Med. 348 (2003) 1967-1976
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1967-1976
    • Drosten, C.1    Gunther, S.2    Preiser, W.3    van der Werf, S.4    Brodt, H.R.5    Becker, S.6
  • 3
    • 0242717589 scopus 로고    scopus 로고
    • Coronavirus as a possible cause of severe acute respiratory syndrome
    • Peiris J.S., Lai S.T., Poon L.L., Guan Y., Yam L.Y., Lim W., et al. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 361 (2003) 1319-1325
    • (2003) Lancet , vol.361 , pp. 1319-1325
    • Peiris, J.S.1    Lai, S.T.2    Poon, L.L.3    Guan, Y.4    Yam, L.Y.5    Lim, W.6
  • 4
    • 21744441372 scopus 로고    scopus 로고
    • Molecular mechanisms of severe acute respiratory syndrome (SARS)
    • Groneberg D.A., Hilgenfeld R., and Zabel P. Molecular mechanisms of severe acute respiratory syndrome (SARS). Respir. Res. 6 (2005) 8
    • (2005) Respir. Res. , vol.6 , pp. 8
    • Groneberg, D.A.1    Hilgenfeld, R.2    Zabel, P.3
  • 5
    • 27944459285 scopus 로고    scopus 로고
    • Structural insights into SARS coronavirus proteins
    • Bartlam M., Yang H., and Rao Z. Structural insights into SARS coronavirus proteins. Curr. Opin. Struct. Biol. 15 (2005) 664-672
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 664-672
    • Bartlam, M.1    Yang, H.2    Rao, Z.3
  • 6
    • 0034990084 scopus 로고    scopus 로고
    • Viral replicase gene products suffice for coronavirus discontinuous transcription
    • Thiel V., Herold J., Schelle B., and Siddell S.G. Viral replicase gene products suffice for coronavirus discontinuous transcription. J. Virol. 75 (2001) 6676-6681
    • (2001) J. Virol. , vol.75 , pp. 6676-6681
    • Thiel, V.1    Herold, J.2    Schelle, B.3    Siddell, S.G.4
  • 8
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J., Snijder E.J., and Gorbalenya A.E. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81 (2000) 853-879
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 9
    • 9144268403 scopus 로고    scopus 로고
    • Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase
    • Fan K., Wei P., Feng Q., Chen S., Huang C., Ma L., et al. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 279 (2004) 1637-1642
    • (2004) J. Biol. Chem. , vol.279 , pp. 1637-1642
    • Fan, K.1    Wei, P.2    Feng, Q.3    Chen, S.4    Huang, C.5    Ma, L.6
  • 10
    • 2642545063 scopus 로고    scopus 로고
    • Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors
    • Shi J., Wei Z., and Song J. Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors. J. Biol. Chem. 279 (2004) 24765-24773
    • (2004) J. Biol. Chem. , vol.279 , pp. 24765-24773
    • Shi, J.1    Wei, Z.2    Song, J.3
  • 11
    • 2442435903 scopus 로고    scopus 로고
    • Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate
    • Kuo C.J., Chi Y.H., Hsu J.T., and Liang P.H. Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate. Biochem. Biophys. Res. Commun. 318 (2004) 862-867
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 862-867
    • Kuo, C.J.1    Chi, Y.H.2    Hsu, J.T.3    Liang, P.H.4
  • 12
    • 9744250871 scopus 로고    scopus 로고
    • Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease
    • Chou C.Y., Chang H.C., Hsu W.C., Lin T.Z., Lin C.H., and Chang G.G. Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease. Biochemistry 43 (2004) 14958-14970
    • (2004) Biochemistry , vol.43 , pp. 14958-14970
    • Chou, C.Y.1    Chang, H.C.2    Hsu, W.C.3    Lin, T.Z.4    Lin, C.H.5    Chang, G.G.6
  • 13
    • 12844272193 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization: biochemical and thermodynamic investigation in conjunction with molecular dynamic simulations
    • Chen S., Chen L., Tan J., Chen J., Du L., Sun T., et al. Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization: biochemical and thermodynamic investigation in conjunction with molecular dynamic simulations. J. Biol. Chem. 280 (2005) 164-173
    • (2005) J. Biol. Chem. , vol.280 , pp. 164-173
    • Chen, S.1    Chen, L.2    Tan, J.3    Chen, J.4    Du, L.5    Sun, T.6
  • 14
    • 20744453676 scopus 로고    scopus 로고
    • Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease
    • Hsu W.C., Chang H.C., Chou C.Y., Tsai P.J., Lin P.I., and Chang G.G. Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. J. Biol. Chem. 280 (2005) 22741-22748
    • (2005) J. Biol. Chem. , vol.280 , pp. 22741-22748
    • Hsu, W.C.1    Chang, H.C.2    Chou, C.Y.3    Tsai, P.J.4    Lin, P.I.5    Chang, G.G.6
  • 15
    • 0030970783 scopus 로고    scopus 로고
    • Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase
    • Ziebuhr J., Heusipp G., and Siddell S.G. Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase. J. Virol. 71 (1997) 3992-3997
    • (1997) J. Virol. , vol.71 , pp. 3992-3997
    • Ziebuhr, J.1    Heusipp, G.2    Siddell, S.G.3
  • 16
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
    • Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., and Hilgenfeld R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 300 (2003) 1763-1767
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, J.2    Wadhwani, P.3    Mesters, J.R.4    Hilgenfeld, R.5
  • 17
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
    • Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., and Hilgenfeld R. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J. 21 (2002) 3213-3224
    • (2002) EMBO J. , vol.21 , pp. 3213-3224
    • Anand, K.1    Palm, G.J.2    Mesters, J.R.3    Siddell, S.G.4    Ziebuhr, J.5    Hilgenfeld, R.6
  • 18
    • 3142613358 scopus 로고    scopus 로고
    • 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism
    • Huang C., Wei P., Fan K., Liu Y., and Lai L. 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism. Biochemistry 43 (2004) 4568-4574
    • (2004) Biochemistry , vol.43 , pp. 4568-4574
    • Huang, C.1    Wei, P.2    Fan, K.3    Liu, Y.4    Lai, L.5
  • 19
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 20
    • 2142713046 scopus 로고    scopus 로고
    • Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro
    • Bacha U., Barrila J., Velazquez-Campoy A., Leavitt S.A., and Freire E. Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro. Biochemistry 43 (2004) 4906-4912
    • (2004) Biochemistry , vol.43 , pp. 4906-4912
    • Bacha, U.1    Barrila, J.2    Velazquez-Campoy, A.3    Leavitt, S.A.4    Freire, E.5
  • 21
    • 9744247544 scopus 로고    scopus 로고
    • Synthesis and evaluation of keto-glutamine analogues as potent inhibitors of severe acute respiratory syndrome 3CLpro
    • Jain R.P., Pettersson H.I., Zhang J., Aull K.D., Fortin P.D., Huitema C., et al. Synthesis and evaluation of keto-glutamine analogues as potent inhibitors of severe acute respiratory syndrome 3CLpro. J. Med. Chem. 47 (2004) 6113-6116
    • (2004) J. Med. Chem. , vol.47 , pp. 6113-6116
    • Jain, R.P.1    Pettersson, H.I.2    Zhang, J.3    Aull, K.D.4    Fortin, P.D.5    Huitema, C.6
  • 22
    • 3142594446 scopus 로고    scopus 로고
    • Small molecules targeting severe acute respiratory syndrome human coronavirus
    • Wu C.Y., Jan J.T., Ma S.H., Kuo C.J., Juan H.F., Cheng Y.S., et al. Small molecules targeting severe acute respiratory syndrome human coronavirus. Proc. Natl Acad. Sci. USA 101 (2004) 10012-10017
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10012-10017
    • Wu, C.Y.1    Jan, J.T.2    Ma, S.H.3    Kuo, C.J.4    Juan, H.F.5    Cheng, Y.S.6
  • 23
    • 4644343545 scopus 로고    scopus 로고
    • Identification of novel small-molecule inhibitors of severe acute respiratory syndrome-associated coronavirus by chemical genetics
    • Kao R.Y., Tsui W.H., Lee T.S., Tanner J.A., Watt R.M., Huang J.D., et al. Identification of novel small-molecule inhibitors of severe acute respiratory syndrome-associated coronavirus by chemical genetics. Chem. Biol. 11 (2004) 1293-1299
    • (2004) Chem. Biol. , vol.11 , pp. 1293-1299
    • Kao, R.Y.1    Tsui, W.H.2    Lee, T.S.3    Tanner, J.A.4    Watt, R.M.5    Huang, J.D.6
  • 25
    • 0345255626 scopus 로고    scopus 로고
    • The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
    • Yang H., Yang M., Ding Y., Liu Y., Lou Z., Zhou Z., et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc. Natl Acad. Sci. USA 100 (2003) 13190-13195
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13190-13195
    • Yang, H.1    Yang, M.2    Ding, Y.3    Liu, Y.4    Lou, Z.5    Zhou, Z.6
  • 26
    • 27444437908 scopus 로고    scopus 로고
    • Design and synthesis of peptidomimetic severe acute respiratory syndrome chymotrypsin-like protease inhibitors
    • Ghosh A.K., Xi K., Ratia K., Santarsiero B.D., Fu W., Harcourt B.H., et al. Design and synthesis of peptidomimetic severe acute respiratory syndrome chymotrypsin-like protease inhibitors. J. Med. Chem. 48 (2005) 6767-6771
    • (2005) J. Med. Chem. , vol.48 , pp. 6767-6771
    • Ghosh, A.K.1    Xi, K.2    Ratia, K.3    Santarsiero, B.D.4    Fu, W.5    Harcourt, B.H.6
  • 27
    • 26444498493 scopus 로고    scopus 로고
    • Design of wide-spectrum inhibitors targeting coronavirus main proteases
    • Yang H., Xie W., Xue X., Yang K., Ma J., Liang W., et al. Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. 3 (2005) e324
    • (2005) PLoS Biol. , vol.3
    • Yang, H.1    Xie, W.2    Xue, X.3    Yang, K.4    Ma, J.5    Liang, W.6
  • 28
    • 21044456863 scopus 로고    scopus 로고
    • Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro
    • Chen L., Gui C., Luo X., Yang Q., Gunther S., Scandella E., et al. Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro. J. Virol. 79 (2005) 7095-7103
    • (2005) J. Virol. , vol.79 , pp. 7095-7103
    • Chen, L.1    Gui, C.2    Luo, X.3    Yang, Q.4    Gunther, S.5    Scandella, E.6
  • 29
    • 27144538090 scopus 로고    scopus 로고
    • Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide
    • Lee T.W., Cherney M.M., Huitema C., Liu J., James K.E., Powers J.C., et al. Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide. J. Mol. Biol. 353 (2005) 1137-1151
    • (2005) J. Mol. Biol. , vol.353 , pp. 1137-1151
    • Lee, T.W.1    Cherney, M.M.2    Huitema, C.3    Liu, J.4    James, K.E.5    Powers, J.C.6
  • 30
    • 0037038317 scopus 로고    scopus 로고
    • Aza-peptide epoxides: a new class of inhibitors selective for clan CD cysteine proteases
    • Asgian J.L., James K.E., Li Z.Z., Carter W., Barrett A.J., Mikolajczyk J., et al. Aza-peptide epoxides: a new class of inhibitors selective for clan CD cysteine proteases. J. Med. Chem. 45 (2002) 4958-4960
    • (2002) J. Med. Chem. , vol.45 , pp. 4958-4960
    • Asgian, J.L.1    James, K.E.2    Li, Z.Z.3    Carter, W.4    Barrett, A.J.5    Mikolajczyk, J.6
  • 31
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • Barrett A.J., and Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 382 (2001) 727-733
    • (2001) Biol. Chem. , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 32
    • 0347358966 scopus 로고    scopus 로고
    • Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases)
    • James K.E., Gotz M.G., Caffrey C.R., Hansell E., Carter W., Barrett A.J., et al. Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases). Biol. Chem. 384 (2003) 1613-1618
    • (2003) Biol. Chem. , vol.384 , pp. 1613-1618
    • James, K.E.1    Gotz, M.G.2    Caffrey, C.R.3    Hansell, E.4    Carter, W.5    Barrett, A.J.6
  • 33
    • 1542328053 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8
    • James K.E., Asgian J.L., Li Z.Z., Ekici O.D., Rubin J.R., Mikolajczyk J., et al. Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8. J. Med. Chem. 47 (2004) 1553-1574
    • (2004) J. Med. Chem. , vol.47 , pp. 1553-1574
    • James, K.E.1    Asgian, J.L.2    Li, Z.Z.3    Ekici, O.D.4    Rubin, J.R.5    Mikolajczyk, J.6
  • 34
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers J.C., Asgian J.L., Ekici O.D., and James K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102 (2002) 4639-4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 35
    • 0036190639 scopus 로고    scopus 로고
    • Mutational analysis of the active centre of coronavirus 3C-like proteases
    • Hegyi A., Friebe A., Gorbalenya A.E., and Ziebuhr J. Mutational analysis of the active centre of coronavirus 3C-like proteases. J. Gen. Virol. 83 (2002) 581-593
    • (2002) J. Gen. Virol. , vol.83 , pp. 581-593
    • Hegyi, A.1    Friebe, A.2    Gorbalenya, A.E.3    Ziebuhr, J.4
  • 36
    • 27344443434 scopus 로고    scopus 로고
    • pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses
    • Tan J., Verschueren K.H., Anand K., Shen J., Yang M., Xu Y., et al. pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses. J. Mol. Biol. 354 (2005) 25-40
    • (2005) J. Mol. Biol. , vol.354 , pp. 25-40
    • Tan, J.1    Verschueren, K.H.2    Anand, K.3    Shen, J.4    Yang, M.5    Xu, Y.6
  • 37
    • 33744470114 scopus 로고    scopus 로고
    • Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer
    • Xu T., Ooi A., Lee H.C., Wilmouth R., Liu D.X., and Lescar J. Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer. Acta Crystallog. sect. F 61 (2005) 964-966
    • (2005) Acta Crystallog. sect. F , vol.61 , pp. 964-966
    • Xu, T.1    Ooi, A.2    Lee, H.C.3    Wilmouth, R.4    Liu, D.X.5    Lescar, J.6
  • 39
    • 11744374008 scopus 로고
    • Dimerization energetics of benzene and aromatic amino acid side-chains
    • Burley S.K., and Petsko G.A. Dimerization energetics of benzene and aromatic amino acid side-chains. J. Am. Chem. Soc. 108 (1986) 7995-8001
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7995-8001
    • Burley, S.K.1    Petsko, G.A.2
  • 40
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles
    • Serrano L., Bycroft M., and Fersht A.R. Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. J. Mol. Biol. 218 (1991) 465-475
    • (1991) J. Mol. Biol. , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 41
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: a mechanism of protein structure stabilization
    • Burley S.K., and Petsko G.A. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229 (1985) 23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 43
    • 33644946136 scopus 로고    scopus 로고
    • The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain
    • Shi J., and Song J. The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain. FEBS J. 273 (2006) 1035-1045
    • (2006) FEBS J. , vol.273 , pp. 1035-1045
    • Shi, J.1    Song, J.2
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 47
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 48
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 49
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 50
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 51
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
    • Satow Y., Cohen G.H., Padlan E.A., and Davies D.R. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. J. Mol. Biol. 190 (1986) 593-604
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 52
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen G.H. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Cryst. 30 (1997) 1160-1161
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1160-1161
    • Cohen, G.H.1
  • 53
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 54
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.