메뉴 건너뛰기




Volumn , Issue , 2005, Pages 185-222

Retrieval and Validation of Structural Information

Author keywords

[No Author keywords available]

Indexed keywords


EID: 36549014038     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9780849361432-13     Document Type: Chapter
Times cited : (2)

References (122)
  • 1
    • 0037252704 scopus 로고    scopus 로고
    • The Molecular Biology Database Collection: 2003 Update
    • AD Baxevanis, The Molecular Biology Database Collection: 2003 Update, Nucleic Acids Res., 31, 1-12, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1-12
    • Baxevanis, A.D.1
  • 5
    • 0031182215 scopus 로고    scopus 로고
    • The first years of the Protein Data Bank
    • EF Meyer, The first years of the Protein Data Bank, Prot. Sci., 6, 1591-1597, 1997.
    • (1997) Prot. Sci. , vol.6 , pp. 1591-1597
    • Meyer, E.F.1
  • 6
    • 84909965442 scopus 로고
    • Protein Data Bank, Acta Crystallogr., B29, 1746, 1973.
    • (1973) Acta Crystallogr. , vol.B29 , pp. 1746
  • 12
  • 14
    • 0033400944 scopus 로고    scopus 로고
    • An analysis of the Protein Data Bank in search of temporal and global trends
    • H Weissig and PE Bourne. An analysis of the Protein Data Bank in search of temporal and global trends, Bioinformatics, 15, 807-831, 1999.
    • (1999) Bioinformatics , vol.15 , pp. 807-831
    • Weissig, H.1    Bourne, P.E.2
  • 16
    • 0001752768 scopus 로고    scopus 로고
    • The Cambridge Structural Database: A quarter of a million crystal structures and rising
    • FH Allen, The Cambridge Structural Database: a quarter of a million crystal structures and rising, Acta Crystallogr., B 58, 380-388, 2002.
    • (2002) Acta Crystallogr., B , vol.58 , pp. 380-388
    • Allen, F.H.1
  • 18
    • 0016367068 scopus 로고
    • Storage and retrieval of macromolecular structural data
    • EF Meyer Jr., Storage and retrieval of macromolecular structural data. Biopolymers, 13, 419-422, 1974.
    • (1974) Biopolymers , vol.13 , pp. 419-422
    • Meyer, E.F.1
  • 19
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • WR Pearson and DJ Lipman, Improved tools for biological sequence comparison, Proc. Natl. Acad. Sci. U.S., 85, 2444-2448, 1988.
    • (1988) Proc. Natl. Acad. Sci. U.S. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 20
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures
    • RA Laskowski, PDBsum: summaries and analyses of PDB structures, Nucleic Acids Res, 29, 221-222, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 23
    • 0033979782 scopus 로고    scopus 로고
    • The IMB Jena Image Library of biological macromolecules
    • J Reichert, A Jabs, P Slickers, and J Suhnel, The IMB Jena Image Library of biological macromolecules, Nucleic Acids Res., 28, 246-249, 2000.
    • (2000) Nucleic Acids Res , vol.28 , pp. 246-249
    • Reichert, J.1    Jabs, A.2    Slickers, P.3    Suhnel, J.4
  • 24
    • 0030461976 scopus 로고    scopus 로고
    • The PDBFINDER database: A summary of PDB, DSSP and HSSP information with added value
    • RW Hooft, C Sander, M Scharf, and G Vriend, The PDBFINDER database: a summary of PDB, DSSP and HSSP information with added value, Comput. Appl. Biosci, 12, 525-529, 1996.
    • (1996) Comput. Appl. Biosci , vol.12 , pp. 525-529
    • Rw Hooft, C.1    Sander, M.2    Scharfvriend, G.3
  • 25
    • 0029967362 scopus 로고    scopus 로고
    • SRS: Information retrieval system for molecular biology data banks
    • T Etzold, A Ulyanov, and P Argos, SRS: information retrieval system for molecular biology data banks, Methods Enzymol., 266, 114-128, 1996.
    • (1996) Methods Enzymol , vol.266 , pp. 114-128
    • Etzold, T.1    Ulyanov, A.2    Argos, P.3
  • 26
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • L Holm and C Sander, The FSSP database of structurally aligned protein fold families, Nucleic Acids Res., 22, 3600-3609, 1994.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 27
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • AG Murzin, SE Brenner, T Hubbard, and C Chothia, SCOP: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol., 247, 536-540, 1995.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 29
    • 0033200307 scopus 로고    scopus 로고
    • A systematic comparison of protein structure classifications: SCOP, CATH and FSSP
    • C Hadley and DT Jones, A systematic comparison of protein structure classifications: SCOP, CATH and FSSP, Structure, 7, 1099-1112, 1999.
    • (1999) Structure , vol.7 , pp. 1099-1112
    • Hadley, C.1    Jones, D.T.2
  • 31
    • 0029973830 scopus 로고    scopus 로고
    • Derivation of 3D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteases and lipases
    • AC Wallace, RA Laskowski, and JM Thornton, Derivation of 3D coordinate templates for searching structural databases: Application to Ser-His-Asp catalytic triads in the serine proteases and lipases, Prot. Sci., 5, 1001-1013, 1996.
    • (1996) Prot. Sci. , vol.5 , pp. 1001-1013
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 32
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • GJ Kleywegt, Recognition of spatial motifs in protein structures, J. Mol. Biol., 285, 1887-1897, 1999.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 33
    • 0036108480 scopus 로고    scopus 로고
    • Interactive motif and fold recognition in protein structures
    • D Madsen and GJ Kleywegt, Interactive motif and fold recognition in protein structures, J. Appl. Crystallogr., 35, 137-139, 2002.
    • (2002) J. Appl. Crystallogr. , vol.35 , pp. 137-139
    • Madsen, D.1    Kleywegt, G.J.2
  • 34
    • 0037424601 scopus 로고    scopus 로고
    • A model for statistical significance of local similarities in structure
    • A Stark, S Sunyaev, and RB Russell, A model for statistical significance of local similarities in structure, J. Mol. Biol., 326, 1307-1316, 2003.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1307-1316
    • Stark, A.1    Sunyaev, S.2    Russell, R.B.3
  • 35
    • 0032214649 scopus 로고    scopus 로고
    • Databases for protein-ligand complexes
    • M Hendlich, Databases for protein-ligand complexes, Acta Crystallogr., D54, 1178-1182, 1998.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 1178-1182
    • Hendlich, M.1
  • 36
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • GJ Kleywegt and TA Jones, Databases in protein crystallography, Acta Crystallogr., D54, 1119-1131, 1998.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 0035102149 scopus 로고    scopus 로고
    • 3Dee: A database of protein structural domains
    • AS Siddiqui, U Dengler, and GJ Barton, 3Dee: a database of protein structural domains, Bioinformatics, 17, 200-201, 2001.
    • (2001) Bioinformatics , vol.17 , pp. 200-201
    • Siddiqui, A.S.1    Dengler, U.2    Barton, G.J.3
  • 38
    • 0037246863 scopus 로고    scopus 로고
    • MolMovDB: Analysis and visualization of conformational change and structural flexibility
    • N Echols, D Milburn, and M Gerstein, MolMovDB: analysis and visualization of conformational change and structural flexibility, Nucleic Acids Res., 31, 478-482, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 40
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • C Sander and R Schneider, Database of homology-derived protein structures and the structural meaning of sequence alignment, Proteins Struct. Funct. Genet., 9, 56-68, 1991.
    • (1991) Proteins Struct. Funct. Genet. , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 41
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • K Henrick and JM Thornton, PQS: a protein quaternary structure file server, Trends Biochem. Sci., 23, 358-361, 1998.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 42
    • 0033829056 scopus 로고    scopus 로고
    • Browsing the SLoop database of structurally classified loops connecting elements of protein secondary structure
    • DF Burke, CM Deane, and TL Blundell, Browsing the SLoop database of structurally classified loops connecting elements of protein secondary structure, Bioinformatics, 16, 513-519, 2000.
    • (2000) Bioinformatics , vol.16 , pp. 513-519
    • Burke, D.F.1    Deane, C.M.2    Blundell, T.L.3
  • 43
    • 0036171255 scopus 로고    scopus 로고
    • SACS — self-maintaining database of antibody crystal structure information
    • LC Allcorn and AC Martin, SACS — self-maintaining database of antibody crystal structure information, Bioinformatics, 18, 175-181, 2002.
    • (2002) Bioinformatics , vol.18 , pp. 175-181
    • Allcorn, L.C.1    Martin, A.C.2
  • 44
    • 0036892381 scopus 로고    scopus 로고
    • HIVdb: A database of the structures of human immunodeficiency virus protease
    • J Vondrasek and A Wlodawer, HIVdb: a database of the structures of human immunodeficiency virus protease, Proteins Struct. Funct. Genet., 49, 429-431, 2002.
    • (2002) Proteins Struct. Funct. Genet. , vol.49 , pp. 429-431
    • Vondrasek, J.1    Wlodawer, A.2
  • 45
    • 0037249551 scopus 로고    scopus 로고
    • RNABase: An annotated database of RNA structures
    • VL Murthy and GD Rose, RNABase: an annotated database of RNA structures, Nucleic Acids Res., 31, 502-504, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 502-504
    • Murthy, V.L.1    Rose, G.D.2
  • 46
    • 0037251966 scopus 로고    scopus 로고
    • SDAP: Database and computational tools for allergenic proteins
    • O Ivanciuc, CH Schein, and W Braun, SDAP: database and computational tools for allergenic proteins, Nucleic Acids Res., 31, 359-362, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 359-362
    • Ivanciuc, O.1    Schein, C.H.2    Braun, W.3
  • 49
    • 0035170508 scopus 로고    scopus 로고
    • Collecting and harvesting biological data: The GPCRDB and NucleaRDB information systems
    • F Horn, G Vriend, and FE Cohen, Collecting and harvesting biological data: the GPCRDB and NucleaRDB information systems, Nucleic Acids Res., 29, 346-349,2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 346-349
    • Horn, F.1    Vriend, G.2    Cohen, F.E.3
  • 51
    • 0032214097 scopus 로고    scopus 로고
    • HAD, a data bank of heavy-atom binding sites in protein crystals: A resource for use in multiple isomorphous replacement and anomalous scattering
    • SA Islam, D Carvin, MJ Sternberg, and TL Blundell, HAD, a data bank of heavy-atom binding sites in protein crystals: a resource for use in multiple isomorphous replacement and anomalous scattering, Acta Crystallogr., D 54, 1199-1206, 1998.
    • (1998) Acta Crystallogr., D , vol.54 , pp. 1199-1206
    • Islam, S.A.1    Carvin, D.2    Sternberg, M.J.3    Blundell, T.L.4
  • 52
    • 0000898340 scopus 로고
    • The Biological Macromolecule Crystallization Database, Version 3.0: New features, data, and the NASA Archive for Protein Crystal Growth Data
    • GL Gilliland, M Tung, DM Blakeslee, and J Ladner, The Biological Macromolecule Crystallization Database, Version 3.0: new features, data, and the NASA Archive for Protein Crystal Growth Data, Acta Crystallogr., D50, 408-413, 1994.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 408-413
    • Gilliland, G.L.1    Tung, M.2    Blakeslee, D.M.3    Ladner, J.4
  • 53
    • 0035162787 scopus 로고    scopus 로고
    • The RESID Database of protein structure modifications and the NRL-3D Sequence-Structure Database
    • JS Garavelli, Z Hou, N Pattabiraman, and RM Stephens, The RESID Database of protein structure modifications and the NRL-3D Sequence-Structure Database, Nucleic Acids Res., 29, 199-201, 2001.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 199-201
    • Js Garavelli, Z.1    Hou, N.P.2    Stephens, R.M.3
  • 54
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • G Wang and RL Dunbrack, PISCES: a protein sequence culling server, Bioinformatics, 12, 1589-1591, 2003.
    • (2003) Bioinformatics , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.2
  • 55
    • 0036089481 scopus 로고    scopus 로고
    • MODBASE, a database of annotated comparative protein structure models
    • U Pieper, N Eswar, AC Stuart, VA Ilyin, and A Sali, MODBASE, a database of annotated comparative protein structure models, Nucleic Acids Res., 30, 255-259, 2002.
    • (2002) Nucleic Acids Res , vol.30 , pp. 255-259
    • Pieper, U.1    Eswar, N.2    Va Ilyin, A.C.S.3    Sali, A.4
  • 56
    • 0036169142 scopus 로고    scopus 로고
    • LigBase: A database of families of aligned ligand binding sites in known protein sequences and structures
    • AC Stuart, VA Ilyin, and A Sali, LigBase: a database of families of aligned ligand binding sites in known protein sequences and structures, Bioinformatics, 18, 200-201 , 2002.
    • (2002) Bioinformatics , vol.18 , pp. 200-201
    • Stuart, A.C.1    Ilyin, V.A.2    Sali, A.3
  • 59
    • 0036850213 scopus 로고    scopus 로고
    • The SUPERFAMILY database in structural genomics
    • J Gough, The SUPERFAMILY database in structural genomics, Acta Crystallogr., D 58, 1897-1900, 2002.
    • (2002) Acta Crystallogr., D , vol.58 , pp. 1897-1900
    • Gough, J.1
  • 60
    • 0035870634 scopus 로고    scopus 로고
    • PartsList: A web-based system for dynamically ranking protein folds based on disparate attributes, including whole-genome expression and interaction information
    • J Qian, B Stenger, CA Wilson, J Lin, R Jansen, SA Teichmann, J Park, WG Krebs, H Yu, V Alexandrov, N Echols, and M Gerstein, PartsList: a web-based system for dynamically ranking protein folds based on disparate attributes, including whole-genome expression and interaction information, Nucleic Acids Res., 29, 1750-1764, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1750-1764
    • Qian, J.1    Stenger, B.2    Ca Wilson, J.3    Lin, R.J.4    Teichmann, S.A.5    Park, J.6    Wg Krebs, H.Y.7    Alexandrov, V.8    Echols, N.9    Gerstein, M.10
  • 62
    • 0001644632 scopus 로고
    • Between objectivity and subjectivity
    • CI Branden and TA Jones, Between objectivity and subjectivity, Nature, 343, 687-689, 1990.
    • (1990) Nature , vol.343 , pp. 687-689
    • Branden, C.I.1    Jones, T.A.2
  • 63
    • 0034013435 scopus 로고    scopus 로고
    • Validation of protein crystal structures
    • GJ Kleywegt, Validation of protein crystal structures, Acta Crystallogr., D56, 249-265, 2000.
    • (2000) Acta Crystallogr., D , vol.56 , pp. 249-265
    • Kleywegt, G.J.1
  • 64
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • GJ Kleywegt and TA Jones, Where freedom is given, liberties are taken, Structure, 3, 535-540, 1995.
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 65
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • GJ Kleywegt, Use of non-crystallographic symmetry in protein structure refinement, Acta Crystallogr., D52, 842-857, 1996.
    • (1996) Acta Crystallogr., D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 66
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • TA Jones, JY Zou, SW Cowan, and M Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr., A47, 110-119, 1991.
    • (1991) Acta Crystallogr., A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 67
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • GJ Kleywegt and AT Brunger, Checking your imagination: applications of the free R value, Structure,4, 897-904, 1996.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brunger, A.T.2
  • 68
    • 0030022569 scopus 로고    scopus 로고
    • Report of a workshop on the use of statistical validators in protein X-ray crystallography
    • E Dodson, GJ Kleywegt, and KS Wilson, Report of a workshop on the use of statistical validators in protein X-ray crystallography, Acta Crystallogr., D52, 228-234, 1996.
    • (1996) Acta Crystallogr., D , vol.52 , pp. 228-234
    • Dodson, E.1    Kleywegt, G.J.2    Wilson, K.S.3
  • 69
    • 0030845843 scopus 로고    scopus 로고
    • Model-building and refinement practice
    • GJ Kleywegt and TA Jones, Model-building and refinement practice, Methods Enzy-mol., 277, 208-230, 1997.
    • (1997) Methods Enzy-Mol , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.A.2
  • 70
    • 0030841587 scopus 로고    scopus 로고
    • Electron density map interpretation
    • TA Jones and M Kjeldgaard, Electron density map interpretation, Methods Enzymol., 277, 173-208, 1997.
    • (1997) Methods Enzymol , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 71
    • 0030918784 scopus 로고    scopus 로고
    • Chirality errors in nucleic acid structures
    • P Schultze and J Feigon, Chirality errors in nucleic acid structures, Nature, 387, 668-668, 1997.
    • (1997) Nature , vol.387 , pp. 668-668
    • Schultze, P.1    Feigon, J.2
  • 74
    • 0038336897 scopus 로고    scopus 로고
    • Applications and limitations of X-ray crystallographic data in structure-based ligand and drug design
    • AM Davis, SJ Teague, and GJ Kleywegt, Applications and limitations of X-ray crystallographic data in structure-based ligand and drug design, Angew Chem. Int. Ed., 42, 2718-2736, 2003.
    • (2003) Angew Chem. Int. Ed. , vol.42 , pp. 2718-2736
    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 75
    • 0030512814 scopus 로고    scopus 로고
    • A re-evaluation of the crystal structure of chloromuconate cycloisomerase
    • GJ Kleywegt, H Hoier, and TA Jones, A re-evaluation of the crystal structure of chloromuconate cycloisomerase, Acta Crystallogr., D52, 858-863, 1996.
    • (1996) Acta Crystallogr., D , vol.52 , pp. 858-863
    • Kleywegt, G.J.1    Hoier, H.2    Jones, T.A.3
  • 76
    • 0026055156 scopus 로고
    • Analysis of steric strain in the polypeptide backbone of protein models
    • O Herzberg and J Moult, Analysis of steric strain in the polypeptide backbone of protein models, Proteins Struct. Funct. Genet., 11, 223-229, 1991.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 77
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • AT Brunger, Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, 355, 472-475, 1992.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 78
    • 0026610767 scopus 로고
    • Assessment of protein models with threedimensional profiles
    • R Luthy, JU Bowie, and D Eisenberg, Assessment of protein models with threedimensional profiles, Nature, 356, 83-85, 1992.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 79
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • GJ Kleywegt and TA Jones, Phi/Psi-chology: Ramachandran revisited, Structure, 4, 1395-1400, 1996.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 82
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • J Janin, S Wodak, M Levitt, and B Maigret, Conformation of amino acid side-chains in proteins, J. Mol. Biol., 125, 357-386, 1978.
    • (1978) J. Mol. Biol. , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigret, B.4
  • 84
    • 0027542118 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • G Vriend and C Sander, Quality control of protein models: directional atomic contact analysis, J. Appl. Crystallogr., 26, 47-60, 1993.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2
  • 85
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • J Kuszewski, AM Gronenborn, and GM Clore, Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases, Protein Sci., 5, 1067-1080, 1996.
    • (1996) Protein Sci , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 86
    • 0032707718 scopus 로고    scopus 로고
    • Validation of nuclear magnetic resonance structures of proteins and nucleic acids: Hydrogen geometry and nomenclature
    • JF Doreleijers, G Vriend, ML Raves, and R Kaptein, Validation of nuclear magnetic resonance structures of proteins and nucleic acids: hydrogen geometry and nomenclature, Proteins Struct. Funct. Genet., 37, 404-416, 1999.
    • (1999) Proteins Struct. Funct. Genet. , vol.37 , pp. 404-416
    • Jf Doreleijers, G.V.1    Raves, M.L.2    Kaptein, R.3
  • 87
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • A Bax, Weak alignment offers new NMR opportunities to study protein structure and dynamics, Protein Sci., 12, 1-16, 2003.
    • (2003) Protein Sci. , vol.12 , pp. 1-16
    • Bax, A.1
  • 88
    • 0027172878 scopus 로고
    • Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy
    • GM Clore, MA Robien, and AM Gronenborn, Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy, J. Mol. Biol., 231, 82-102, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 82-102
    • Clore, G.M.1    Robien, M.A.2    Gronenborn, A.M.3
  • 89
    • 0028232369 scopus 로고
    • An assessment of the precision and accuracy of protein structures determined by NMR
    • D Zhao and O Jardetzky, An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors, J. Mol. Biol., 239, 601-607, 1994.
    • (1994) Dependence on Distance Errors, J. Mol. Biol. , vol.239 , pp. 601-607
    • Zhao, D.1    Jardetzky, O.2
  • 91
    • 0024351231 scopus 로고
    • Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy
    • GM Clore and AM Gronenborn, Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. Crit. Rev. Biochem. Mol. Biol., 24, 479-564, 1989.
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 479-564
    • Clore, G.M.1    Gronenborn, A.M.2
  • 92
    • 0032177976 scopus 로고    scopus 로고
    • NMR structure determination of proteins and protein complexes larger than 20 kDa
    • GM Clore and AM Gronenborn, NMR structure determination of proteins and protein complexes larger than 20 kDa, Curr. Opinions Chem. Biol., 2, 564-570, 1998.
    • (1998) Curr. Opinions Chem. Biol. , vol.2 , pp. 564-570
    • Clore, G.M.1    Gronenborn, A.M.2
  • 93
    • 0032568556 scopus 로고    scopus 로고
    • New methods of structure refinement for macromo-lecular structure determination by NMR
    • GM Clore and AM Gronenborn, New methods of structure refinement for macromo-lecular structure determination by NMR, Proc. Natl. Acad. Sci. U.S., 95, 5891-5898,1998.
    • (1998) Proc. Natl. Acad. Sci. U.S. , vol.95 , pp. 5891-5898
    • Clore, G.M.1    Gronenborn, A.M.2
  • 94
    • 0031714689 scopus 로고    scopus 로고
    • Structure calculation of biological macromolecules from NMR data
    • P Guntert, Structure calculation of biological macromolecules from NMR data, Q. Rev. Biophys, 31, 145-237, 1998.
    • (1998) Q. Rev. Biophys , vol.31 , pp. 145-237
    • Guntert, P.1
  • 95
    • 0027445544 scopus 로고
    • Conformational analysis of protein structures derived from NMR data
    • MW MacArthur and JM Thornton, Conformational analysis of protein structures derived from NMR data, Proteins Struct. Funct. Genet., 17, 232-251, 1993.
    • (1993) Proteins Struct. Funct. Genet. , vol.17 , pp. 232-251
    • Macarthur, M.W.1    Thornton, J.M.2
  • 96
    • 0032493714 scopus 로고    scopus 로고
    • Quality assessment of NMR structures: A statistical survey
    • JF Doreleijers, JAC Rullman, and R Kaptein, Quality assessment of NMR structures: a statistical survey, J. Mol. Biol., 281, 149-164, 1998.
    • (1998) J. Mol. Biol. , vol.281 , pp. 149-164
    • Doreleijers, J.F.1    Rullman, J.A.C.2    Kaptein, R.3
  • 98
    • 0033027208 scopus 로고    scopus 로고
    • Completeness of NOEs in protein structure: A statistical analysis of NMR
    • JF Doreleijers, ML Raves, T Rullmann, and R Kaptein, Completeness of NOEs in protein structure: a statistical analysis of NMR, J. Biomol. NMR, 14, 123-132, 1999.
    • (1999) J. Biomol. NMR , vol.14 , pp. 123-132
    • Ml Raves, J.F.D.1    Rullmann, T.2    Kaptein, R.3
  • 100
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • G Cornilescu, J Marquardt, M Ottiger, and A Bax, Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase, J. Am. Chem. Soc., 120, 6836-6837, 1998.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.2    Ottiger, M.3    Bax, A.4
  • 101
    • 0032174883 scopus 로고    scopus 로고
    • Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules
    • M Ottiger and A Bax, Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules, J. Biomol. NMR, 12, 361-372, 1998.
    • (1998) J. Biomol. NMR , vol.12 , pp. 361-372
    • Ottiger, M.1    Bax, A.2
  • 102
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures
    • DS Garrett and GM Clore, R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures, J. Am. Chem. Soc., 121, 9008-9012, 1999.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Garrett, D.S.1    Clore, G.M.2
  • 103
    • 0032939805 scopus 로고    scopus 로고
    • The use of dipolar couplings for determining the solution structure of rat apo-S100B(bb)
    • AC Drohat, N Tjandra, DM Baldisseri, and DJ Weber, The use of dipolar couplings for determining the solution structure of rat apo-S100B(bb), Protein Sci., 8, 800-809,1999.
    • (1999) Protein Sci , vol.8 , pp. 800-809
    • Ac Drohat, N.T.1    Baldisseri, D.M.2    Weber, D.J.3
  • 104
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • AC Wallace, RA Laskowski, and JM Thornton, LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Prot. Eng., 8, 127-134, 1995.
    • (1995) Prot. Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 106
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • G Vriend, WHAT IF: a molecular modeling and drug design program, J. Mol. Graph., 8, 52-56, 1990.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 107
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N Guex and MC Peitsch, SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Electrophoresis, 18, 2714-2723, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 108
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • AA Vaguine, J Richelle, and SJ Wodak, SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model, Acta Crystallogr., D55, 191-205, 1999.
    • (1999) Acta Crystallogr., D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 110
    • 0030831667 scopus 로고    scopus 로고
    • Validation of protein models from Ca coordinates alone
    • GJ Kleywegt, Validation of protein models from Ca coordinates alone, J. Mol. Biol., 273, 371-376, 1997.
    • (1997) J. Mol. Biol. , vol.273 , pp. 371-376
    • Kleywegt, G.J.1
  • 111
    • 0032545158 scopus 로고    scopus 로고
    • Stepping through an RNA structure: A novel approach to conformational analysis
    • CM Duarte and AM Pyle, Stepping through an RNA structure: a novel approach to conformational analysis, J. Mol. Biol., 284, 1465-1478, 1998.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1465-1478
    • Duarte, C.M.1    Pyle, A.M.2
  • 112
    • 0029926326 scopus 로고    scopus 로고
    • Valence screening of water in protein crystals reveals potential Na+ binding sites
    • M Nayal and E Di Cera, Valence screening of water in protein crystals reveals potential Na+ binding sites, J. Mol. Biol., 256, 228-234, 1996.
    • (1996) J. Mol. Biol. , vol.256 , pp. 228-234
    • Nayal, M.1    Di Cera, E.2
  • 113
    • 0032820136 scopus 로고    scopus 로고
    • A method to detect nonproline cis peptide bonds in proteins
    • MS Weiss and R Hilgenfeld, A method to detect nonproline cis peptide bonds in proteins, Biopolymers, 50, 536-544, 1999.
    • (1999) Biopolymers , vol.50 , pp. 536-544
    • Weiss, M.S.1    Hilgenfeld, R.2
  • 115
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • C Colovos and TO Yeates, Verification of protein structures: patterns of nonbonded atomic interactions, Prot. Sci., 2, 1511-1519, 1993.
    • (1993) Prot. Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 117
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • D Eisenberg, R Luthy, and JU Bowie, VERIFY3D: Assessment of protein models with three-dimensional profiles, Methods Enzymol., 277, 396-404, 1997.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 119
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • F Melo and E Feytmans, Assessing protein structures with a non-local atomic interaction energy, J. Mol. Biol., 277, 1141-1152, 1998.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 120
    • 0036889887 scopus 로고    scopus 로고
    • The evolution of structural databases
    • O Carugo and S Pongor, The evolution of structural databases, Trends Biotechnol., 20, 498-501, 2002.
    • (2002) Trends Biotechnol , vol.20 , pp. 498-501
    • Carugo, O.1    Pongor, S.2
  • 121
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • GJ Kleywegt, T Bergfors, H Senn, P Le Motte, B Gsell, K Shudo, and TA Jones, Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid, Structure, 2, 1241-1258, 1994.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 122
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R Koradi, M Billeter, and K Wuthrich, MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graph., 14, 51-55, 1996.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.