메뉴 건너뛰기




Volumn 54, Issue 3, 2012, Pages 267-283

CING: An integrated residue-based structure validation program suite

Author keywords

Errors; NMR; PDB; Protein structure; Quality; Structure validation

Indexed keywords

ARTICLE; COMMON INTERFACE FOR NMR STRUCTURE GENERATION; COMPUTER ANALYSIS; COMPUTER INTERFACE; COMPUTER PROGRAM; CONTROLLED STUDY; EMPIRICAL RESEARCH; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE; VALIDATION PROCESS; WEB BROWSER;

EID: 84868207831     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9669-7     Document Type: Article
Times cited : (99)

References (69)
  • 1
    • 84862970421 scopus 로고    scopus 로고
    • Protein structure validation by generalized linear model rootmean-square deviation prediction
    • doi:10.1002/pro.2007
    • Bagaria A, Jaravine V, Huang YJ, Montelione GT, Güntert P (2012) Protein structure validation by generalized linear model rootmean-square deviation prediction. Protein Sci 21(2):229-238. doi:10.1002/pro.2007
    • (2012) Protein Sci , vol.21 , Issue.2 , pp. 229-238
    • Bagaria, A.1    Jaravine, V.2    Huang, Y.J.3    Montelione, G.T.4    Güntert, P.5
  • 3
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • DOI 10.1016/j.sbi.2005.08.006, PII S0959440X05001545, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Bax A, Grishaev A (2005) Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr Opin Struct Biol 15(5):563-570. doi:10.1016/j.sbi.2005.08.006 (Pubitemid 41393488)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 6
    • 37848999781 scopus 로고    scopus 로고
    • Application of the random coil index to studying protein flexibility
    • doi101007/s10858-007-9208-9210
    • Berjanskii MV, Wishart DS (2008) Application of the random coil index to studying protein flexibility. J Biomol NMR 40(1):31-48. doi:10.1007/s10858-007- 9208-0
    • (2008) J Biomol NMR , vol.40 , Issue.1 , pp. 31-48
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 7
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • DOI 10.1038/nsb1203-980
    • Berman H, Henrick K, Nakamura H (2003) Announcing the worldwide Protein Data Bank. Nat Struct Biol 10(12):980. doi: 10.1038/nsb1203-980 (Pubitemid 37500485)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 8
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • doi101002/rot 21165
    • Bhattacharya A, Tejero R, Montelione GT (2007) Evaluating protein structures determined by structural genomics consortia. Proteins Struct Funct Bioinformatics 66(4):778-795. doi:10.1002/prot. 21165
    • (2007) Proteins Struct Funct Bioinformatics , vol.66 , Issue.4 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 9
    • 84865655100 scopus 로고    scopus 로고
    • NMR structure note: Solution structure of Ca2? binding domain 2B of the third isoform of the Na?/Ca2? exchanger
    • Breukels V, Touw W, Vuister GW (2012) NMR structure note: Solution structure of Ca2? binding domain 2B of the third isoform of the Na?/Ca2? exchanger. J Biomol NMR 54:115-121
    • (2012) J Biomol NMR , vol.54 , pp. 115-121
    • Breukels, V.1    Touw, W.2    Vuister, G.W.3
  • 11
    • 29244438431 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos.
    • DeLano W, Bromberg S (2004) PyMOL user guide. DeLano Scientific, San Carlos. http://pymol.sourceforge.net/newman/ userman.pdf
    • (2004) PyMOL User Guide
    • DeLano, W.1    Bromberg, S.2
  • 12
    • 0034529140 scopus 로고    scopus 로고
    • Disulfide recognition in an optimized threading potential
    • Dombkowski AA, Crippen GM (2000) Disulfide recognition in an optimized threading potential. Protein Eng Des Sel 13(10):679-689. doi:10.1093/protein/13. 10.679 (Pubitemid 32001376)
    • (2000) Protein Engineering , vol.13 , Issue.10 , pp. 679-689
    • Dombkowski, A.A.1    Crippen, G.M.2
  • 13
    • 0032493714 scopus 로고    scopus 로고
    • Quality assessment of NMR structures: A statistical survey
    • DOI 10.1006/jmbi.1998.1808
    • Doreleijers JF, Rullmann J, Kaptein R (1998) Quality assessment of NMR structures: A statistical survey. J Mol Biol 281(1):149-164. doi:10.1006/jmbi.1998.1808 (Pubitemid 28360678)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.1 , pp. 149-164
    • Doreleijers, J.F.1    Rullmann, J.A.C.2    Kaptein, R.3
  • 14
    • 0032707718 scopus 로고    scopus 로고
    • Validation of nuclear magnetic resonance structures of proteins and nucleic acids: Hydrogen geometry and nomenclature
    • DOI 10.1002/(SICI)1097-0134(19991 115)37:3<404::AID-PROT8>3. 0.CO;2-2
    • Doreleijers JF, Vriend G, Raves ML, Kaptein R (1999) Validation of nuclear magnetic resonance structures of proteins and nucleic acids: Hydrogen geometry and nomenclature. Proteins Struct Funct Bioinformatics 37(3):404-416. doi:10.1002/(SICI)1097-0134(19991115)37:3\404:AID-PROT8[3.0.CO;2-2 (Pubitemid 29519730)
    • (1999) Proteins: Structure, Function and Genetics , vol.37 , Issue.3 , pp. 404-416
    • Doreleijers, J.F.1    Vriend, G.2    Raves, M.L.3    Kaptein, R.4
  • 15
    • 23144441604 scopus 로고    scopus 로고
    • BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures
    • DOI 10.1007/s10858-005-2195-0
    • Doreleijers JF, Nederveen AJ, Vranken W, Lin J, Bonvin AMJJ, Kaptein R, Markley JL et al (2005) Bio Mag Res Bank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures. J Biomol NMR 32(1):1-12. doi:10.1007/ s10858-005-2195-0 (Pubitemid 41086462)
    • (2005) Journal of Biomolecular NMR , vol.32 , Issue.1 , pp. 1-12
    • Doreleijers, J.F.1    Nederveen, A.J.2    Vranken, W.3    Lin, J.4    Bonvin, A.M.J.J.5    Kaptein, R.6    Markley, J.L.7    Ulrich, E.L.8
  • 16
    • 71049172008 scopus 로고    scopus 로고
    • The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries
    • doi101007/s10858-389-396 doi101007/s10009
    • Doreleijers JF, Vranken WF, Schulte C, Lin J, Wedell JR, Penkett CJ, Vuister GW et al (2009) The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries. J Biomol NMR 45(4):389-396. doi:10.1007/s10858-009- 9378-z Doreleijers JF, Vranken WF, Schulte C, Markley JL, Ulrich EL, Vriend G, Vuister GW (2011) NRG-CING: Integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB. Nucleic Acids Res. doi:10.1093/nar/ gkr1134
    • (2009) J Biomol NMR , vol.45 , Issue.4 , pp. 389-396
    • Doreleijers, J.F.1    Vranken, W.F.2    Schulte, C.3    Lin, J.4    Wedell, J.R.5    Penkett, C.J.6    Vuister, G.W.7
  • 17
    • 84855878395 scopus 로고    scopus 로고
    • Comprehensive automation for NMR structure determination of proteins
    • doi:101007/978-429-451 doi:101007/971
    • Guerry P, Herrmann T (2012) Comprehensive automation for NMR structure determination of proteins. Methods Mol Biol (Clifton, NJ) 831:429-451. doi:10.1007/978-1-61779-480-3-22
    • (2012) Methods Mol Biol (Clifton, NJ , vol.831 , pp. 429-451
    • Guerry, P.1    Herrmann, T.2
  • 18
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • doi: 101385/1-353-378 doi: 10159259
    • Güntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol (Clifton, NJ) 278:353-378. doi: 10.1385/1-59259-809-9:353
    • (2004) Methods Mol Biol (Clifton, NJ , vol.278 , pp. 353-378
    • Güntert, P.1
  • 19
    • 58849162221 scopus 로고    scopus 로고
    • Automated structure determination from NMR spectra
    • doi:10.1007/s00249-008-0367-z
    • protein PDB structures. J Biomol NMR 32(1):1-12. doi:10.1007/ s10858-005-2195-0Güntert P (2009) Automated structure determination from NMR spectra. Eur Biophys J 38(2):129-143. doi:10.1007/s00249-008-0367-z
    • (2009) Eur Biophys J , vol.38 , Issue.2 , pp. 129-143
    • Güntert, P.1
  • 20
    • 4644223325 scopus 로고    scopus 로고
    • NOE assignment with ARIA 2.0: The nuts and bolts
    • doi:10.1385/1-59259-809-9:379
    • Habeck M, Rieping W, Linge JP, Nilges M (2004) NOE assignment with ARIA 2.0: The nuts and bolts. Methods Mol Biol (Clifton, NJ) 278:379-402. doi:10.1385/1-59259-809-9:379
    • (2004) Methods Mol Biol (Clifton, NJ , vol.278 , pp. 379-402
    • Habeck, M.1    Rieping, W.2    Linge, J.P.3    Nilges, M.4
  • 21
    • 77954298717 scopus 로고    scopus 로고
    • NMR constraints analyser: A webserver for the graphical analysis of NMR experimental constraints
    • (Web Server issue). doi:10.1093/nar/gkq484
    • Heller DM, Giorgetti A (2010) NMR constraints analyser: A webserver for the graphical analysis of NMR experimental constraints. Nucleic Acids Res 38(Web Server issue):W628-W632. doi:10.1093/nar/gkq484
    • (2010) Nucleic Acids Res , vol.38
    • Heller, D.M.1    Giorgetti, A.2
  • 23
    • 33746124556 scopus 로고    scopus 로고
    • Biomolecules in the computer: Jmol to the rescue
    • Herráez A (2006) Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ 34(4):255-261
    • (2006) Biochem Mol Biol Educ , vol.34 , Issue.4 , pp. 255-261
    • Herráez, A.1
  • 24
    • 33646001409 scopus 로고    scopus 로고
    • Ca2? regulation in the Na?/ Ca2? exchanger involves two markedly different Ca2? sensors
    • doi101016/jmolcel2006.03008
    • Hilge M, Aelen JMA, VuisterGW(2006) Ca2? regulation in the Na?/ Ca2? exchanger involves two markedly different Ca2? sensors. Mol Cell 22(1):15-25. doi:10.1016/j.molcel.2006.03.008
    • (2006) Mol Cell , vol.22 , Issue.1 , pp. 15-25
    • Hilge, M.1    Aelen, J.M.A.2    Vuister, G.W.3
  • 25
    • 70149116358 scopus 로고    scopus 로고
    • Ca2? regulation in the Na?/Ca2? exchanger features a dual electrostatic switch mechanism
    • doi101073/nas0902171106
    • Hilge M, Aelen J, Foarce A, Perrakis A, Vuister GW (2009) Ca2? regulation in the Na?/Ca2? exchanger features a dual electrostatic switch mechanism. Proc Natl Acad Sci USA 106(34): 14333-14338. doi:10.1073/pnas.0902171106
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.34 , pp. 14333-14338
    • Hilge, M.1    Aelen, J.2    Foarce, A.3    Perrakis, A.4    Vuister, G.W.5
  • 26
    • 0030461976 scopus 로고    scopus 로고
    • The PDBFINDER database: A summary of PDB, DSSP and HSSP information with added value
    • Hooft RWW, Sander C, Scharf M, Vriend G (1996a) The PDBFINDER database: A summary of PDB, DSSP and HSSP information with added value. Bioinformatics 12(6):525-529. doi:10.1093/bioinformatics/12.6.525 (Pubitemid 27067446)
    • (1996) Computer Applications in the Biosciences , vol.12 , Issue.6 , pp. 525-529
    • Hooft, R.W.W.1    Sander, C.2    Scharf, M.3    Vriend, G.4
  • 27
    • 0030047142 scopus 로고    scopus 로고
    • Errors in protein structures
    • doi:10.1038/381272a0
    • Hooft R, Vriend G, Sander C, Abola E (1996b) Errors in protein structures. Nature 381(6580):272. doi:10.1038/381272a0
    • (1996) Nature , vol.381 , Issue.6580 , pp. 272
    • Hooft, R.1    Vriend, G.2    Sander, C.3    Abola, E.4
  • 28
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • Hooft RWW, Sander C, Vriend G (1997) Objectively judging the quality of a protein structure from a Ramachandran plot. Bioinformatics 13(4):425-430. doi:10.1093/bioinformatics/13. 4.425 (Pubitemid 27384626)
    • (1997) Computer Applications in the Biosciences , vol.13 , Issue.4 , pp. 425-430
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 29
    • 34247493236 scopus 로고    scopus 로고
    • Matplotlib: A 2D graphics environment
    • doi101109/MCSE2007.55
    • Hunter J (2007) Matplotlib: A 2D graphics environment. Comput Sci Eng 9(3):90-95. doi:10.1109/MCSE.2007.55
    • (2007) Comput Sci Eng , vol.9 , Issue.3 , pp. 90-95
    • Hunter, J.1
  • 30
    • 0018115846 scopus 로고
    • Conformation of amino acid side chains in proteins
    • Janin J, Wodak S, Levitt M, Maigret B (1978) Conformation of amino acid side-chains in proteins. J Mol Biol 125(3):357-386. doi: 10.1016/0022-2836(78) 90408-4 (Pubitemid 9063908)
    • (1978) Journal of Molecular Biology , vol.125 , Issue.3 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigret, B.4
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • doi101002/bi 360221211
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22(12):2577-2637. doi:10.1002/bip. 360221211
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 33
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14(1):51-55. doi:10.1016/0263-7855(96)00009-4 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 34
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • DOI 10.1002/1439-7633(200 20703)3:7<604::AID-CB IC604>3.0.CO;2-X
    • Kumar S, Nussinov R (2002) Close-range electrostatic interactions in proteins. Chembiochem: Eur J Chem Biol 3(7):604-617. doi: 10.1002/1439- 7633(20020703)3:7\604:AID-CBIC604[3.0.CO; 2-X (Pubitemid 36004524)
    • (2002) ChemBioChem , vol.3 , Issue.7 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 35
    • 0037263939 scopus 로고    scopus 로고
    • Structural quality assurance
    • doi:10.1002/0471721204.ch14
    • Laskowski R (2003) Structural quality assurance. Methods Biochem Anal 44:273-303. doi:10.1002/0471721204.ch14
    • (2003) Methods Biochem Anal , vol.44 , pp. 273-303
    • Laskowski, R.1
  • 39
    • 0003880237 scopus 로고    scopus 로고
    • 2nd edn. O'Reilly, Sebastopol
    • Lutz M (2001) Programming python, 2nd edn. O'Reilly, Sebastopol
    • (2001) Programming Python
    • Lutz, M.1
  • 40
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids
    • Markley JL, Bax A, Arata Y, Hilbers C, Kaptein R, Sykes B, Wright P et al (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. J Biomol NMR 12(1):1-23
    • (1998) J Biomol NMR , vol.12 , Issue.1 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.4    Kaptein, R.5    Sykes, B.6    Wright, P.7
  • 41
    • 41149116500 scopus 로고    scopus 로고
    • Bio Mag Res Bank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): New policies affecting biomolecular NMR depositions
    • doi101007/s10858-008-9221-y
    • Markley JL, Ulrich EL, Berman HM, Henrick K, Nakamura H, Akutsu H (2008) Bio Mag Res Bank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): New policies affecting biomolecular NMR depositions. J Biomol NMR 40(3):153-155. doi:10.1007/s10858-008-9221-y
    • (2008) J Biomol NMR , vol.40 , Issue.3 , pp. 153-155
    • Markley, J.L.1    Ulrich, E.L.2    Berman, H.M.3    Henrick, K.4    Nakamura, H.5    Akutsu, H.6
  • 42
    • 35648988945 scopus 로고    scopus 로고
    • Benchmarking consensus model quality assessment for protein fold recognition
    • doi101186/1471-2105-8-345
    • McGuffin LJ (2007) Benchmarking consensus model quality assessment for protein fold recognition. BMC Bioinformatics 8:345. doi:10.1186/1471-2105-8-345
    • (2007) BMC Bioinformatics , vol.8 , pp. 345
    • McGuffin, L.J.1
  • 43
    • 79952591087 scopus 로고    scopus 로고
    • Python for scientists and engineers
    • doi:10.1109/MCSE.2011.36
    • Millman KJ, Aivazis M (2011) Python for scientists and engineers. Comput Sci Eng 13(2):9-12. doi:10.1109/MCSE.2011.36
    • (2011) Comput Sci Eng , vol.13 , Issue.2 , pp. 9-12
    • Millman, K.J.1    Aivazis, M.2
  • 44
    • 70349558318 scopus 로고    scopus 로고
    • Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts
    • doi101002/cbic200900086
    • Mulder F (2009) Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts. Chembiochem Eur J Chem Biol 10(9):1477-1479. doi:10.1002/cbic.200900086
    • (2009) Chembiochem Eur J Chem Biol , vol.10 , Issue.9 , pp. 1477-1479
    • Mulder, F.1
  • 48
    • 33645790319 scopus 로고    scopus 로고
    • Traditional biomolecular structure determination by NMR spectroscopy allows for major errors
    • doi: 10.1371/journal.pcbi.0020009
    • Nabuurs SB, Spronk CAEM, Vuister GW, Vriend G (2006) Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. PLoS Comput Biol 2(2):e9. doi: 10.1371/journal.pcbi.0020009
    • (2006) PLoS Comput Biol , vol.2 , Issue.2
    • Nabuurs, S.B.1    Caem, S.2    Vuister, G.W.3    Vriend, G.4
  • 50
    • 45949117843 scopus 로고
    • A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data
    • doi:10.1016/0014-5793(87)81181-X
    • Nilges M, Clore G, Gronenborn A (1987) A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data. FEBS Lett 219(1):11-16. doi:10.1016/0014-5793(87) 81181-X
    • (1987) FEBS Lett , vol.219 , Issue.1 , pp. 11-16
    • Nilges, M.1    Clore, G.2    Gronenborn, A.3
  • 51
    • 33748282179 scopus 로고    scopus 로고
    • Multi-template approach to modeling engineered bisulfide bonds
    • DOI 10.1002/prot.21059
    • Pellequer J-L, Chen S-WW (2006) Multi-template approach to modeling engineered disulfide bonds. Proteins Struct Funct Bioinformatics 65(1):192-202. doi:10.1002/(ISSN)1097-0134 (Pubitemid 44320628)
    • (2006) Proteins: Structure, Function and Genetics , vol.65 , Issue.1 , pp. 192-202
    • Pellequer, J.-L.1    Chen, S.-W.W.2
  • 52
    • 77955794370 scopus 로고    scopus 로고
    • Validation of archived chemical shifts through atomic coordinates
    • doi:10.1002/prot.22756
    • Rieping W, Vranken WF (2010) Validation of archived chemical shifts through atomic coordinates. Proteins Struct Funct Bioinformatics 78(11):2482-2489. doi:10.1002/prot.22756
    • (2010) Proteins Struct Funct Bioinformatics , vol.78 , Issue.11 , pp. 2482-2489
    • Rieping, W.1    Vranken, W.F.2
  • 53
    • 33847283016 scopus 로고    scopus 로고
    • ARIA2: Automated NOE assignment and data integration in NMR structure calculation
    • DOI 10.1093/bioinformatics/btl589
    • Rieping W, Habeck M, Bardiaux B, Bernard A, Malliavin TE, Nilges M (2007) ARIA2: Automated NOE assignment and data integration in NMR structure calculation. Bioinformatics 23(3):381-382. doi:10.1093/bioinformatics/btl589 (Pubitemid 46323164)
    • (2007) Bioinformatics , vol.23 , Issue.3 , pp. 381-382
    • Rieping, W.1    Bardiaux, B.2    Bernard, A.3    Malliavin, T.E.4    Nilges, M.5
  • 54
    • 69549138143 scopus 로고    scopus 로고
    • CASD-NMR: Critical assessment of automated structure determination by NMR
    • doi101038/nmeth0909-625-626 doi101038/nmeth0625
    • Rosato A, Bagaria A, Baker D, Bardiaux B, Cavalli A, Doreleijers JF, Giachetti A et al (2009) CASD-NMR: Critical assessment of automated structure determination by NMR. Nat Methods 6(9):625-626. doi:10.1038/nmeth0909-625
    • (2009) Nat Methods , vol.6 , Issue.9 , pp. 625-626
    • Rosato, A.1    Bagaria, A.2    Baker, D.3    Bardiaux, B.4    Cavalli, A.5    Doreleijers, J.F.6    Giachetti, A.7
  • 55
    • 84863011912 scopus 로고    scopus 로고
    • Blind testing of routine, fully automated determination of protein structures from NMR data
    • doi:10.1016/j.str.2012.01.002
    • Rosato A, Aramini JM, Arrowsmith C, Bagaria A, Baker D, Cavalli A, Doreleijers JF et al (2012) Blind testing of routine, fully automated determination of protein structures from NMR data. Structure 20(2):227-236. doi:10.1016/j.str.2012.01.002
    • (2012) Structure , vol.20 , Issue.2 , pp. 227-236
    • Rosato, A.1    Aramini, J.M.2    Arrowsmith, C.3    Bagaria, A.4    Baker, D.5    Cavalli, A.6    Doreleijers, J.F.7
  • 56
    • 41349112195 scopus 로고    scopus 로고
    • Peirce's criterion for the elimination of suspect experimental data
    • Ross S (2003) Peirce's criterion for the elimination of suspect experimental data. J Eng Technol 20(2):38-41
    • (2003) J Eng Technol , vol.20 , Issue.2 , pp. 38-41
    • Ross, S.1
  • 57
    • 84868207659 scopus 로고    scopus 로고
    • Using Xplor-NIH for NMR molecular structure determination
    • doi101002/chin200644278
    • Schwieters CD, Kuszewski JJ, Clore GM (2006) Using Xplor-NIH for NMR molecular structure determination. ChemInform 37(44):47-62. doi:10.1002/chin. 200644278
    • (2006) ChemInform , vol.37 , Issue.44 , pp. 47-62
    • Schwieters, C.D.1    Kuszewski, J.J.2    Clore, G.M.3
  • 58
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
    • doi:10.1007/s10858-009-9395-y
    • Shen Y, Bax A (2009) Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts. J Biomol NMR 46(3):199-204. doi:10.1007/s10858- 009-9395-y
    • (2009) J Biomol NMR , vol.46 , Issue.3 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 60
    • 68349093958 scopus 로고    scopus 로고
    • TALOS?: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • doi: 10.1007/s10858-009-9333-z
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS?: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-223. doi: 10.1007/s10858-009-9333-z
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 61
    • 18844415920 scopus 로고    scopus 로고
    • Clustering algorithms for identifying core atom sets and for assessing the precision of protein structure ensembles
    • DOI 10.1002/prot.20402
    • Snyder D, Montelione G (2005) Clustering algorithms for identifying core atom sets and for assessing the precision of protein structure ensembles. Proteins Struct 59(4):673-686. doi:10.1002/prot. 20402 (Pubitemid 40695844)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.4 , pp. 673-686
    • Snyder, D.A.1    Montelione, G.T.2
  • 62
  • 63
    • 28144455335 scopus 로고    scopus 로고
    • Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex
    • DOI 10.1016/j.jmb.2005.10.017, PII S0022283605012507
    • Song J, Tyler RC, Lee MS, Tyler EM, Markley JL (2005) Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex. J Mol Biol 354(5):1043-1051. doi:10.1016/ j.jmb.2005.10.017 (Pubitemid 41698914)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.5 , pp. 1043-1051
    • Song, J.1    Tyler, R.C.2    Lee, M.S.3    Tyler, E.M.4    Markley, J.L.5
  • 64
    • 0036219167 scopus 로고    scopus 로고
    • Improving the quality of protein structures derived by NMR spectroscopy
    • DOI 10.1023/A:1014971029663
    • Spronk CAEM, Linge JP, Hilbers CW, Vuister GW (2002) Improving the quality of protein structures derived by NMR spectroscopy. J Biomol NMR 22(3):281-289 (Pubitemid 34296110)
    • (2002) Journal of Biomolecular NMR , vol.22 , Issue.3 , pp. 281-289
    • Spronk, C.A.E.M.1    Linge, J.P.2    Hilbers, C.W.3    Vuister, G.W.4
  • 66
    • 77952661254 scopus 로고    scopus 로고
    • Importance Of The C-terminal Loop L137-S141 for the folding and folding stability of staphylococcal nuclease
    • doi:10.1021/bi100118k
    • Wang M, Feng Y, Yao H, Wang J (2010) Importance of the C-terminal loop L137-S141 for the folding and folding stability of staphylococcal nuclease. Biochemistry 49(20):4318-4326. doi:10.1021/bi100118k
    • (2010) Biochemistry , vol.49 , Issue.20 , pp. 4318-4326
    • Wang, M.1    Feng, Y.2    Yao, H.3    Wang, J.4
  • 69
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • DOI 10.1023/A:1022836027055
    • Zhang H, Neal S, Wishart DS (2003) RefDB: A database of uniformly referenced protein chemical shifts. J Biomol NMR 25(3):173-195. doi:10.1023/A:1022836027055 (Pubitemid 36410583)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.3 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.