메뉴 건너뛰기




Volumn 55, Issue 3, 2004, Pages 483-486

DRESS: A Database of REfined Solution NMR Structures

Author keywords

Explicit solvent; Molecular dynamics; Nuclear magnetic resonance (NMR); Protein structures; Structure refinement; Structure validation

Indexed keywords

ARTICLE; CRYSTAL STRUCTURE; DATA BASE; DIAGNOSTIC VALUE; MOLECULAR BIOLOGY; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; QUALITY CONTROL; STATISTICAL SIGNIFICANCE; STRUCTURE ANALYSIS; THEORY; VALIDATION PROCESS;

EID: 2442610955     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20118     Document Type: Article
Times cited : (93)

References (25)
  • 1
    • 0037263939 scopus 로고    scopus 로고
    • Structural quality assurance
    • Laskowski RA. Structural quality assurance. Methods Biochem Anal 2003;44:273-303.
    • (2003) Methods Biochem Anal , vol.44 , pp. 273-303
    • Laskowski, R.A.1
  • 2
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 4
    • 0032493714 scopus 로고    scopus 로고
    • Quality assessment of NMR structures: A statistical survey
    • Doreleijers JF, Rullmann JA, Kaptein R. Quality assessment of NMR structures: a statistical survey. J Mol Biol 1998;281:149-164.
    • (1998) J Mol Biol , vol.281 , pp. 149-164
    • Doreleijers, J.F.1    Rullmann, J.A.2    Kaptein, R.3
  • 5
    • 0036219167 scopus 로고    scopus 로고
    • Improving the quality of protein structures derived by NMR spectroscopy
    • Spronk CA, Linge JP, Hilbers CW, Vuister GW. Improving the quality of protein structures derived by NMR spectroscopy. J Biomol NMR 2002;22:281-289.
    • (2002) J Biomol NMR , vol.22 , pp. 281-289
    • Spronk, C.A.1    Linge, J.P.2    Hilbers, C.W.3    Vuister, G.W.4
  • 6
    • 0032707718 scopus 로고    scopus 로고
    • Validation of nuclear magnetic resonance structures of proteins and nucleic acids: Hydrogen geometry and nomenclature
    • Doreleijers JF, Vriend G, Raves ML, Kaptein R. Validation of nuclear magnetic resonance structures of proteins and nucleic acids: hydrogen geometry and nomenclature. Proteins 1999;37:404-416.
    • (1999) Proteins , vol.37 , pp. 404-416
    • Doreleijers, J.F.1    Vriend, G.2    Raves, M.L.3    Kaptein, R.4
  • 7
    • 0041819710 scopus 로고    scopus 로고
    • Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: A molecular dynamics simulation study
    • Fan H, Mark AE. Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study. Proteins 2003;53:111-120.
    • (2003) Proteins , vol.53 , pp. 111-120
    • Fan, H.1    Mark, A.E.2
  • 8
    • 0031842640 scopus 로고    scopus 로고
    • Energy strain in three-dimensional protein structures
    • Maiorov V, Abagyan R. Energy strain in three-dimensional protein structures. Fold Des 1998;3:259-269.
    • (1998) Fold Des , vol.3 , pp. 259-269
    • Maiorov, V.1    Abagyan, R.2
  • 9
    • 0034788323 scopus 로고    scopus 로고
    • Free-energy calculations highlight differences in accuracy between X-ray and NMR structures and add value to protein structure prediction
    • Lee MR, Kollman PA. Free-energy calculations highlight differences in accuracy between X-ray and NMR structures and add value to protein structure prediction. Structure (Camb) 2001;9:905-916.
    • (2001) Structure (Camb) , vol.9 , pp. 905-916
    • Lee, M.R.1    Kollman, P.A.2
  • 11
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang G, Dunbrack RL, Jr. PISCES: a protein sequence culling server. Bioinformatics 2003;19:1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 12
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex
    • Billeter M, Qian YQ, Otting G, Muller M, Gehring W, Wuthrich K. Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J Mol Biol 1993;234:1084-1093.
    • (1993) J Mol Biol , vol.234 , pp. 1084-1093
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Muller, M.4    Gehring, W.5    Wuthrich, K.6
  • 13
    • 0029128264 scopus 로고
    • Refined solution structure of the Tyr41 → His mutant of the M13 gene V protein. A comparison with the crystal structure
    • Prompers JJ, Folmer RH, Nilges M, Folkers PJ, Konings RN, Hilbers CW. Refined solution structure of the Tyr41 → His mutant of the M13 gene V protein. A comparison with the crystal structure. Eur J Biochem 1995;232:506-514.
    • (1995) Eur J Biochem , vol.232 , pp. 506-514
    • Prompers, J.J.1    Folmer, R.H.2    Nilges, M.3    Folkers, P.J.4    Konings, R.N.5    Hilbers, C.W.6
  • 14
    • 0031241809 scopus 로고    scopus 로고
    • Protein solution structure calculations in solution: Solvated molecular dynamics refinement of calbindin D9k
    • Kordel J, Pearlman DA, Chazin WJ. Protein solution structure calculations in solution: solvated molecular dynamics refinement of calbindin D9k. J Biomol NMR 1997;10:231-243.
    • (1997) J Biomol NMR , vol.10 , pp. 231-243
    • Kordel, J.1    Pearlman, D.A.2    Chazin, W.J.3
  • 15
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • Linge JP, Nilges M. Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation. J Biomol NMR 1999;13:51-59.
    • (1999) J Biomol NMR , vol.13 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 16
    • 0036234027 scopus 로고    scopus 로고
    • Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water
    • Xia B, Tsui V, Case DA, Dyson HJ, Wright PE. Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water. J Biomol NMR 2002;22:317-331.
    • (2002) J Biomol NMR , vol.22 , pp. 317-331
    • Xia, B.1    Tsui, V.2    Case, D.A.3    Dyson, H.J.4    Wright, P.E.5
  • 18
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge JP, Habeck M, Rieping W, Nilges M. ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 2003;19:315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 20
    • 0037986814 scopus 로고    scopus 로고
    • BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank
    • Doreleijers JF, Mading S, Maziuk D, Sojourner K, Yin L, Zhu J, Markley JL, Ulrich EL. BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank. J Biomol NMR 2003;26:139-146.
    • (2003) J Biomol NMR , vol.26 , pp. 139-146
    • Doreleijers, J.F.1    Mading, S.2    Maziuk, D.3    Sojourner, K.4    Yin, L.5    Zhu, J.6    Markley, J.L.7    Ulrich, E.L.8
  • 22
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 1991;47:392-400.
    • (1991) Acta Crystallogr A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 24
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • Hooft RWW, Sander C, Vriend G. Objectively judging the quality of a protein structure from a Ramachandran plot. Comput Appl Biosci 1997;13:425-430.
    • (1997) Comput Appl Biosci , vol.13 , pp. 425-430
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 25
    • 0027542118 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • Vriend G, Sander C. Quality control of protein models: directional atomic contact analysis. J Appl Cryst 1993;26:47-60.
    • (1993) J Appl Cryst , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.