Abstract
It has been commonly recognized that residual dipolar coupling data provide a measure of quality for protein structures. To quantify this observation, a database of 100 single-domain proteins has been compiled where each protein was represented by two independently solved structures. Backbone 1H–15N dipolar couplings were simulated for the target structures and then fitted to the model structures. The fits were characterized by an R-factor which was corrected for the effects of non-uniform distribution of dipolar vectors on a unit sphere. The analyses show that favorable values \(\tilde{R}\) virtually guarantee high accuracy of the model structure (where accuracy is defined as the backbone coordinate rms deviation). On the other hand, unfavorable \(\tilde{R}\) values do not necessarily suggest low accuracy. Based on the simulated data, a simple empirical formula is proposed to estimate the accuracy of protein structures. The method is illustrated with a number of examples, including PDZ2 domain of human phosphatase hPTP1E.
Similar content being viewed by others
References
C. Abeygunawardana D.J. Weber A.G. Gittis D.N. Frick J. Lin A.F. Miller M.J. Bessman A.S. Mildvan (1995) Biochemistry 34 14997–15005 Occurrence Handle10.1021/bi00046a006 Occurrence Handle7578113
C.R. Babu P.F. Flynn A.J. Wand (2001) J. Am. Chem. Soc. 123 2691–2692 Occurrence Handle10.1021/ja005766d Occurrence Handle11456950
A. Bax (2003) Protein Sci. 12 1–16 Occurrence Handle10.1110/ps.0233303 Occurrence Handle12493823
D. Bentrop I. Bertini M.A. Cremonini S. Forsén C. Luchinat A. Malmendal (1997) Biochemistry 36 11605–11618 Occurrence Handle10.1021/bi971022+ Occurrence Handle9305950
H.M. Berman J. Westbrook Z. Feng G. Gilliland T.N. Bhat H. Weissig I.N. Shindyalov P.E. Bourne (2000) Nucleic Acids Res. 28 235–242 Occurrence Handle10.1093/nar/28.1.235 Occurrence Handle10592235
C.A. Bewley (2001) J. Am. Chem. Soc. 123 1014–1015 Occurrence Handle10.1021/ja005714o Occurrence Handle11456652
P.R. Blake J.B. Park Z.H. Zhou D.R. Hare M.W.W. Adams M.F. Summers (1992) Protein Sci. 1 1508–1521 Occurrence Handle1303769
A.M.J.J. Bonvin A.T. Brunger (1995) J. Mol. Biol. 250 80–93 Occurrence Handle10.1006/jmbi.1995.0360 Occurrence Handle7602599
A.M.J.J. Bonvin A.T. Brunger (1996) J. Biomol. NMR 7 72–76 Occurrence Handle10.1007/BF00190458 Occurrence Handle8720833
A.T. Brunger G.M. Clore A.M. Gronenborn R. Saffrich M. Nilges (1993) Science 261 328–331 Occurrence Handle8332897
F.R. Chalaoux S.I. O’Donoghue M. Nilges (1999) Proteins 34 453–463 Occurrence Handle10.1002/(SICI)1097-0134(19990301)34:4<453::AID-PROT5>3.0.CO;2-7 Occurrence Handle10081958
J.J. Chou S.P. Li C.B. Klee A. Bax (2001) Nat. Struct. Biol. 8 990–997 Occurrence Handle10.1038/nsb1101-990 Occurrence Handle11685248
G.M. Clore D.S. Garrett (1999) J. Am. Chem. Soc. 121 9008–9012 Occurrence Handle10.1021/ja991789k
G.M. Clore A.M. Gronenborn (1998) Proc. Natl. Acad. Sci. USA 95 5891–5898 Occurrence Handle10.1073/pnas.95.11.5891 Occurrence Handle9600889
G.M. Clore J. Kuszewski (2003) J. Am. Chem. Soc. 125 1518–1525 Occurrence Handle10.1021/ja028383j Occurrence Handle12568611
G.M. Clore C.D. Schwieters (2004) J. Am. Chem. Soc. 126 2923–2938 Occurrence Handle10.1021/ja0386804 Occurrence Handle14995210
G. Cornilescu J.L. Marquardt M. Ottiger A. Bax (1998) J. Am. Chem. Soc. 120 6836–6837 Occurrence Handle10.1021/ja9812610
U. Dengler A.S. Siddiqui G.J. Barton (2001) Proteins 42 332–344 Occurrence Handle10.1002/1097-0134(20010215)42:3<332::AID-PROT40>3.0.CO;2-S Occurrence Handle11151005
J.F. Doreleijers S. Mading D. Maziuk K. Sojourner L. Yin J. Zhu J.L. Markley E.L. Ulrich (2003) J. Biomol. NMR 26 139–146 Occurrence Handle10.1023/A:1023514106644 Occurrence Handle12766409
J.F. Doreleijers J.A.C. Rullmann R. Kaptein (1998) J. Mol. Biol. 281 149–164 Occurrence Handle10.1006/jmbi.1998.1808 Occurrence Handle9680482
A.C. Drohat N. Tjandra D.M. Baldisseri D.J. Weber (1999) Protein Sci. 8 800–809 Occurrence Handle10211826
J. Fejzo A.M. Krezel W.M. Westler S. Macura J.L. Markley (1991) Biochemistry 30 3807–3811 Occurrence Handle10.1021/bi00230a001 Occurrence Handle1850288
É. Freyssingeas F. Nallet D. Roux (1996) Langmuir 12 6028–6035 Occurrence Handle10.1021/la9605246
D. Fushman R. Ghose D. Cowburn (2000) J. Am. Chem. Soc. 122 10640–10649 Occurrence Handle10.1021/ja001128j
H. Hatanaka M. Oka D. Kohda S. Tate A. Suda N. Tamiya F. Inagaki (1994) J. Mol. Biol. 240 155–166 Occurrence Handle10.1006/jmbi.1994.1429 Occurrence Handle8027999
D.M. Jacobs K. Saxena M. Vogtherr P. Bernado M. Pons K.M. Fiebig (2003) J. Biol. Chem. 278 26174–26182 Occurrence Handle10.1074/jbc.M300796200 Occurrence Handle12686540
W. Kabsch C. Sander (1983) Biopolymers 22 2577–2637 Occurrence Handle10.1002/bip.360221211 Occurrence Handle6667333
G.J. Kleywegt T.A. Jones (2002) Struct. Fold. Des. 10 465–472 Occurrence Handle10.1016/S0969-2126(02)00743-8
R. Koradi M. Billeter K. Wüthrich (1996) J. Mol. Graph. 14 51–55 Occurrence Handle10.1016/0263-7855(96)00009-4 Occurrence Handle8744573
G. Kozlov K. Gehring I. Ekiel (2000) Biochemistry 39 2572–2580 Occurrence Handle10.1021/bi991913c Occurrence Handle10704206
B.B. Kragelund K.V. Andersen J.C. Madsen J. Knudsen F.M. Poulsen (1993) J. Mol. Biol. 230 1260–1277 Occurrence Handle10.1006/jmbi.1993.1240 Occurrence Handle8503960
R.A. Laskowski M.W. Macarthur D.S. Moss J.M. Thornton (1993) J. Appl. Cryst. 26 283–291 Occurrence Handle10.1107/S0021889892009944
Lerche, M.H., Kragelund, B.B., Redfield, C. and Poulsen, F.M. (2004). To be published; PDB deposition 1NTI
K. Lindorff-Larsen R.B. Best M.A. DePristo C.M. Dobson M. Vendruscolo (2005) Nature 433 128–132 Occurrence Handle10.1038/nature03199 Occurrence Handle15650731
J.A. Losonczi M. Andrec M.W.F. Fischer J.H. Prestegard (1999) J. Magn. Reson. 138 334–342 Occurrence Handle10.1006/jmre.1999.1754 Occurrence Handle10341140
M. Louhivuori K. Pääkkönen K. Fredriksson P. Permi J. Lounila A. Annila (2003) J. Am. Chem. Soc. 125 15647–15650 Occurrence Handle10.1021/ja035427v Occurrence Handle14664613
J.Y. Lu C.L. Lin C.G. Tang J.W. Ponder J.L.F. Kao D.P. Cistola E. Li (1999) J. Mol. Biol. 286 1179–1195 Occurrence Handle10.1006/jmbi.1999.2544 Occurrence Handle10047490
M.A. Massiah V. Saraswat H.F. Azurmendi A.S. Mildvan (2003) Biochemistry 42 10140–10154 Occurrence Handle10.1021/bi030105p Occurrence Handle12939141
J. Meiler J.J. Prompers W. Peti C. Griesinger R. Bruschweiler (2001) J. Am. Chem. Soc. 123 6098–6107 Occurrence Handle10.1021/ja010002z Occurrence Handle11414844
A. Mittermaier L.E. Kay (2001) J. Am. Chem. Soc. 123 6892–6903 Occurrence Handle10.1021/ja010595d Occurrence Handle11448195
R. Mohana-Borges N.K. Goto G.J.A. Kroon H.J. Dyson P.E. Wright (2004) J. Mol. Biol. 340 1131–1142 Occurrence Handle10.1016/j.jmb.2004.05.022 Occurrence Handle15236972
M. Ottiger A. Bax (1998) J. Biomol. NMR 12 361–372 Occurrence Handle10.1023/A:1008366116644 Occurrence Handle9835045
M. Ottiger A. Bax (1999) J. Biomol. NMR 13 187–191 Occurrence Handle10.1023/A:1008395916985 Occurrence Handle10070759
M. Ottiger F. Delaglio J.L. Marquardt N. Tjandra A. Bax (1998) J. Magn. Reson. 134 365–369 Occurrence Handle10.1006/jmre.1998.1546 Occurrence Handle9761712
K. Pääkkönen T. Sorsa T. Drakenberg P. Pollesello C. Tilgmann P. Permi S. Heikkinen I. Kilpeläinen A. Annila (2000) Eur. J. Biochem. 267 6665–6672 Occurrence Handle10.1046/j.1432-1327.2000.01763.x Occurrence Handle11054120
M. Rückert G. Otting (2000) J. Am. Chem. Soc. 122 7793–7797 Occurrence Handle10.1021/ja001068h
H. Schwalbe S.B. Grimshaw A. Spencer M. Buck J. Boyd C.M. Dobson C. Redfield L.J. Smith (2001) Protein Sci. 10 677–688 Occurrence Handle10.1110/ps.43301 Occurrence Handle11274458
A.S. Siddiqui G.J. Barton (1995) Protein Sci. 4 872–884 Occurrence Handle7663343
N.R. Skrynnikov N.K. Goto D.W. Yang W.Y. Choy J.R. Tolman G.A. Mueller L.E. Kay (2000) J. Mol. Biol. 295 1265–1273 Occurrence Handle10.1006/jmbi.1999.3430 Occurrence Handle10653702
L.J. Smith M.J. Sutcliffe C. Redfield C.M. Dobson (1993) J. Mol. Biol. 229 930–944 Occurrence Handle10.1006/jmbi.1993.1097 Occurrence Handle8445657
F.D. Sonnichsen C.I. DeLuca P.L. Davies B.D. Sykes (1996) Struct. Fold. Des. 4 1325–1337 Occurrence Handle10.1016/S0969-2126(96)00140-2
C.A.E.M. Spronk J.P. Linge C.W. Hilbers G.W. Vuister (2002) J. Biomol. NMR 22 281–289 Occurrence Handle10.1023/A:1014971029663 Occurrence Handle11991356
C.A.E.M. Spronk S.B. Nabuurs A.M.J.J. Bonvin E. Krieger G.W. Vuister G. Vriend (2003) J. Biomol. NMR 25 225–234
F. Tian H. Valafar J.H. Prestegard (2001) J. Am. Chem. Soc. 123 11791–11796 Occurrence Handle10.1021/ja011806h Occurrence Handle11716736
N. Tjandra A. Bax (1997) Science 278 1111–1114 Occurrence Handle10.1126/science.278.5340.1111 Occurrence Handle9353189
V. Tugarinov L.E. Kay (2003) J. Mol. Biol. 327 1121–1133 Occurrence Handle10.1016/S0022-2836(03)00238-9 Occurrence Handle12662935
T.S. Ulmer B.E. Ramirez F. Delaglio A. Bax (2003) J. Am. Chem. Soc. 125 9179–9191 Occurrence Handle10.1021/ja0350684 Occurrence Handle15369375
G. Vriend (1990) J. Mol. Graph. 8 52–56 Occurrence Handle10.1016/0263-7855(90)80070-V Occurrence Handle2268628
L.C. Wang Y.X. Pang T. Holder J.R. Brender A.V. Kurochkin E.R.P. Zuiderweg (2001) Proc. Natl. Acad. Sci. USA 98 7684–7689 Occurrence Handle10.1073/pnas.121069998 Occurrence Handle11438724
J. Weigelt S.E. Brown C.S. Miles N.E. Dixon G. Otting (1999) Struct. Fold. Des. 7 681–690 Occurrence Handle10.1016/S0969-2126(99)80089-6
M.P. Williamson J. Kikuchi T. Asakura (1995) J. Mol. Biol. 247 541–546 Occurrence Handle10.1006/jmbi.1995.0160 Occurrence Handle7723012
D.Q. Zhao O. Jardetzky (1994) J. Mol. Biol. 239 601–607
M. Zweckstetter A. Bax (2000) J. Am. Chem. Soc. 122 3791–3792 Occurrence Handle10.1021/ja0000908
M. Zweckstetter A. Bax (2002) J. Biomol. NMR 23 127–137 Occurrence Handle10.1023/A:1016316415261 Occurrence Handle12153038
M. Zweckstetter G. Hummer A. Bax (2004) Biophys. J. 86 3444–3460 Occurrence Handle10.1529/biophysj.103.035790 Occurrence Handle15189846
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
Rights and permissions
About this article
Cite this article
Simon, K., Xu, J., Kim, C. et al. Estimating the Accuracy of Protein Structures using Residual Dipolar Couplings. J Biomol NMR 33, 83–93 (2005). https://doi.org/10.1007/s10858-005-2601-7
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/s10858-005-2601-7