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Mumenthaler C, Braun W Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry. J Mol Biol 1996, 254:465-480. Ambiguous NOEs are assigned automatically by analysis of systematic restraint violations. The algorithm can also identify restraints attributable to noise peaks.
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(1996)
J Mol Biol
, vol.254
, pp. 465-480
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Mumenthaler, C.1
Braun, W.2
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52
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0027929299
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A computer-based protocol for semiautomated assignments and 3D structure determination of proteins
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Meadows RP, Olejniczak ET, Fesik SW A computer-based protocol for semiautomated assignments and 3D structure determination of proteins. J Biomol NMR 1994, 4:79-96.
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(1994)
J Biomol NMR
, vol.4
, pp. 79-96
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Meadows, R.P.1
Olejniczak, E.T.2
Fesik, S.W.3
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53
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0000194538
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The program ASNO for computer supported collection of NOE upper distance constraints as input for protein structure determination
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Güntert P, Berndt KD, Wüthrich K The program ASNO for computer supported collection of NOE upper distance constraints as input for protein structure determination. J Biomol NMR 1993, 3:601-606.
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(1993)
J Biomol NMR
, vol.3
, pp. 601-606
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Güntert, P.1
Berndt, K.D.2
Wüthrich, K.3
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54
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0025894164
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Relaxation matrix refinement of the solution structure of squash trypsin inhibitor
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Nilges M, Habazettl J, Brünger AT, Holak TA Relaxation matrix refinement of the solution structure of squash trypsin inhibitor. JMo/B/o/1991, 219:499-510.
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(1991)
JMo/B/o
, vol.219
, pp. 499-510
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Nilges, M.1
Habazettl, J.2
Brünger, A.T.3
Holak, T.A.4
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55
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0027383637
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A calculation strategy for the structure determination of symmetric dimers by 1H NMR
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Nilges M A calculation strategy for the structure determination of symmetric dimers by 1H NMR. Proteins 1993, 17:297-309.
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(1993)
Proteins
, vol.17
, pp. 297-309
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Nilges, M.1
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56
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0001441922
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Calculation of symmetric multimer structures from NMR data using a priori knowledge of the monomer structure, co-monomer restraints, and interface mapping: The case of leucine zippers
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in press
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O'Donoghue SI, King GF, Nilges M Calculation of symmetric multimer structures from NMR data using a priori knowledge of the monomer structure, co-monomer restraints, and interface mapping: the case of leucine zippers. J Biomol NMR 1996. in press. New calculation protocols are developed for the case of leucine zippers to incorporate ambiguous data. The protocol yields significant improvement in convergence rate.
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(1996)
J Biomol NMR
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O'Donoghue, S.I.1
King, G.F.2
Nilges, M.3
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57
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0029058994
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Structure of . the dsRNA binding domain of E. coli RNase III
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Kharrat A, Macias MJ, Gibson T, Nilges M, Pastore A Structure of . the dsRNA binding domain of E. coli RNase III. EMBO J 1995, 14:3572-3584. The structure is derived from the data using an iterative NOE assignment scheme with ambiguous distance restraints. The initially unambiguously assigned NOEs are insufficient to determine the fold of the domain.
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(1995)
EMBO J
, vol.14
, pp. 3572-3584
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Kharrat, A.1
Macias, M.J.2
Gibson, T.3
Nilges, M.4
Pastore, A.5
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58
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0001077775
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A general Bayesian method for an automated signal class recognition in 2D NMR spectra combined with a multivariate discriminant analysis
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Antz C, Neidig KP, Kalbitzer HR A general Bayesian method for an automated signal class recognition in 2D NMR spectra combined with a multivariate discriminant analysis. J Biomol WMR1995, 5:287-296. Statistical methods are used to distinguish spectral artefacts, noise, and solvent peaks from useful experimental information.
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(1995)
J Biomol WMR
, vol.5
, pp. 287-296
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Antz, C.1
Neidig, K.P.2
Kalbitzer, H.R.3
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59
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0029988528
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Three dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
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Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A Three dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell 1996, 85:237-246.
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(1996)
Cell
, vol.85
, pp. 237-246
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Musco, G.1
Stier, G.2
Joseph, C.3
Castiglione Morelli, M.A.4
Nilges, M.5
Gibson, T.J.6
Pastore, A.7
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60
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0028244489
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Structure of the pleckstrin homology domain from β-spectrin
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Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H Structure of the pleckstrin homology domain from β-spectrin. Nature 1994, 369:675-677.
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(1994)
Nature
, vol.369
, pp. 675-677
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Macias, M.J.1
Musacchio, A.2
Ponstingl, H.3
Nilges, M.4
Saraste, M.5
Oschkinat, H.6
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61
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0029096888
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Structure of the binding site for inositol phosphates in a PH domain
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Hyvönen M, Macias MJ, Nilges M, Oschkinat H, Saraste M, Wilmanns M Structure of the binding site for inositol phosphates in a PH domain. EMBO J 1995, 14:4676-4685. The crystal structure is solved from the automatically refined NMR ensemble by molecular replacement. The uncertainty in the structures is used as a pseudo B factor to weight different parts of the molecule in the molecularreplacement program.
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(1995)
EMBO J
, vol.14
, pp. 4676-4685
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Hyvönen, M.1
Macias, M.J.2
Nilges, M.3
Oschkinat, H.4
Saraste, M.5
Wilmanns, M.6
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62
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0028674167
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Automated assignment of multidimensional nuclear magnetic resonance spectra
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Oschkinat H, Croft D Automated assignment of multidimensional nuclear magnetic resonance spectra. Methods Enzymol 1994, 239:308-318.
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(1994)
Methods Enzymol
, vol.239
, pp. 308-318
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Oschkinat, H.1
Croft, D.2
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63
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0028029630
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15N separated NOE data: A novel real space ab initi'o approach
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15N separated NOE data: a novel real space ab initi'o approach. J Mol Biol 1994, 243:696-718.
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(1994)
J Mol Biol
, vol.243
, pp. 696-718
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Kraulis, P.1
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64
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0027918891
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Assessing the quality of solution nuclear magnetic resonance structures by complete cross validation
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Brünger AT, Clore GM, Gronenborn AM, Saffrich R, Nilges M Assessing the quality of solution nuclear magnetic resonance structures by complete cross validation. Science 1993, 261:328-331.
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(1993)
Science
, vol.261
, pp. 328-331
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Brünger, A.T.1
Clore, G.M.2
Gronenborn, A.M.3
Saffrich, R.4
Nilges, M.5
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