Protein backbone angle restraints from searching a database for chemical shift and sequence homology

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961

1H, 13C and 15N chemical shift referencing in biomolecular NMR

Wishart, D. S., Bigam, C. G., Yao, J. S., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,361

The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data

Wishart, D. S., & Sykes, B. D. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,174

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90214-q · Cited by 1,908

Structure of ubiquitin refined at 1.8 A resolution.

Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,635

Tcl and the Tk Toolkit

Ousterhout, J. K. (1994) · Cited by 1,627

Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

Spera, S., & Bax, A. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00014a071 · Cited by 1,101

Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex

Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211764 · Cited by 1,012

A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

Ikura, M., Kay, L. E., & Bax, A. (1990) · Biochemistry · doi:10.1021/bi00471a022 · Cited by 922

Rational Design of Potent, Bioavailable, Nonpeptide Cyclic Ureas as HIV Protease Inhibitors

Lam, P. Y. S., Jadhav, P. K., Eyermann, C. J., Hodge, C. N., Ru, Y., Bacheler, L. T., Meek, J. L., Otto, M. J., Rayner, M. M., Wong, Y. N., et al. (1994) · Science · doi:10.1126/science.8278812 · Cited by 835

Calmodulin structure refined at 1.7 Å resolution

Chattopadhyaya, R., Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90324-d · Cited by 736

Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2

Nilges, M., Gronenborn, A. M., Brünger, A. T., & Clore, G. M. (1988) · Protein Engineering Design and Selection · doi:10.1093/protein/2.1.27 · Cited by 534

Recommendations for the presentation of NMR structures of proteins and nucleic acids – IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy

Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008290618449 · Cited by 467

Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach

de Dios, A. C., Pearson, J. G., & Oldfield, E. (1993) · Science · doi:10.1126/science.8502992 · Cited by 446

Conformation‐dependent 13C chemical shifts: A new means of conformational characterization as obtained by high‐resolution solid‐state 13C NMR

Saitô, H. (1986) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1260241002 · Cited by 390

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer

Weichsel, A., Gasdaska, J. R., Powis, G., & Montfort, W. R. (1996) · Structure · doi:10.1016/s0969-2126(96)00079-2 · Cited by 377

Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis

Concha, N. O., Rasmussen, B. A., Bush, K., & Herzberg, O. (1996) · Structure · doi:10.1016/s0969-2126(96)00089-5 · Cited by 360

A relational database for sequence-specific protein NMR data

Seavey, B. R., Farr, E. A., Westler, W. M., & Markley, J. L. (1991) · Journal of Biomolecular NMR · doi:10.1007/bf01875516 · Cited by 353

Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped Viruses

Clore, G. M., Starich, M. R., & Gronenborn, A. M. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982592f · Cited by 316

Structure of a dehydratase–isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site

Leesong, M., Henderson, B. S., Gillig, J. R., Schwab, J. M., & Smith, J. L. (1996) · Structure · doi:10.1016/s0969-2126(96)00030-5 · Cited by 278

Solution structure of cyanovirin-N, a potent HIV-inactivating protein

Bewley, C. A., Gustafson, K. R., Boyd, M. R., Covell, D. G., Bax, A., Clore, G. M., & Gronenborn, A. M. (1998) · Nature Structural Biology · doi:10.1038/828 · Cited by 266

The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+ and the inhibitor pdTp, refined at 1.65 Å

Loll, P. J., & Lattman, E. E. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340050302 · Cited by 261

Protein conformation and proton nuclear‐magnetic‐resonance chemical shifts

Pardi, A., Wagner, G. H., & Wüthrich, K. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07848.x · Cited by 256

Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: stereochemical analysis

Longhi, S., Czjzek, M., Lamzin, V. S., Nicolas, A., & Cambillau, C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1000 · Cited by 233

The Impact of Direct Refinement against 13Cα and 13Cβ Chemical Shifts on Protein Structure Determination by NMR

Kuszewski, J. J., Qin, J., Gronenborn, A. M., & Clore, G. M. (1995) · Journal of Magnetic Resonance Series B · doi:10.1006/jmrb.1995.1017 · Cited by 208

Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures

Berndt, K. D., Güntert, P., Orbons, L. P. M., & Kurt Wüthrich, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90222-6 · Cited by 201

Structure of form III crystals of bovine pancreatic trypsin inhibitor

Wlodawer, A., Nachman, J., Gilliland, G. L., Gallagher, W. H., & Woodward, C. K. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90294-4 · Cited by 200

Assignment of the side-chain proton and carbon-13 resonances of interleukin-1.beta. using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy

Clore, G. M., Bax, A., Driscoll, P. C., Wingfield, P. T., & Gronenborn, A. M. (1990) · Biochemistry · doi:10.1021/bi00487a027 · Cited by 195

Improvements and Extensions in the Conformational Database Potential for the Refinement of NMR and X-ray Structures of Proteins and Nucleic Acids

Kuszewski, J. J., Gronenborn, A. M., & Clore, G. M. (1997) · Journal of Magnetic Resonance · doi:10.1006/jmre.1997.1116 · Cited by 189

High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium

Bax, A., & Tjandra, N. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018308717741 · Cited by 185

Refined 1.8-.ANG. structure reveals the mode of binding of .beta.-cyclodextrin to the maltodextrin binding protein

Sharff, A., Rodseth, L. E., & Quiocho, F. A. (1993) · Biochemistry · doi:10.1021/bi00091a004 · Cited by 178

Refined structure of α-lytic protease at 1.7 Å resolution analysis of hydrogen bonding and solvent structure

Fujinaga, M., Delbaere, L. T. J., Brayer, G. D., & James, M. N. G. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90296-7 · Cited by 174

The relationship between chemical shift and secondary structure in proteins

Pastore, A., & Saudek, V. (1990) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(90)90375-j · Cited by 171

Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution.

Ke, H., Zydowsky, L. D., Liu, J., & Walsh, C. T. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9483 · Cited by 170

Secondary structure of peptides. 3. Carbon-13 NMR cross polarization/magic angle spinning spectroscopic characterization of solid polypeptides

Kricheldorf, H. R., & Mueller, D. (1983) · Macromolecules · doi:10.1021/ma00238a025 · Cited by 155

Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution

Betzel, C., Klupsch, S., Papendorf, G., Hastrup, S., Branner, S., & Wilson, K. S. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90662-4 · Cited by 153

Solution NMR Studies of a 42 KDa Escherichia C oli Maltose Binding Protein/β-Cyclodextrin Complex: Chemical Shift Assignments and Analysis

Gardner, K. H., Zhang, X., Gehring, K., & Kay, L. E. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982019w · Cited by 150

Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography

Svensson, L. A., Thulin, E., & Forsén, S. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90976-q · Cited by 147

Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix

Ikura, M., Kay, L. E., Krinks, M. H., & Bax, A. (1991) · Biochemistry · doi:10.1021/bi00236a024 · Cited by 142

Secondary‐structure dependent chemical shifts in proteins

Williamson, M. P. (1990) · Biopolymers · doi:10.1002/bip.360291009 · Cited by 141

Analysis of proton chemical shifts in regular secondary structure of proteins

�sapay, K., & Case, D. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175249 · Cited by 127

Statistical Basis for the Use of13CαChemical Shifts in Protein Structure Determination

Luginbühl, P., Szyperski, T., & Wüthrich, K. (1995) · Journal of Magnetic Resonance Series B · doi:10.1006/jmrb.1995.0016 · Cited by 111

Observation of Long-Range 1H−1H Distances in Solution by Dipolar Coupling Interactions

Hansen, M. R., Rance, M., & Pardi, A. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9829665 · Cited by 103

Automated 1H and 13C chemical shift prediction using the BioMagResBank

Wishart, D. S., Watson, M., Boyko, R. F., & Sykes, B. D. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018373822088 · Cited by 94

Conformation-dependent carbon-13 NMR chemical shifts of poly(L-alanine) in the solid state: FPT INDO calculation of N-acetyl-N'-methyl-L-alanine amide as a model compound of poly(L-alanine)

Ando, I., Saitô, H., Tabeta, R., Shoji, A., & Ozaki, T. (1984) · Macromolecules · doi:10.1021/ma00133a036 · Cited by 93

Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.

Worthylake, D. K., Meadow, N. D., Roseman, S., Liao, D.-I., Herzberg, O., & Remington, S. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10382 · Cited by 90

Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N

Wang, A., Grzesiek, S., Tschudin, R. G., Lodi, P. J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00182281 · Cited by 89

Amide chemical shifts in many helices in peptides and proteins are periodic

Kuntz, I. D., Kosen, P. A., & Craig, E. C. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00004a050 · Cited by 88

Ionization Equilibria for Side-Chain Carboxyl Groups in Oxidized and Reduced Human Thioredoxin and in the Complex with Its Target Peptide from the Transcription Factor NFκB

Qin, J., Clore, G. M., & Gronenborn, A. M. (1996) · Biochemistry · doi:10.1021/bi952299h · Cited by 87

The NMR solution conformation of unligated human cyclophilin A 1 1Edited by P. E. Wright

Ottiger, M., Zerbe, O., Güntert, P., & Kurt Wüthrich, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1220 · Cited by 84

X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.

Fedorov, A. A., Magnus, K. A., Graupe, M. H., Lattman, E. E., Pollard, T. D., & Almo, S. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8636 · Cited by 83

Three‐dimensional solution structure of the HIV‐1 protease complexed with DMP323, a novel cyclic urea‐type inhibitor, determined by nuclear magnetic resonance spectroscopy

Yamazaki, T., Hinck, A. P., Wang, Y., Nicholson, L. K., Torchia, D. A., Wingfield, P. T., Stahl, S. J., Kaufman, J. D., Chang, C., Domaille, P. J., et al. (1996) · Protein Science · doi:10.1002/pro.5560050311 · Cited by 81

Functional implications of interleukin‐1β based on the three‐dimensional structure

Veerapandian, B., Gilliland, G. L., Raag, R., Svensson, A. L., Masui, Y., Hirai, Y., & Poulos, T. L. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340120103 · Cited by 79

An empirical correlation between 1JC.alpha.H.alpha. and protein backbone conformation

Vuister, G. W., Delaglio, F., & Bax, A. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00050a066 · Cited by 72

The use of 1JC?H? coupling constants as a probe for protein backbone conformation

Vuister, G. W., Delaglio, F., & Bax, A. (1993) · Journal of Biomolecular NMR · doi:10.1007/bf00242476 · Cited by 71

Identification of N-terminal helix capping boxes by means of 13C chemical shifts

Gronenborn, A. M., & Clore, G. M. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00179351 · Cited by 71

Ab Initio Study of the Effects of Torsion Angles on Carbon-13 Nuclear Magnetic Resonance Chemical Shielding in N-Formyl-L-alanine Amide, N-Formyl-L-valine Amide, and Some Simple Model Compounds: Applications to Protein NMR Spectroscopy

de Dios, A. C., & Oldfield, E. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00091a040 · Cited by 69

Simultaneous Measurement of 1H−15N, 1H−13C‘, and 15N−13C‘ Dipolar Couplings in a Perdeuterated 30 kDa Protein Dissolved in a Dilute Liquid Crystalline Phase

Wang, Y., Marquardt, J. L., Wingfield, P. T., Stahl, S. J., Lee‐Huang, S., Torchia, D. A., & Bax, A. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980862o · Cited by 66

Elucidation of the poly‐ l ‐proline binding site in Acanthamoeba profilin I by NMR spectroscopy

Archer, S. J., Vinson, V. K., Pollard, T. D., & Torchia, D. A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80262-9 · Cited by 61

Proton, nitrogen-15, and carbon-13 NMR signal assignments of IIIGlc a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques

Pelton, J. G., Torchia, D. A., Meadow, N. D., Wong, C. Y., & Roseman, S. (1991) · Biochemistry · doi:10.1021/bi00105a032 · Cited by 59

Enzyme-Substrate Interactions

Kumar, V., & Kannan, K. K. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1491 · Cited by 59

Protein φ and ψ dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structures

Beger, R. D., & Bolton, P. H. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018302105638 · Cited by 55

Protein Structure Refinement Using Carbon-13 Nuclear Magnetic Resonance Spectroscopic Chemical Shifts and Quantum Chemistry

Pearson, J. G., Wang, J., Markley, J. L., Le, H. C., & Oldfield, E. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00139a016 · Cited by 38

Combined use of 13C chemical shift and 1H??13C? heteronuclear NOE data in monitoring a protein NMR structure refinement

Celda, B., Biamonti, C., Arnau, M., Tejero, R., & Montelione, G. T. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00208807 · Cited by 36

1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution

Prompers, J. J., Hilbers, C. W., Groenewegen, A., van Schaik, R. C., & Pepermans, H. A. M. (1997) · Protein Science · doi:10.1002/pro.5560061111 · Cited by 33

Assignment of the natural abundance carbon-13 spectrum of proteins using carbon-13-proton detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants

Hansen, P. E. (1991) · Biochemistry · doi:10.1021/bi00107a014 · Cited by 26

Proton NMR studies of porcine calbindin D9k in solution: sequential resonance assignment, secondary structure, and global fold

Drakenberg, T., Hofmann, T., & Chazin, W. (1989) · Biochemistry · doi:10.1021/bi00440a035 · Cited by 22

Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus

Fogh, R. H., Schipper, D., Boelens, R., & Kaptein, R. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211753 · Cited by 22

ORB, a homology-based program for the prediction of protein NMR chemical shifts

Gronwald, W., Boyko, R. F., Sönnichsen, F. D., Wishart, D. S., & Sykes, B. D. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018389332160 · Cited by 19

Secondary structure of ?-hydroxydecanoyl thiol ester dehydrase, a 39-kDa protein, derived from H?, C?, C? and CO signal assignments and the Chemical Shift Index: Comparison with the crystal structure

Copi�, V., Battles, J., Schwab, J. M., & Torchia, D. A. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00200435 · Cited by 18

Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling

Sethson, I., Edlund, U. G., Holak, T. A., Ross, A., & Jonsson, B. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228144 · Cited by 14

Alterations in chemical shifts and exchange broadening upon peptide boronic acid inhibitor binding to α-lytic protease

Davis, J. H., Agard, D. A., Handel, T. M., & Basus, V. J. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018314808361 · Cited by 10

1H, 13C and 15N NMR backbone assignments of 25.5 kDa metallo-β-lactamase from shape Bacteroides fragilis

Scrofani, S. D. B., Wright, P. E., & Dyson, H. J. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008279832041 · Cited by 5

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Shen, Y., Delaglio, F., Cornilescu, G., & Bax, A. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9333-z · Cited by 2,538

A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR

Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,847

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687

Molecular Interplay of the Noncoding RNA ANRIL and Methylated Histone H3 Lysine 27 by Polycomb CBX7 in Transcriptional Silencing of INK4a

Yap, K. L., Li, S., Muñoz-Cabello, A. M., Raguz, S., Zeng, L., Mujtaba, S., Gil, J., Walsh, M. J., & Zhou, M.-M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.021 · Cited by 1,391

Structure of a bacterial multidrug ABC transporter

Dawson, R. J. P., & Locher, K. P. (2006) · Nature · doi:10.1038/nature05155 · Cited by 1,320

Journal of Biomolecular NMR, 13: 289–302, 1999. KLUWER/ESCOM © 1999 Kluwer Academic Publishers. Printed in the Netherlands.

Cornilescu, G., Delaglio, F., & Bax, A. (1999)

Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology

Shen, Y., & Bax, A. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9166-6 · Cited by 367

ARTICLE TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Bax, A. (2016)

SimShiftDB; local conformational restraints derived from chemical shift similarity searches on a large synthetic database

Ginzinger, S., & Coles, M. P. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9301-7 · Cited by 14

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Shen, Y., Delaglio, F., Cornilescu, G., & Bax, A. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9333-z · Cited by 2,538