Freq.	Weight	Association
3	1.000	Secondary structure - Torsion angles
3	1.000	Protein - Torsion angles
3	1.000	Protein - Secondary structure
3	1.000	Protein - Protein structures
3	1.000	Protein - Protein structure
3	1.000	Protein structures - Torsion angles
3	1.000	Protein structures - Secondary structure
3	1.000	Protein structure - Torsion angles
3	1.000	Protein structure - Secondary structure
3	1.000	Protein structure - Protein structures
4	1.000	Biol - Residue
3	0.866	Residue - Torsion angles
3	0.866	Residue - Secondary structure
3	0.866	Protein - Residue
3	0.866	Protein structures - Residue
3	0.866	Protein structure - Residue
3	0.866	Biol - Torsion angles
3	0.866	Biol - Secondary structure
3	0.866	Biol - Protein
3	0.866	Biol - Protein structures
3	0.866	Biol - Protein structure
2	0.816	Resolution range - Torsion angles
2	0.816	Resolution range - Secondary structure
2	0.816	Protein - Resolution range
2	0.816	Protein structures - Resolution range
2	0.816	Protein structure - Resolution range
2	0.707	Residue - Resolution range

Documents par ordre de pertinence

000124 (1994)	T. J. Oldfield [Royaume-Uni] ; R. E. Hubbard [Royaume-Uni]	Analysis of Cα geometry in protein structures
000133 (1992)	Anne Louise Morris [Royaume-Uni] ; Malcolm W. Macarthur [Royaume-Uni] ; E. Gail Hutchinson [Royaume-Uni] ; Janet M. Thornton [Royaume-Uni]	Stereochemical quality of protein structure coordinates
000129 (1993)	Pawel Herzyk [Royaume-Uni] ; Rodrick E. Hubbard [Royaume-Uni]	A reduced representation of proteins for use in restraint satisfaction calculations
000096 (2000)	Jens Kleinjung [France, Royaume-Uni] ; Marie-Christine Petit [France] ; Piotr Orlewski [France] ; Avgi Mamalaki [Grèce] ; Socrates J. Tzartos [Grèce] ; Vassilios Tsikaris [Grèce] ; Maria Sakarellos-Daitsiotis [Grèce] ; Constantinos Sakarellos [Grèce] ; Michel Marraud (chimiste) [France] ; Manh-Thong Cung [France]	The third‐dimensional structure of the complex between an Fv antibody fragment and an analogue of the main immunogenic region of the acetylcholine receptor: A combined two‐dimensional NMR, homology, and molecular modeling approach

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