Dataset for: A novel chitin binding mode of the chitin binding domain of chitinase A1 from Bacillus circulans WL-12 revealed by solid-state NMR Hiroki Tanaka Hideo Akutsu Izumi Yabuta Masashi Hara Hayuki Sugimoto Takahisa Ikegami Takeshi Watanabe Toshimichi Fujiwara 10.6084/m9.figshare.6974378.v1 https://wiley.figshare.com/articles/dataset/Dataset_for_A_novel_chitin_binding_mode_of_the_chitin_binding_domain_of_chitinase_A1_from_Bacillus_circulans_WL-12_revealed_by_solid-state_NMR/6974378 Chitin-binding domain of chitinase A1 (ChBDChiA1) is characteristic because it binds only to insoluble crystalline chitin. While binding sites of major carbohydrate-binding modules carry multiple aromatic rings aligned on a surface, lethal mutations for ChBDChiA1 were reported only at W687, a location completely different from the site mentioned above, in spite of their similar main chain folds. Here, the structural mechanism underlying its crystalline chitin-binding was uncovered by solid-state NMR. Based on 13C- and 15N-signal assignment of microcrystalline ChBDChiA1, the chemical shift perturbation on chitin-binding was carefully examined. The perturbation was greatest at W687 and non-aromatic residues surrounding it, revealing their direct involvement in chitin-binding. These residues and Q679 should provide a novel chitin-binding platform parallel to the W687 ring. 2018-09-01 09:09:10 insoluble chitin carbohydrate-binding protein NMR Biophysics Synthetic Biology Biochemistry Plant Biology Virology Receptors and Membrane Biology Computational Biology Immunology Neuroscience Cell Development, Proliferation and Death Molecular Biology Evolutionary Biology Signal Transduction Cancer Cell Biology Systems Biology Structural Biology