Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #80 / Phage major coat protein, Gp8 / Bacteriophage M13, G8P, capsid domain superfamily / Capsid protein G8P / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha 類似検索 - ドメイン・相同性
Capsid protein G8P / Capsid protein G8P 類似検索 - 構成要素
Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
Remark 999
Authors informed that the sequence of their protein is identical to residues 27-76 of the database ...Authors informed that the sequence of their protein is identical to residues 27-76 of the database reference sequence provided in GenBank entry 8698956 but that the source of their protein is different. Residue 21 was mutated from Tyr to Met.
Text: This structure was generated from the five-fold symmetry of PDB entry 1IFI, which has the symmetry that relates one pentamer to the next. This one has had the sidechains added using the program ...Text: This structure was generated from the five-fold symmetry of PDB entry 1IFI, which has the symmetry that relates one pentamer to the next. This one has had the sidechains added using the program SCWRL. The structure was determined by solid state nuclear magnetic resonance using the whole virus in suspension. A model of a section of the virion capsid was built with 20 copies of the protein arranged in agreement with previous studies by fiber diffraction (Marvin et al., J. Mol. Biol. 235, 260286 (1994)).
手法: SOLID-STATE NMR SPECTROSCOPY / ソフトェア番号: 1 詳細: The first five N-terminal residues of the coat protein undergo isotropic movements at room temperature and structural parameters cannot be resolved.