Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
Remark 999
SEQUENCE The phage-derived peptide, chain B, is de novo design. No sequence database reference is ...SEQUENCE The phage-derived peptide, chain B, is de novo design. No sequence database reference is available for the peptide.
手法: torsion angle dynamics, simulated annealing / ソフトェア番号: 1 詳細: The complex was determined using a total of 1717 NOE distance restraints (148 intra residue, 339 sequential, 328 medium range, 699 long-range and 203 intermolecular), 36 hydrogen bond ...詳細: The complex was determined using a total of 1717 NOE distance restraints (148 intra residue, 339 sequential, 328 medium range, 699 long-range and 203 intermolecular), 36 hydrogen bond restraints, 156 dihedral angle restraints (86 phi, 44 psi and 26 chi-1) and 82 15N residual dipolar coupling restraints. The best 20 conformers (of 100) had no distance violations greater than 0.12A and no dihedral angle violations greater than 3.0 degrees. RMSD from experimental distance restraints was 0.0055+/-0.0007. The mean backbone rmsd from the mean structure was 0.40+/- 0.05 A for N, Ca and C atoms of residues 10-100. 74% (25%) of residues were in the most favoured (allowed) region of phi/psi space; no residues were in the disallowed region.
代表構造
選択基準: closest to the average
NMRアンサンブル
コンフォーマー選択の基準: least violation of experimental restraints 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 20