SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
THE FIRST 41 AMINO ACIDS ARE NOT PRESENT IN THE EXPRESSED, SECRETED PROTEIN, AND MAY CONTAIN A ...THE FIRST 41 AMINO ACIDS ARE NOT PRESENT IN THE EXPRESSED, SECRETED PROTEIN, AND MAY CONTAIN A POSSIBLE N-TERMINAL SIGNAL PEPTIDE SEQUENCE
解像度: 1.85→97.85 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.953 / SU B: 2.525 / SU ML: 0.075 / 交差検証法: THROUGHOUT / ESU R: 0.102 / ESU R Free: 0.106 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. RESIDUES 299-308 IN MOLECULE B HAVE BEEN MODELLED WITH 2 CONFORMATIONS. THERE IS UNMODELLED DENSITY NEAR THE ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. RESIDUES 299-308 IN MOLECULE B HAVE BEEN MODELLED WITH 2 CONFORMATIONS. THERE IS UNMODELLED DENSITY NEAR THE SIDE CHAINS OF TRP 349 AND TRP 396.
Rfactor
反射数
%反射
Selection details
Rfree
0.20231
6067
5 %
RANDOM
Rwork
0.16263
-
-
-
obs
0.16465
114637
99.83 %
-
溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: MASK