#200 - 2016年8月 正二十面体型ウイルスの準対称性 (Quasisymmetry in Icosahedral Viruses) 類似性 (4)
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集合体
登録構造単位
A: Major capsid protein B: Major capsid protein C: Major capsid protein D: Major capsid protein E: Major capsid protein F: Major capsid protein G: Major capsid protein
A: Major capsid protein B: Major capsid protein C: Major capsid protein D: Major capsid protein E: Major capsid protein F: Major capsid protein G: Major capsid protein
A: Major capsid protein B: Major capsid protein C: Major capsid protein D: Major capsid protein E: Major capsid protein F: Major capsid protein G: Major capsid protein
x 5
icosahedral pentamer
1.04 MDa, 35 ポリマー
分子量 (理論値)
分子数
合計 (水以外)
1,040,843
35
ポリマ-
1,040,843
35
非ポリマー
0
0
水
0
タイプ
名称
対称操作
数
identity operation
1_555
x,y,z
1
point symmetry operation
4
4
A: Major capsid protein B: Major capsid protein C: Major capsid protein D: Major capsid protein E: Major capsid protein F: Major capsid protein G: Major capsid protein
x 6
icosahedral 23 hexamer
1.25 MDa, 42 ポリマー
分子量 (理論値)
分子数
合計 (水以外)
1,249,011
42
ポリマ-
1,249,011
42
非ポリマー
0
0
水
0
タイプ
名称
対称操作
数
identity operation
1_555
x,y,z
1
point symmetry operation
5
5
登録構造と同一
icosahedral asymmetric unit, std point frame
タイプ
名称
対称操作
数
identity operation
1_555
x,y,z
1
6
A: Major capsid protein B: Major capsid protein C: Major capsid protein D: Major capsid protein E: Major capsid protein F: Major capsid protein G: Major capsid protein
THE FIRST 103 RESIDUES ARE CLEAVED. THE SEQUENCE OF PROHEAD II BEGINS AT RESIDUE 104. THERE IS ...THE FIRST 103 RESIDUES ARE CLEAVED. THE SEQUENCE OF PROHEAD II BEGINS AT RESIDUE 104. THERE IS DYNAMICS IN THE N-TERMINUS REGION THEREFORE SOME N-TERMINAL RESIDUES COULD NOT BE MODELED IN THE CRYSTAL STRUCTURE. THE CONSTRUCT WAS ALSO TRUNCATED BETWEEN RESIDUE 159-171 AND REPLACED BY THE LINKER APGD.
解像度: 3.65→3.74 Å / 冗長度: 1.1 % / Rmerge(I) obs: 0.431 / Mean I/σ(I) obs: 1.4 / Num. unique all: 11086 / Rsym value: 0.431 / % possible all: 14.8
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位相決定
位相決定
手法: 分子置換
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解析
ソフトウェア
名称
バージョン
分類
NB
SCALA
データスケーリング
CNS
精密化
PDB_EXTRACT
3.006
データ抽出
DENZO
データ削減
SCALEPACK
データスケーリング
RAVE
位相決定
精密化
構造決定の手法: 分子置換 開始モデル: Prohead II 12A Cryo-EM model and PII 5.2A crystal structure 解像度: 3.65→35 Å / Occupancy max: 1 / Occupancy min: 1 / σ(I): 0 詳細: cross validation was not used and R-free was not calculated due to the high NCS symmetry (15-fold).