DE NOVO PROTEIN / COILED-COIL / D-PEPTIDE INHIBITOR
機能・相同性
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
BIOMOLECULE: 1, 2 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON BURIED SURFACE AREA. COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. BIOMOLECULE: 1 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC SOFTWARE USED: PISA TOTAL BURIED SURFACE AREA: 12270 ANGSTROM**2 SURFACE AREA OF THE COMPLEX: 10770 ANGSTROM**2 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL APPLY THE FOLLOWING TO CHAINS: A, H BIOMT1 1 1.000000 0.000000 0.000000 0.00000 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 BIOMT1 2 -0.500000 -0.866025 0.000000 20.55850 BIOMT2 2 0.866025 -0.500000 0.000000 -35.60837 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 BIOMT1 3 -0.500000 0.866025 0.000000 41.11700 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 BIOMOLECULE: 2 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC SOFTWARE USED: PISA TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2 SURFACE AREA OF THE COMPLEX: 6110 ANGSTROM**2 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL APPLY THE FOLLOWING TO CHAINS: A, H BIOMT1 1 1.000000 0.000000 0.000000 0.00000 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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要素
#1: タンパク質・ペプチド
GP41N-PEPTIDE
分子量: 5466.574 Da / 分子数: 1 / 由来タイプ: 合成 詳細: L-PEPTIDE WITH N-TERMINAL ACETYL GROUP AND C-TERMINAL AMIDE GROUP
#2: タンパク質・ペプチド
HIVENTRYINHIBITORPIE12
分子量: 1972.249 Da / 分子数: 1 / 由来タイプ: 合成 詳細: D-PEPTIDE WITH N-TERMINAL ACETYL GROUP AND C-TERMINAL AMIDE GROUP
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.97945 Å / 相対比: 1
反射
解像度: 1.45→30 Å / Num. obs: 14802 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / 冗長度: 12.6 % / Rmerge(I) obs: 0.107 / Net I/σ(I): 22.644
反射 シェル
解像度: 1.45→1.5 Å / 冗長度: 6.6 % / Rmerge(I) obs: 0.235 / % possible all: 96.6
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解析
ソフトウェア
名称
バージョン
分類
PHASER
位相決定
REFMAC
5.5.0062
精密化
HKL-2000
データ削減
HKL-2000
データスケーリング
精密化
構造決定の手法: 分子置換 / 解像度: 1.45→21.64 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.92 / SU B: 1.122 / SU ML: 0.045 / 交差検証法: THROUGHOUT / ESU R: 0.083 / ESU R Free: 0.086 / 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
Rfactor
反射数
%反射
Selection details
Rfree
0.278
1136
7.7 %
RANDOM
Rwork
0.243
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obs
0.246
13620
99.6 %
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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: 1.4 Å / 溶媒モデル: MASK