ジャーナル: J.Mol.Biol. / 年: 2001 タイトル: Folded-Back Solution Structure of Monomeric Factor H of Human Complement by Synchrotron X-Ray and Neutron Scattering, Analytical Ultracentrifugation and Constrained Molecular Modelling. 著者: Aslam, M. / Perkins, S.J.
分子量: 137244.484 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: HUMAN PLASMA / 由来: (天然) HOMO SAPIENS (ヒト) / 参照: UniProt: P08603
構成要素の詳細
FACTOR H IS A COFACTOR IN THE INACTIVATION OF C3B BY FACTOR I
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実験情報
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実験
実験
手法: 溶液散乱
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試料調製
結晶化
*PLUS
手法: t / 詳細: theoretical model
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データ収集
Soln scatter
タイプ
ID
Buffer name
Conc. range (mg/ml)
Data reduction software list
検出器タイプ
Max mean cross sectional radii gyration (nm)
Max mean cross sectional radii gyration esd (nm)
Mean guiner radius (nm)
Mean guiner radius esd (nm)
Min mean cross sectional radii gyration (nm)
Min mean cross sectional radii gyration esd (nm)
Num. of time frames
Protein length
Source class
Source type
温度 (K)
Source beamline instrument
Source beamline
x-ray
1
TRIS
0.7 - 14
OTOKO
500-CHANNEL QUADRANT
1.7
0.1
11.1
0.4
4.4
0.2
10
40
Y
SRSBEAMLINE2.1
288
neutron
2
PBSIN99.9% D2O
0.4 - 9.6
DETEC, RNILS, SPOLLY
AREA
1.51
0.06
11.3
0.4
3.9
0.2
37 - 39
N
ILL
D11, D22
neutron
3
PBSIN99.9% D2O
3.7, 6.1
COLLETTE
AREA (TIME-OF-FLIGHT)
11.7
0.5
40
N
ISIS
LOQ
PULSEDNEUTRON
modelling
4
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解析
ソフトウェア
名称: INSIGHT / バージョン: II 98.0 / 分類: 精密化
精密化
詳細: DISCOVER WAS USED FOR ENERGY MINIMISATION
精密化ステップ
サイクル: LAST
タンパク質
核酸
リガンド
溶媒
全体
原子数
1213
0
0
0
1213
Soln scatter model
手法: CONSTRAINED SCATTERING FITTING OF HOMOLOGY MODELS コンフォーマー選択の基準: THE MODELLED SCATTERING CURVES WERE ASSESSED BY CALCULATION OF THE RG, RSX-1 AND RXS-2 VALUES IN THE SAME Q RANGES USED IN THE EXPERIMENTAL GUINIER FITS. MODELS ...コンフォーマー選択の基準: THE MODELLED SCATTERING CURVES WERE ASSESSED BY CALCULATION OF THE RG, RSX-1 AND RXS-2 VALUES IN THE SAME Q RANGES USED IN THE EXPERIMENTAL GUINIER FITS. MODELS WERE THEN RANKED USING A GOODNESS-OF-FIT R-FACTOR DEFINED BY ANALOGY WITH PROTEIN CRYSTALLOGRAPHY AND BASED ON THE EXPERIMENTAL CURVES IN THE Q RANGE EXTENDING TO 1.4 NM-1. 詳細: HOMOLOGY MODELS WERE BUILT FOR THE 17 SCR DOMAINS AND ENERGY MINIMISATIONS WERE PERFORMED TO IMPROVE THE CONNECTIVITY IN THE FH MODEL. TRIANTENNARY COMPLEX-TYPE CARBOHYDRATE STRUCTURES ...詳細: HOMOLOGY MODELS WERE BUILT FOR THE 17 SCR DOMAINS AND ENERGY MINIMISATIONS WERE PERFORMED TO IMPROVE THE CONNECTIVITY IN THE FH MODEL. TRIANTENNARY COMPLEX-TYPE CARBOHYDRATE STRUCTURES (MAN3GLCNAC6GAL3FUC3NEUNAC1) WERE ADDED TO EACH OF THE N-LINKED GLYCOSYLATION SITES. A LIBRARY OF LINKER PEPTIDE CONFORMATIONS WAS USED IN DOMAIN MODELLING CONSTRAINED BY THE SOLUTION SCATTERING FITS. MODELLING WITH THE SCATTERING DATA WAS ALSO CARRIED OUT BY ROTATIONAL SEARCH METHODS. THE X-RAY AND NEUTRON SCATTERING CURVE I(Q) WAS CALCULATED ASSUMING A UNIFORM SCATTERING DENSITY FOR THE SPHERES USING THE DEBYE EQUATION AS ADAPTED TO SPHERES. X-RAY CURVES WERE CALCULATED FROM THE HYDRATED SPHERE MODELS WITHOUT CORRECTIONS FOR WAVELENGTH SPREAD OR BEAM DIVERGENCE, WHILE THESE CORRECTIONS WERE APPLIED FOR THE NEUTRON CURVES BUT NOW USING UNHYDRATED MODELS. Entry fitting list: PDB CODE 1HFI, 1HCC, 1HFH, 1VCC / Num. of conformers calculated: 2010 / Num. of conformers submitted: 4 / 代表コンフォーマー: 1 / Software author list: MSI Software list: INSIGHT II, HOMOLOGY, DISCOVERY, BIOPOLYMER, DELPHI, SCTPL5, GNOM