第X因子 / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins ...第X因子 / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / Intrinsic Pathway of Fibrin Clot Formation / phospholipid binding / Golgi lumen / 凝固・線溶系 / positive regulation of cell migration / external side of plasma membrane / 小胞体 / serine-type endopeptidase activity / calcium ion binding / タンパク質分解 / extracellular space / extracellular region / 細胞膜 類似検索 - 分子機能
Group: Data collection / Experimental preparation / Other / カテゴリ: exptl_crystal_grow / pdbx_database_status Item: _exptl_crystal_grow.method / _pdbx_database_status.status_code_sf
Remark 700
SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
ACTIVATEDFACTORXAHEAVYCHAIN / COAGULATION FACTOR X / STUART FACTOR / STUART-PROWER FACTOR
分子量: 28550.596 Da / 分子数: 1 / 由来タイプ: 天然 詳細: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM HUMAN BLOOD 由来: (天然) HOMO SAPIENS (ヒト) / 参照: UniProt: P00742, 第X因子
#2: タンパク質
FACTORXLIGHTCHAIN / 第X因子 / COAGULATION FACTOR X / STUART FACTOR / STUART-PROWER FACTOR
分子量: 15210.793 Da / 分子数: 1 / Fragment: ACTIVATED DESGLA, RESIDUES 46-179 / 由来タイプ: 天然 詳細: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM HUMAN BLOOD 由来: (天然) HOMO SAPIENS (ヒト) / 参照: UniProt: P00742, 第X因子
SOME RESIDUES IN CHAIN ARE NOT SEEN IN THE ELECTRON DENSITY. SEQUENCE DATABASE RESIDUES 1-45 (THE ...SOME RESIDUES IN CHAIN ARE NOT SEEN IN THE ELECTRON DENSITY. SEQUENCE DATABASE RESIDUES 1-45 (THE GLA DOMAIN) WERE BIOCHEMICALLY REMOVED IN CHAIN B
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 1.81 Å3/Da / 溶媒含有率: 49.3 % / 解説: NONE
結晶化
手法: 蒸気拡散法 / pH: 5.75 詳細: CRYSTALLISATION WAS CARRIED OUT USING VAPOUR DIFFUSION IN 2UL DROPS CONTAINING A 1:1 MIXTURE OF PROTEIN AND WELL SOLUTION. WELL SOLUTION CONTAINED 16-20% PEG 6K, 50 MM MES-NAOH (PH 5.5-6), 5 ...詳細: CRYSTALLISATION WAS CARRIED OUT USING VAPOUR DIFFUSION IN 2UL DROPS CONTAINING A 1:1 MIXTURE OF PROTEIN AND WELL SOLUTION. WELL SOLUTION CONTAINED 16-20% PEG 6K, 50 MM MES-NAOH (PH 5.5-6), 5 MM CACL2 AND 50 MM NACL.
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: 0.961 Å / 相対比: 1
反射
解像度: 1.69→44.54 Å / Num. obs: 35816 / % possible obs: 97.6 % / Observed criterion σ(I): 0 / 冗長度: 5.5 % / Biso Wilson estimate: 20.615 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 14.4
反射 シェル
解像度: 1.69→1.78 Å / 冗長度: 5.4 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 3.4 / % possible all: 100
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解析
ソフトウェア
名称
バージョン
分類
REFMAC
5.5.0109
精密化
MOSFLM
データ削減
SCALA
データスケーリング
精密化
構造決定の手法: その他 開始モデル: NONE 解像度: 1.7→20 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.935 / SU B: 2.119 / SU ML: 0.07 / 交差検証法: THROUGHOUT / ESU R: 0.106 / ESU R Free: 0.107 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD / 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
反射数
%反射
Selection details
Rfree
0.22473
1753
5 %
RANDOM
Rwork
0.1861
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obs
0.18801
33357
100 %
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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: BABINET MODEL WITH MASK