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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 1qae | ||||||
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タイトル | THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER | ||||||
![]() | PROTEIN (EXTRACELLULAR ENDONUCLEASE) | ||||||
![]() | ENDONUCLEASE / NUCLEASE / DNASE / RNASE / SUGAR-NONSPECIFIC NUCLEASE / MAGNESIUM | ||||||
機能・相同性 | ![]() Serratia marcescens nuclease / single-stranded DNA endodeoxyribonuclease activity / RNA endonuclease activity / nucleic acid binding / extracellular region / metal ion binding 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() | ||||||
![]() | Miller, M.D. / Krause, K.L. | ||||||
![]() | ![]() タイトル: The active site of Serratia endonuclease contains a conserved magnesium-water cluster. 著者: Miller, M.D. / Cai, J. / Krause, K.L. #1: ![]() タイトル: Identification of the Serratia Endonuclease Dimer: Structural Basis and Implications for Catalysis 著者: Miller, M.D. / Krause, K.L. #2: ![]() タイトル: 2.1 Angstroms Structure of Serratia Endonuclease Suggests a Mechanism for Binding to Double-Stranded DNA 著者: Miller, M.D. / Tanner, J. / Alpaugh, M. / Benedik, M.J. / Krause, K.L. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 108.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 83.6 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 371.5 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 374.9 KB | 表示 | |
XML形式データ | ![]() | 10.5 KB | 表示 | |
CIF形式データ | ![]() | 16.8 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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非結晶学的対称性 (NCS) | NCSドメイン:
NCS oper: (Code: given Matrix: (-0.999819, -0.018722, -0.003478), ベクター: 詳細 | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 5 .. A 245 B 5 .. B 245 0.131 | |
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要素
#1: タンパク質 | 分子量: 26738.896 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() Plasmid details: PLASMID WHICH ENCODES THE GENE AND CARRIES AN OPERATOR CONSTITUTIVE MUTATION プラスミド: PUC19NUC4OC / 遺伝子 (発現宿主): NUCA / 発現宿主: ![]() #2: 化合物 | #3: 水 | ChemComp-HOH / | 配列の詳細 | REFERENCE DATABASE: GENBANK ENTRY_NAME: SMANUCES | |
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-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.57 Å3/Da / 溶媒含有率: 52 % | ||||||||||||||||||||
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結晶化 | 温度: 277 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 8.2 詳細: CRYSTALLIZATION METHOD: VAPOR DIFFUSION SITTING DROP CRYSTALLIZATION TEMPERATURE: 277 K CRYSTALLIZATION PH: 4.6 CRYSTALS WERE GROWN FROM PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE, AND STORED ...詳細: CRYSTALLIZATION METHOD: VAPOR DIFFUSION SITTING DROP CRYSTALLIZATION TEMPERATURE: 277 K CRYSTALLIZATION PH: 4.6 CRYSTALS WERE GROWN FROM PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE, AND STORED IN A STABILIZATION SOLUTION CONTAINING 20% PEG 3000, 400mM GLYCINE, 40mM TRIS, PH8.2 (293 K), 20% PEG 3000, 10% PEG 400. THIS SOLUTION WAS EXCHANGED THREE TIMES TO MINIMIZE CARRY OVER FROM THE STORAGE SOLUTION. AFTER 3 DAYS IN THE MAGNESIUM STABILIZATION SOLUTION, THE CRYSTAL OF DIMENSION 0.4 X 0.4 X 0.3 MM**2 WAS MOUNTED IN A SILICONIZED SPECIAL GLASS CAPILLARY. , VAPOR DIFFUSION, SITTING DROP | ||||||||||||||||||||
結晶 | *PLUS | ||||||||||||||||||||
結晶化 | *PLUS 温度: 4 ℃ / pH: 4.6 / 手法: other | ||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
回折 | 平均測定温度: 288 K |
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放射光源 | 由来: ![]() |
検出器 | タイプ: ENRAF-NONIUS FAST / 検出器: DIFFRACTOMETER / 日付: 1998年2月2日 |
放射 | モノクロメーター: GRAPHITE / 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: 1.5418 Å / 相対比: 1 |
反射 | 解像度: 2.05→45 Å / Num. obs: 30574 / % possible obs: 84.3 % / Observed criterion σ(I): 0 / 冗長度: 3.1 % / Biso Wilson estimate: 6.6 Å2 / Rmerge(I) obs: 0.025 / Net I/σ(I): 40.87 |
反射 シェル | 解像度: 2.05→2.1 Å / 冗長度: 1.6 % / Rmerge(I) obs: 0.045 / Mean I/σ(I) obs: 18.9 / % possible all: 20.4 |
反射 | *PLUS Num. measured all: 93785 |
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解析
ソフトウェア |
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精密化 | 開始モデル: 1.4 ANGSTROM STRUCTURE OF THE SERRATIAL ENDONUCLEASE (CAI, MILLER AND KRAUSE) WITH WATER AND ALTERNATE SIDE CHAIN CONFORMERS REMOVED AND THE SIDE CHAINS FOR THE ACTIVE SITE RESIDUES ...開始モデル: 1.4 ANGSTROM STRUCTURE OF THE SERRATIAL ENDONUCLEASE (CAI, MILLER AND KRAUSE) WITH WATER AND ALTERNATE SIDE CHAIN CONFORMERS REMOVED AND THE SIDE CHAINS FOR THE ACTIVE SITE RESIDUES ARG 57, HIS 89, ASN 199 AND GLU 127 OMITTED 解像度: 2.05→50 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / 交差検証法: THROUGHOUT / σ(F): 2 詳細: BULK SOLVENT MODEL USED, NCS B-FACTORS RESTRAINTS WERE APPLIED TO PROTEIN ATOMS AND PAIRS OF WATER MOLECULES WHICH DEVIATED LESS THAN 1.0 ANGSTROMS FROM NCS. THE PROTEIN ATOMS ARE IN GROUP 1 ...詳細: BULK SOLVENT MODEL USED, NCS B-FACTORS RESTRAINTS WERE APPLIED TO PROTEIN ATOMS AND PAIRS OF WATER MOLECULES WHICH DEVIATED LESS THAN 1.0 ANGSTROMS FROM NCS. THE PROTEIN ATOMS ARE IN GROUP 1 AND THE WATER IS IN GROUP 2. WATER HOH 1 SITS ON THE NON-CRYSTALLOGRAPHIC 2-FOLD AXIS AND IT IS ITS OWN NCS MATE. THE WATER PAIRS IN GROUP 2 BEGIN WITH (HOH 2,HOH 3) AND END WITH (HOH 188, HOH 189). WATERS HOH 190 TO HOH 241 DO NOT HAVE NCS MATES WITHIN 1.0 ANGSTROMS. CRYST1 THERE IS STRONG PSEUDO-CENTERING ARISING FROM THE NON-CRYSTALLOGRAPHIC SYMMETRY. SHIFTING ONE MONOMER BY ONLY 1.4 ANGSTROMS WITH A 1 DEGREE ROTATION WOULD CHANGE THE SPACE GROUP TO I 2 2 2.
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原子変位パラメータ | Biso mean: 14.8 Å2
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Refine analyze |
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精密化ステップ | サイクル: LAST / 解像度: 2.05→50 Å
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拘束条件 |
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Refine LS restraints NCS |
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LS精密化 シェル | 解像度: 2.05→2.18 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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ソフトウェア | *PLUS 名称: X-PLOR(ONLINE) / バージョン: 3.851 / 分類: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化 | *PLUS Rfactor obs: 0.167 / Rfactor Rfree: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
拘束条件 | *PLUS
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