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基本情報
登録情報 | データベース: PDB / ID: 3gb1 | ||||||
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タイトル | STRUCTURES OF B1 DOMAIN OF STREPTOCOCCAL PROTEIN G | ||||||
![]() | PROTEIN (B1 DOMAIN OF STREPTOCOCCAL PROTEIN G) | ||||||
![]() | IMMUNOGLOBULIN BINDING PROTEIN | ||||||
機能・相同性 | ![]() | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
![]() | Clore, G.M. | ||||||
![]() | ジャーナル: J.Am.Chem.Soc. / 年: 1999 タイトル: Improving the Packing and Accuracy of NMR Structures with a Pseudopotential for the Radius of Gyration 著者: Juszewski, K. / Gronenborn, A.M. / Clore, G.M. #1: ![]() タイトル: Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped Viruses. 著者: Clore, G.M. / Starich, M.R. / Gronenborn, A.M. #2: ![]() タイトル: A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. 著者: Gronenborn, A.M. / Filpula, D.R. / Essig, N.Z. / Achari, A. / Whitlow, M. / Wingfield, P.T. / Clore, G.M. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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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NMR アンサンブル |
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要素
#1: タンパク質 | 分子量: 6201.784 Da / 分子数: 1 / 断片: B1 DOMAIN / 由来タイプ: 組換発現 由来: (組換発現) ![]() 発現宿主: ![]() ![]() |
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-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||
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NMR実験 |
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試料調製
試料状態 | 圧: AMBIENT / 温度: 298.00 K |
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結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker AM600 / 製造業者: Bruker / モデル: AM600 / 磁場強度: 600 MHz |
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解析
NMR software |
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精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: INCORPORATES RADIUS OF GYRATION RESTRAINT AND DIPOLAR COUPLINGS A TOTAL OF 31 SIMULATED ANNEALING STRUCTURES WERE CALCULATED THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE LISTED ...詳細: INCORPORATES RADIUS OF GYRATION RESTRAINT AND DIPOLAR COUPLINGS A TOTAL OF 31 SIMULATED ANNEALING STRUCTURES WERE CALCULATED THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE LISTED FIRST. THIS WAS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. IN THE CASE OF THE RESTRAINED MINIMIZED MEAN STRUCTURE THE QUANTITY PRESENTED IN THE B VALUE FIELD (COLUMNS 61 - 66 OF THE ATOM AND HETATM RECORDS BELOW) REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS. FOR THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES THE NUMBERS IN THE B-FACTOR C NO MEANING ALL THE INTERPROTON DISTANCE, TORSION ANGLE RESTRAINTS 3G AND DIPOLAR COUPLING RESTRAINTS ARE AVAILABLE FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. (RMR3GB1) TERMS IN TARGET FUNCTION USED FOR SIMULATED ANNEALING: NOE (SUM AVERAGING) AND TORSION ANGLE RESTRAINTS 3JHNALPHA COUPLING CONSTANT RESTRAINTS (GARRETT ET AL J. MAGN. RESON. B104, 99-103 (1994). DIPOLAR COUPLING RESTRAINTS USING TWO ALIGNMENT TENSO (IN TMV AND IN BICELLES) TERM FOR THE RADIUS OF GYRATION (KUSZEWSKI J, GRONENB CLORE, GM J AM CHEM SOC 121, 2337-2338 (1999)) TORSION ANGLE DATABASE POTENTIAL (KUSZEWSKI J, GRONEN CLORE GM. PROTEIN SCI 5, 1067-1080 (1996); J. MAGN 125, 171-177 (1997). COVALENT GEOMETRY RESTRAINTS (BONDS, ANGLES, IMPROPER QUARTIC VAN DER WAALS REPULSION TERM (NILGES. M, GRONENBORN, A.M., BRUNGER, A.T., CLORE, G.M. (1988) PROTEIN ENG. 2, 27-38). RESTRAINTS: NOES: 138 SEQUENTIAL, 133 MEDIUM, 279 LONG RANGE IN 185 INTRARESIDUE TORSION ANGLES: 145 3JHNALPHA COUPLINGS: 53 DIPOLAR COUPLINGS: 152 IN TMV AND 148 IN BICELLES (NH, N-C AND HN-C) THE B-FACTOR COLUMN GIVES THE AVERAGE RMS OF THE 31 SIMULATED AN STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS FILENAME=G_TMV_BICE_RGYR_AVE.MIN ============================================================ BONDS,ANGLES,IMPROPERS,CDIH,NOE,COUP 162664E-03,0.47617,0.436105,0,1.84255E-02,0.534352 ============================================================ | ||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: RESTRAINED MINIMIZATION 計算したコンフォーマーの数: 32 / 登録したコンフォーマーの数: 32 |