分子量: 8880.119 Da / 分子数: 1 / 断片: IGAMMA SUBDOMAIN, RESIDUES 174 - 247 / 由来タイプ: 天然 / 詳細: MUA OF PHAGE MU TRANSPOSASE / 由来: (天然) Enterobacteria phage Mu (ファージ) / 属: Mu-like viruses / 参照: UniProt: P07636
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実験情報
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実験
実験
手法: 溶液NMR
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試料調製
試料状態
pH: 6.3 / 温度: 303 K
結晶化
*PLUS
手法: other / 詳細: NMR
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NMR測定
NMRスペクトロメーター
タイプ
製造業者
モデル
磁場強度 (MHz)
Spectrometer-ID
Bruker AMX500
Bruker
AMX500
500
1
Bruker AMX600
Bruker
AMX600
600
2
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解析
ソフトウェア
名称
バージョン
分類
X-PLOR
3.1
モデル構築
X-PLOR
3.1
精密化
X-PLOR
3.1
位相決定
NMR software
名称
バージョン
分類
X-PLOR (SEE ABOVE)
ABOVE)
構造決定
X-PLOR (SEE ABOVE)
ABOVE)
精密化
精密化
手法: simulated annealing / ソフトェア番号: 1 詳細: THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS: 264 SEQUENTIAL (|I- J|=1), 282 ...詳細: THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS: 264 SEQUENTIAL (|I- J|=1), 282 MEDIUM RANGE (1 < |I-J| <=5) AND 178 LONG RANGE (|I-J| >5) INTERRESIDUES AND 245 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 40 DISTANCE RESTRAINTS FOR 20 BACKBONE H-BONDS; 108 TORSION ANGLE RESTRAINTS; 47 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 129 (66 CALPHA AND 63 CBETA) 13C SHIFT RESTRAINTS. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI. 5, 1067-1080; KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125, 171-177). THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN ENTRY 2EZH AND 30 STRUCTURES ARE PRESENTED IN ENTRY 2EZI, AND THE EXPERIMENTAL RESTRAINTS IN 2EZHMR. IN THE RESTRAINED REGULARIZED MEAN COORDINATES (2EZH) THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 180 - 240. NOTE THAT THE OCCUPANCY FIELD HAS NO MEANING.