NO DISTANCE VIOLATIONS WERE GREATER THAN 0.3 A, NO ANGLE VIOLATIONS WERE GREATER THAN 5.0 DEGREES, AND NO RDC VIOLATIONS WERE GREATER THAN 2.5 HZ
代表モデル
モデル #1
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要素
#1: タンパク質
ALPHA-HEMOGLOBINSTABILIZINGPROTEIN / ERYTHROID ASSOCIATED FACTOR / ERYTHROID DIFFERENTIATION RELATED FACTOR
分子量: 10862.253 Da / 分子数: 1 / 断片: RESIDUES 3-94 / 由来タイプ: 組換発現 / 詳細: ASP 29-PRO 30 PEPTIDE BOND IN TRANS CONFORMATION / 由来: (組換発現) HOMO SAPIENS (ヒト) / プラスミド: PRSET (A) / 発現宿主: ESCHERICHIA COLI BL21(DE3) (大腸菌) / Variant (発現宿主): C41 / 参照: UniProt: Q9NZD4
構成要素の詳細
ACTS AS A CHAPERONE TO PREVENT THE HARMFUL AGGREGATION OF ALPHA-HEMOGLOBIN DURING NORMAL ERYTHROID ...ACTS AS A CHAPERONE TO PREVENT THE HARMFUL AGGREGATION OF ALPHA-HEMOGLOBIN DURING NORMAL ERYTHROID CELL DEVELOPMENT.
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実験情報
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実験
実験
手法: 溶液NMR
NMR実験
Conditions-ID
Experiment-ID
Solution-ID
タイプ
1
1
1
HSQC
1
2
1
HNCO
1
3
1
HN(CA)CO
1
4
1
HN(CA)CB
1
5
1
CBCA(CO)NH
1
6
1
(H)CCH-COSY
2
7
1
DQF- COSY
2
8
1
TOCSY
2
9
1
HSQC
2
10
1
NOESY
2
11
1
3D- 15N-HSQC-NOESY
2
12
1
3D-13C-HSQC- NOESY
NMR実験の詳細
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY
手法: CNS / ソフトェア番号: 1 詳細: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMRアンサンブル
コンフォーマー選択の基準: NO DISTANCE VIOLATIONS WERE GREATER THAN 0.3 A, NO ANGLE VIOLATIONS WERE GREATER THAN 5.0 DEGREES, AND NO RDC VIOLATIONS WERE GREATER THAN 2.5 HZ 計算したコンフォーマーの数: 40 / 登録したコンフォーマーの数: 20