Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
Remark 999
SEQUENCE The sequence here corresponds to a strain different than that found in the sequence ...SEQUENCE The sequence here corresponds to a strain different than that found in the sequence database (GenBank accession CAB98186).
structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy
代表モデル
モデル #1
fewest violations,lowest energy
-
要素
#1: タンパク質・ペプチド
GAGprotein
分子量: 4872.646 Da / 分子数: 1 / 断片: RESIDUES 390-431 / 変異: C28H / 由来タイプ: 合成 詳細: Two peptides have been chemically synthesized with and without a 15N/13C labelled Histidine residue at position 28 参照: UniProt: Q9PY17
Text: The structure was determined using standard 2D homonuclear experiments and 1H-15N HSQC experiments.
-
試料調製
詳細
Solution-ID
内容
溶媒系
1
2 mM His28(12-53)NCp7 90% H2O, 10% D2O with 3 equivalents of zinc
90% H2O, 10% D2O, pH6.6from278Kto323K
2
2 mM His28(12-53)NCp7 100% D2O with 3 equivalents of zinc
100% D2O, pH6.6from278Kto323K
試料状態
Conditions-ID
イオン強度
pH
圧 (kPa)
温度 (K)
1
6mMZnSO4
6.6
ambient
278K
2
6mMZnSO4
6.6
ambient
293K
-
NMR測定
放射
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M
放射波長
相対比: 1
NMRスペクトロメーター
タイプ: Bruker AMX / 製造業者: Bruker / モデル: AMX / 磁場強度: 600 MHz
-
解析
NMR software
名称
バージョン
開発者
分類
XwinNMR
Version3.0
Bruker
collection
XwinNMR
Version3.0
Bruker
解析
Felix
Version98.0
Accelrys
データ解析
X-PLOR
Version3.851
Brunger
精密化
精密化
手法: distance geometry, simulated annealing, molecular dynamics ソフトェア番号: 1 詳細: The structure has been calculated using 339 NOE derived distance restraints.
代表構造
選択基準: fewest violations,lowest energy
NMRアンサンブル
コンフォーマー選択の基準: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy 計算したコンフォーマーの数: 100 / 登録したコンフォーマーの数: 1