+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1bzg | ||||||
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タイトル | THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE-RELATED PROTEIN (1-34) IN NEAR-PHYSIOLOGICAL SOLUTION, NMR, 30 STRUCTURES | ||||||
要素 | PARATHYROID HORMONE-RELATED PROTEIN | ||||||
キーワード | HORMONE (ホルモン) / HUMAN PEPTIDE HORMONE (ペプチドホルモン) / STIMULATING INTRACELLULAR CAMP FORMATION / SERUM CALCIUM LEVEL / HUMORAL HYPERCALCEMIA OF MALIGNANCY / SOLUTION STRUCTURE / PTHRP / PTH | ||||||
機能・相同性 | 機能・相同性情報 negative regulation of chondrocyte development / regulation of chondrocyte differentiation / cAMP metabolic process / negative regulation of chondrocyte differentiation / Class B/2 (Secretin family receptors) / osteoblast development / peptide hormone receptor binding / bone mineralization / epidermis development / skeletal system development ...negative regulation of chondrocyte development / regulation of chondrocyte differentiation / cAMP metabolic process / negative regulation of chondrocyte differentiation / Class B/2 (Secretin family receptors) / osteoblast development / peptide hormone receptor binding / bone mineralization / epidermis development / skeletal system development / female pregnancy / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / cell-cell signaling / G alpha (s) signalling events / 遺伝子発現の調節 / negative regulation of cell population proliferation / positive regulation of cell population proliferation / ゴルジ体 / extracellular space / extracellular region / 核質 / 細胞質基質 / 細胞質 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | 溶液NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
データ登録者 | Weidler, M. / Marx, U.C. / Seidel, G. / Roesch, P. | ||||||
引用 | ジャーナル: FEBS Lett. / 年: 1999 タイトル: The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution. 著者: Weidler, M. / Marx, U.C. / Seidel, G. / Schafer, W. / Hoffmann, E. / Esswein, A. / Rosch, P. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 1bzg.cif.gz | 338.1 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1bzg.ent.gz | 280.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1bzg.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/bz/1bzg ftp://data.pdbj.org/pub/pdb/validation_reports/bz/1bzg | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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NMR アンサンブル |
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-要素
#1: タンパク質・ペプチド | 分子量: 4027.636 Da / 分子数: 1 / 断片: RESIDUES 1-34 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 参照: UniProt: P12272 |
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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
詳細 | 内容: H2O/D2O (9:1) |
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試料状態 | イオン強度: 550mM / pH: 5.1 / 圧: 10E+5PA atm / 温度: 277 K |
結晶化 | *PLUS 手法: その他 / 詳細: NMR |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker AMX600 / 製造業者: Bruker / モデル: AMX600 / 磁場強度: 600 MHz |
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-解析
ソフトウェア |
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NMR software |
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精密化 | 手法: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS / ソフトェア番号: 1 詳細: STRATEGY USED FOR NMR STRUCTURE CALCULATION: EXPERIMENTAL RESTRAINTS FOR THE STRUCTURE CALCULATIONS INITIALLY, FREQUENCY DEGENERATED NOESY CROSS-PEAKS WERE INCORPORATED INTO THE STRUCTURE ...詳細: STRATEGY USED FOR NMR STRUCTURE CALCULATION: EXPERIMENTAL RESTRAINTS FOR THE STRUCTURE CALCULATIONS INITIALLY, FREQUENCY DEGENERATED NOESY CROSS-PEAKS WERE INCORPORATED INTO THE STRUCTURE CALCULATION AS 'AMBIGUOUS'. SUBSEQUENTLY, THE PROTON- PROTON DISTANCES IN THE CALCULATED STRUCTURES WERE DETERMINED USING THE PROGRAM BACKCALC_DB 2.0 (SOFTWARE SYMBIOSE, INC., BAYREUTH, GERMANY) AND COMPARED WITH THE COMBINATIONS OF DISTANCES POSSIBLE FOR EACH FREQUENCY DEGENERATED NOESY CROSS-PEAK. IF ONLY ONE OF THE POSSIBLE DISTANCE COMBINATIONS WAS FULFILLED IN MORE THAN 50% OF THE CALCULATED STRUCTURES, THE DISTANCE INFORMATION WAS USED IN FURTHER STRUCTURE CALCULATIONS. THIS PROCEDURE WAS REPEATED SEVERAL TIMES, LEADING TO A TOTAL OF 424 INTRARESIDUAL AND 337 INTERRESIDUAL NOE CONNECTIVITIES. STRUCTURES CALCULATIONS WERE PERFORMED USING A MODIFIED AB INITIO SIMULATED ANNEALING PROTOCOL (NILGES, UNPUBLISHED) WITH X-PLOR V3.840. THE CALCULATION STRATEGY INCLUDES FLOATING ASSIGNMENT OF PROCHIRAL GROUPS AND A REDUCED PRESENTATION FOR NON-BONDED INTERACTIONS FOR PART OF THE CALCULATION TO INCREASE EFFICIENCY. A MORE DETAILED DESCRIPTION OF THE PROTOCOL IS GIVEN IN KHARRAT ET AL. (EMBO J. 14 (1995) 3572-84). STRUCTURE PARAMETERS WERE EXTRACTED FROM THE STANDARD FILES PARALLHDG.PRO AND TOPALLHDG.PRO OF X-PLOR V3.840. IN EACH ROUND OF THE STRUCTURE CALCULATION 100 STRUCTURES WERE CALCULATED. OF THE 100 STRUCTURES RESULTING FROM THE FINAL ROUND OF STRUCTURE CALCULATION, THOSE 30 STRUCTURES THAT SHOWED THE LOWEST TOTAL ENERGY VALUES WERE SELECTED FOR FURTHER CHARACTERIZATION. | ||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: ENERGY, AGREEMENT WITH EXPERIMENTAL DATA 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: 30 |