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- PDB-8sg2: BIVALENT INTERACTIONS OF PIN1 WITH THE C-TERMINAL TAIL OF PKC -

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基本情報

登録情報
データベース: PDB / ID: 8sg2
タイトルBIVALENT INTERACTIONS OF PIN1 WITH THE C-TERMINAL TAIL OF PKC
要素
  • Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
  • Protein kinase C beta type
キーワードISOMERASE / bivalent complex / Pin1 / protein kinase C / hydrophobic motif / turn motif
機能・相同性
機能・相同性情報


dibenzo-p-dioxin metabolic process / Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / cellular response to carbohydrate stimulus / protein kinase C signaling / positive regulation of odontogenesis of dentin-containing tooth / spectrin / regulation of D-glucose transmembrane transport / Trafficking of GluR2-containing AMPA receptors / Depolymerization of the Nuclear Lamina ...dibenzo-p-dioxin metabolic process / Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / cellular response to carbohydrate stimulus / protein kinase C signaling / positive regulation of odontogenesis of dentin-containing tooth / spectrin / regulation of D-glucose transmembrane transport / Trafficking of GluR2-containing AMPA receptors / Depolymerization of the Nuclear Lamina / WNT5A-dependent internalization of FZD4 / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / calcium,diacylglycerol-dependent serine/threonine kinase activity / protein kinase C / phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / negative regulation of D-glucose transmembrane transport / diacylglycerol-dependent serine/threonine kinase activity / mitotic nuclear membrane disassembly / cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / response to vitamin D / regulation of protein localization to nucleus / GTPase activating protein binding / response to angiotensin / RUNX1 regulates transcription of genes involved in differentiation of myeloid cells / regulation of growth / positive regulation of vascular endothelial growth factor receptor signaling pathway / protein targeting to mitochondrion / lipoprotein transport / protein peptidyl-prolyl isomerization / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / nuclear androgen receptor binding / regulation of synaptic vesicle exocytosis / negative regulation of SMAD protein signal transduction / PI5P Regulates TP53 Acetylation / regulation of dopamine secretion / negative regulation of amyloid-beta formation / B cell activation / cytoskeletal motor activity / postsynaptic cytosol / RHO GTPases Activate NADPH Oxidases / phosphoserine residue binding / presynaptic cytosol / response to glucose / calcium channel regulator activity / presynaptic modulation of chemical synaptic transmission / negative regulation of protein binding / positive regulation of GTPase activity / calyx of Held / negative regulation of insulin receptor signaling pathway / VEGFR2 mediated cell proliferation / peptidyl-prolyl cis-trans isomerase activity / protein kinase C binding / regulation of cytokinesis / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / peptidylprolyl isomerase / B cell receptor signaling pathway / phosphoprotein binding / Negative regulators of DDX58/IFIH1 signaling / negative regulation of transforming growth factor beta receptor signaling pathway / Activation of NF-kappaB in B cells / brush border membrane / synapse organization / negative regulation of ERK1 and ERK2 cascade / regulation of protein stability / negative regulation of protein catabolic process / positive regulation of insulin secretion / beta-catenin binding / tau protein binding / ISG15 antiviral mechanism / intracellular calcium ion homeostasis / neuron differentiation / positive regulation of angiogenesis / calcium ion transport / G alpha (z) signalling events / positive regulation of canonical Wnt signaling pathway / positive regulation of protein phosphorylation / regulation of gene expression / midbody / cellular response to hypoxia / Regulation of TP53 Activity through Phosphorylation / adaptive immune response / histone binding / response to ethanol / positive regulation of canonical NF-kappaB signal transduction / transcription coactivator activity / histone H3T6 kinase activity / response to hypoxia / protein stabilization / intracellular signal transduction / nuclear speck / ciliary basal body / protein phosphorylation / response to xenobiotic stimulus / protein serine kinase activity / protein serine/threonine kinase activity
類似検索 - 分子機能
Classical protein kinase C beta, catalytic domain / Protein kinase C, alpha/beta/gamma types / : / Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site / PpiC-type peptidyl-prolyl cis-trans isomerase signature. / PPIC-type PPIASE domain / PpiC-type peptidyl-prolyl cis-trans isomerase family profile. / Peptidyl-prolyl cis-trans isomerase, PpiC-type / Protein kinase, C-terminal / Protein kinase C terminal domain ...Classical protein kinase C beta, catalytic domain / Protein kinase C, alpha/beta/gamma types / : / Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site / PpiC-type peptidyl-prolyl cis-trans isomerase signature. / PPIC-type PPIASE domain / PpiC-type peptidyl-prolyl cis-trans isomerase family profile. / Peptidyl-prolyl cis-trans isomerase, PpiC-type / Protein kinase, C-terminal / Protein kinase C terminal domain / Diacylglycerol/phorbol-ester binding / Phorbol esters/diacylglycerol binding domain (C1 domain) / Zinc finger phorbol-ester/DAG-type signature. / Protein kinase C conserved region 2 (CalB) / C2 domain / WW domain / WW/rsp5/WWP domain signature. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C2 domain / C2 domain profile. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / Peptidyl-prolyl cis-trans isomerase domain superfamily / C2 domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
類似検索 - ドメイン・相同性
Protein kinase C beta type / Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
類似検索 - 構成要素
生物種Homo sapiens (ヒト)
手法溶液NMR / torsion angle dynamics / simulated annealing
データ登録者Dixit, K. / Yang, Y. / Chen, X.R. / Igumenova, T.I.
資金援助 米国, 2件
組織認可番号国
Welch FoundationA-1784 米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM108998 米国
引用ジャーナル: Elife / 年: 2024
タイトル: A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation.
著者: Chen, X.R. / Dixit, K. / Yang, Y. / McDermott, M.I. / Imam, H.T. / Bankaitis, V.A. / Igumenova, T.I.
履歴
登録2023年4月11日登録サイト: RCSB / 処理サイト: RCSB
改定 1.02024年5月8日Provider: repository / タイプ: Initial release
改定 1.12024年5月15日Group: Database references / カテゴリ: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
改定 1.22024年11月20日Group: Structure summary
カテゴリ: pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification

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構造の表示

構造ビューア分子:
MolmilJmol/JSmol

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集合体

登録構造単位
A: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
B: Protein kinase C beta type


分子量 (理論値)分子数
合計 (水以外)21,1242
ポリマ－21,1242
非ポリマー00
水00
1


  • 登録構造と同一
  • 登録者が定義した集合体
  • 根拠: NMR-detected binding experiments provided direct evidence of the complex formation.
タイプ名称対称操作数
identity operation1_555x,y,z1
NMR アンサンブル
データ基準
コンフォーマー数 (登録 / 計算)20 / 50structures with the lowest energy
代表モデルモデル #1lowest energy

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要素

#1: タンパク質 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 / Peptidyl-prolyl cis-trans isomerase Pin1 / PPIase Pin1 / Rotamase Pin1


分子量: 18271.309 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: PIN1 / プラスミド: PET SUMO / Cell (発現宿主): CYTOPLASM / 発現宿主: Escherichia coli BL21(DE3) (大腸菌) / 株 (発現宿主): BL21(DE3) / 参照: UniProt: Q13526, peptidylprolyl isomerase
#2: タンパク質・ペプチド Protein kinase C beta type / PKC-B / PKC-beta


分子量: 2852.888 Da / 分子数: 1 / Fragment: C-TERMINAL RESIDUES 639-661 / 由来タイプ: 合成 / 由来: (合成) Homo sapiens (ヒト) / 参照: UniProt: P05771, protein kinase C
研究の焦点であるリガンドがあるかY
Has protein modificationY

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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-IDExperiment-IDSolution-IDSample stateSpectrometer-IDタイプ
111isotropic12D [15N,1H] HSQC
121isotropic12D 1H-15N HSQC NH2
131isotropic13D HNCO
141isotropic23D HN(CA)CB
151isotropic13D C(CO)NH
161isotropic23D CBCA(CO)NH
171isotropic23D HN(CA)CO
181isotropic23D HNHA
191isotropic23D HNHB
1101isotropic13D H(CCO)NH
1111isotropic13D 15N-EDITED NOESY- HSQC
1121isotropic13D [F1] 13C,15N-FILTERED NOESY-15N-HSQC
2132isotropic13D [F1] 13C,15N-FILTERED NOESY-13C-HSQC
2142isotropic13D 13C-EDITED NOESY- HSQC
2152isotropic23D 13Caro-EDITED NOESY- HSQC
2162isotropic12D CT [13C, 1H] HSQC
2172isotropic12D CT 1H-13C AROMATIC HSQC
2182isotropic13D (H)CCH-TOCSY
2192isotropic13D (H)CCH-COSY
1201isotropic22D (HB)CB(CGCDCE)HE
1211isotropic22D (HB)CB(CGCD)HD
1223isotropic12D [F1] 13C, 15N- FILTERED NOESY
1233isotropic12D [F2] 13C,15N- FILTERED NOESY
1243isotropic22D [F1,F2] 13C,15N-FILTERED NOESY
1253isotropic12D [F1,F2] 13C,15N-FILTERED TOCSY
1264isotropic13D [F1] 13C,15N-FILTERED NOESY-15N-HSQC
1274isotropic13D [F1] 13C, 15N-FILTERED NOESY- 13Caro-HSQC
1285isotropic12D [F1] 13C,15N- FILTERED NOESY
1295isotropic12D [F2] 13C,15N- FILTERED NOESY
1305isotropic12D [F1,F2] 13C,15N-FILTERED NOESY
1315isotropic12D [F1,F2] 13C,15N-FILTERED TOCSY
1326isotropic13D [F1] 13C,15N-FILTERED NOESY-15N-HSQC
1336isotropic13D [F1] 13C, 15N-FILTERED NOESY- 13Caro-HSQC
1346isotropic13D [F1] 13C, 15N-FILTERED NOESY- 13Cali-HSQC
1356isotropic12D [15N,1H] HSQC
1366isotropic12D CT [13C, 1H] HSQC
1376isotropic33D HN(CA)CB
1387isotropic13D [F1] 13C,15N-FILTERED NOESY-15N-HSQC
1397isotropic13D [F1] 13C,15N-FILTERED NOESY-13C-HSQC
1407isotropic12D [15N,1H] HSQC
1417isotropic12D CT [13C, 1H] HSQC
1428isotropic13D [F1] 13C,15N-FILTERED NOESY-15N-HSQC
1438isotropic13D [F1] 13C,15N-FILTERED NOESY-13C-HSQC
1449isotropic12D [F1] 13C, 15N- FILTERED NOESY
1459isotropic12D [F2] 13C, 15N- FILTERED NOESY
1469isotropic12D [F1,F2] 13C,15N-FILTERED NOESY
1479isotropic12D [F1,F2] 13C,15N-FILTERED TOCSY

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試料調製

詳細
タイプSolution-ID内容詳細Label溶媒系
solution11.05 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 0.9 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-Pin1+pV5bII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3[U-13C, 15N-Pin1+pV5bII]92% H2O/8% D2O
solution21.05 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 0.9 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 100% D2O[U-13C, 15N-Pin1+pV5bII]-D2O The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, and 0.02% NaN3[U-13C, 15N-Pin1+pV5bII]-D2O100% D2O
solution31 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 1.3 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-Pin1-saturated-pV5bII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, and 0.02% NaN[U-13C, 15N-Pin1-saturated-pV5bII]92% H2O/8% D2O
solution40.8 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 5.5 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-PPIase+pHMbII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3[U-13C, 15N-PPIase+pHMbII]92% H2O/8% D2O
solution50.5 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 1.8 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-PPIase-saturated-pHMbII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3[U-13C, 15N-PPIase-saturated-pHMbII]92% H2O/8% D2O
solution60.5 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 2.5 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[na-PPIase+selective residues-13C,15N pHMbII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3PPIase+[U-13C,15N Phe]pHMbII92% H2O/8% D2O
solution71 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 1.5 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[na-Pin1+selective residues-13C,15N pTMbII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3Pin1+[U-13C,15N Pro, Ile, Val]pTMbII92% H2O/8% D2O
solution81.3 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 1 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-Pin1+Ext-pV5bII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3[U-13C, 15N-Pin1+Ext-pV5bII]92% H2O/8% D2O
solution90.8 mM [U-13C; U-15N] PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, 1.3 mM The C-terminal tail of PKC, 10 mM [U-100% 2H] imidazole, 100 mM potassium chloride, 1 mM TCEP, 0.02 % w/v sodium azide, 92% H2O/8% D2O[U-13C, 15N-Pin1-saturated-Ext-pV5bII] The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3[U-13C, 15N-Pin1-saturated-Ext-pV5bII]92% H2O/8% D2O
試料
濃度 (mg/ml)構成要素Isotopic labelingSolution-ID
1.05 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]1
0.9 mMThe C-terminal tail of PKCnatural abundance1
10 mMimidazole[U-100% 2H]1
100 mMpotassium chloridenatural abundance1
1 mMTCEPnatural abundance1
0.02 % w/vsodium azidenatural abundance1
1.05 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]2
0.9 mMThe C-terminal tail of PKCnatural abundance2
10 mMimidazole[U-100% 2H]2
100 mMpotassium chloridenatural abundance2
1 mMTCEPnatural abundance2
0.02 % w/vsodium azidenatural abundance2
1 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]3
1.3 mMThe C-terminal tail of PKCnatural abundance3
10 mMimidazole[U-100% 2H]3
100 mMpotassium chloridenatural abundance3
1 mMTCEPnatural abundance3
0.02 % w/vsodium azidenatural abundance3
0.8 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]4
5.5 mMThe C-terminal tail of PKCnatural abundance4
10 mMimidazole[U-100% 2H]4
100 mMpotassium chloridenatural abundance4
1 mMTCEPnatural abundance4
0.02 % w/vsodium azidenatural abundance4
0.5 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]5
1.8 mMThe C-terminal tail of PKCnatural abundance5
10 mMimidazole[U-100% 2H]5
100 mMpotassium chloridenatural abundance5
1 mMTCEPnatural abundance5
0.02 % w/vsodium azidenatural abundance5
0.5 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]6
2.5 mMThe C-terminal tail of PKCnatural abundance6
10 mMimidazole[U-100% 2H]6
100 mMpotassium chloridenatural abundance6
1 mMTCEPnatural abundance6
0.02 % w/vsodium azidenatural abundance6
1 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]7
1.5 mMThe C-terminal tail of PKCnatural abundance7
10 mMimidazole[U-100% 2H]7
100 mMpotassium chloridenatural abundance7
1 mMTCEPnatural abundance7
0.02 % w/vsodium azidenatural abundance7
1.3 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]8
1 mMThe C-terminal tail of PKCnatural abundance8
10 mMimidazole[U-100% 2H]8
100 mMpotassium chloridenatural abundance8
1 mMTCEPnatural abundance8
0.02 % w/vsodium azidenatural abundance8
0.8 mMPEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1[U-13C; U-15N]9
1.3 mMThe C-terminal tail of PKCnatural abundance9
10 mMimidazole[U-100% 2H]9
100 mMpotassium chloridenatural abundance9
1 mMTCEPnatural abundance9
0.02 % w/vsodium azidenatural abundance9
試料状態

イオン強度: 0.1 M / pH: 6.66 / PH err: 0.02 / 圧: 1 atm / Pressure err: 0.001 / 温度: 298 K / Temperature err: 0.2

Conditions-ID詳細Label
1The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 8% D2O, and 0.02% NaN3condition_1
2The NMR buffer contained 10 mM D4-imidazole at pH 6.6, 100 mM KCl, 1 mM TCEP, 100% D2O, and 0.02% NaN3condition_2

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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詳細
Bruker AVANCEBrukerAVANCE8001cryoprobe
Bruker AVANCEBrukerAVANCE6002cryoprobe
Bruker AVANCEBrukerAVANCE5003room temperature probe

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解析

NMR software
名称開発者分類
X-PLOR NIHSCHWIETERS, KUSZEWSKI, Tjandra and Clore精密化
CYANAGuntert, Mumenthaler, and Wuthrichstructure calculation
CcpNmr AnalysisCCPNchemical shift assignment
NMRDrawDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxpeak picking
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax解析
精密化
手法ソフトェア番号詳細
torsion angle dynamics2STRUCTURE DETERMINATION
simulated annealing1water-refinement
代表構造選択基準: lowest energy
NMRアンサンブルコンフォーマー選択の基準: structures with the lowest energy
計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 20

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  • このバージョンアップで、電子顕微鏡の実験手法に関する多くの項目の書式が改定されました(例：em_softwareなど)。
  • EM NavigatorとYorodumiでも、この改定に基づいた表示内容になります。

外部リンク:wwPDB Remediation / OneDepデータ基準に準拠した、より強化された内容のモデル構造ファイルが、PDBアーカイブで公開されました。

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万見 (Yorodumi)

幾万の構造データを、幾万の視点から

  • 万見(Yorodumi)は、EMDB/PDB/SASBDBなどの構造データを閲覧するためのページです。
  • EM Navigatorの詳細ページの後継、Omokage検索のフロントエンドも兼ねています。

関連情報:EMDB / PDB / SASBDB / 3つのデータバンクの比較 / 万見検索 / 2016年8月31日: 新しいEM Navigatorと万見 / 万見文献 / Jmol/JSmol / 機能・相同性情報 / 新しいEM Navigatorと万見の変更点

他の情報も見る