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- PDB-7mo0: Crystal Structure of Nucleoporin NUP50 Ran-Binding Domain in Comp... -

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基本情報

登録情報
データベース: PDB / ID: 7mo0
タイトルCrystal Structure of Nucleoporin NUP50 Ran-Binding Domain in Complex with Ran-GPPNHP
要素
  • GTP-binding nuclear protein Ran
  • Nuclear pore complex protein Nup50
キーワードTRANSPORT PROTEIN / nuclear pore complex component / nucleocytoplasmic transport / complex (small GTPase-nuclear protein)
機能・相同性
機能・相同性情報


neural tube formation / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Nuclear Pore Complex (NPC) Disassembly / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Transport of the SLBP independent Mature mRNA ...neural tube formation / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Nuclear Pore Complex (NPC) Disassembly / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Transport of the SLBP independent Mature mRNA / NS1 Mediated Effects on Host Pathways / Transport of the SLBP Dependant Mature mRNA / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / SUMOylation of RNA binding proteins / NEP/NS2 Interacts with the Cellular Export Machinery / Transport of Mature mRNA derived from an Intron-Containing Transcript / GTP metabolic process / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / MicroRNA (miRNA) biogenesis / Viral Messenger RNA Synthesis / DNA metabolic process / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / mitotic sister chromatid segregation / SUMOylation of DNA replication proteins / ribosomal large subunit export from nucleus / Regulation of HSF1-mediated heat shock response / mRNA transport / viral process / nuclear pore / ribosomal subunit export from nucleus / SUMOylation of DNA damage response and repair proteins / ribosomal small subunit export from nucleus / centriole / SUMOylation of chromatin organization proteins / protein export from nucleus / HCMV Late Events / mitotic spindle organization / Transcriptional regulation by small RNAs / recycling endosome / ISG15 antiviral mechanism / positive regulation of protein import into nucleus / HCMV Early Events / positive regulation of protein binding / protein import into nucleus / GDP binding / melanosome / nuclear envelope / mitotic cell cycle / G protein activity / snRNP Assembly / midbody / 加水分解酵素; 酸無水物に作用; GTPに作用・細胞または細胞小器官の運動に関与 / nuclear membrane / cadherin binding / protein heterodimerization activity / cell division / GTPase activity / chromatin binding / GTP binding / chromatin / nucleolus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / magnesium ion binding / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / nucleus / membrane / cytosol / cytoplasm
類似検索 - 分子機能
Nuclear pore complex, NUP2/50/61 / NUP50 (Nucleoporin 50 kDa) / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / Ran GTPase / Small GTPase Ran-type domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) ...Nuclear pore complex, NUP2/50/61 / NUP50 (Nucleoporin 50 kDa) / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / Ran GTPase / Small GTPase Ran-type domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / PH-like domain superfamily / Roll / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
類似検索 - ドメイン・相同性
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GTP-binding nuclear protein Ran / Nuclear pore complex protein Nup50
類似検索 - 構成要素
生物種Homo sapiens (ヒト)
手法X線回折 / シンクロトロン / 単波長異常分散 / 解像度: 2.45 Å
データ登録者Bley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. ...Bley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. / Brown, B. / Tang, A.W. / Rundlet, E.J. / Correia, A.R. / Chen, S. / Regmi, S.G. / Stevens, T.A. / Jette, C.A. / Dasso, M. / Patke, A. / Palazzo, A.F. / Kossiakoff, A.A. / Hoelz, A.
資金援助 米国, 3件
組織認可番号国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM117360 米国
Howard Hughes Medical Institute (HHMI)55108534 米国
Heritage Medical Research Institute 米国
引用ジャーナル: Science / 年: 2022
タイトル: Architecture of the cytoplasmic face of the nuclear pore.
著者: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / ...著者: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / Emily J Rundlet / Ana R Correia / Shane Chen / Saroj G Regmi / Taylor A Stevens / Claudia A Jette / Mary Dasso / Alina Patke / Alexander F Palazzo / Anthony A Kossiakoff / André Hoelz /
要旨: INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are ...INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are generated by the circumscribed fusion of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) are the sole bidirectional gateways for nucleocytoplasmic transport. The ~110-MDa human NPC is an ~1000-protein assembly that comprises multiple copies of ~34 different proteins, collectively termed nucleoporins. The symmetric core of the NPC is composed of an inner ring encircling the central transport channel and outer rings formed by Y‑shaped coat nucleoporin complexes (CNCs) anchored atop both sides of the nuclear envelope. The outer rings are decorated with compartment‑specific asymmetric nuclear basket and cytoplasmic filament nucleoporins, which establish transport directionality and provide docking sites for transport factors and the small guanosine triphosphatase Ran. The cytoplasmic filament nucleoporins also play an essential role in the irreversible remodeling of messenger ribonucleoprotein particles (mRNPs) as they exit the central transport channel. Unsurprisingly, the NPC's cytoplasmic face represents a hotspot for disease‑associated mutations and is commonly targeted by viral virulence factors. RATIONALE Previous studies established a near-atomic composite structure of the human NPC's symmetric core by combining (i) biochemical reconstitution to elucidate the interaction network between symmetric nucleoporins, (ii) crystal and single-particle cryo-electron microscopy structure determination of nucleoporins and nucleoporin complexes to reveal their three-dimensional shape and the molecular details of their interactions, (iii) quantitative docking in cryo-electron tomography (cryo-ET) maps of the intact human NPC to uncover nucleoporin stoichiometry and positioning, and (iv) cell‑based assays to validate the physiological relevance of the biochemical and structural findings. In this work, we extended our approach to the cytoplasmic filament nucleoporins to reveal the near-atomic architecture of the cytoplasmic face of the human NPC. RESULTS Using biochemical reconstitution, we elucidated the protein-protein and protein-RNA interaction networks of the human and cytoplasmic filament nucleoporins, establishing an evolutionarily conserved heterohexameric cytoplasmic filament nucleoporin complex (CFNC) held together by a central heterotrimeric coiled‑coil hub that tethers two separate mRNP‑remodeling complexes. Further biochemical analysis and determination of a series of crystal structures revealed that the metazoan‑specific cytoplasmic filament nucleoporin NUP358 is composed of 16 distinct domains, including an N‑terminal S‑shaped α‑helical solenoid followed by a coiled‑coil oligomerization element, numerous Ran‑interacting domains, an E3 ligase domain, and a C‑terminal prolyl‑isomerase domain. Physiologically validated quantitative docking into cryo-ET maps of the intact human NPC revealed that pentameric NUP358 bundles, conjoined by the oligomerization element, are anchored through their N‑terminal domains to the central stalk regions of the CNC, projecting flexibly attached domains as far as ~600 Å into the cytoplasm. Using cell‑based assays, we demonstrated that NUP358 is dispensable for the architectural integrity of the assembled interphase NPC and RNA export but is required for efficient translation. After NUP358 assignment, the remaining 4-shaped cryo‑ET density matched the dimensions of the CFNC coiled‑coil hub, in close proximity to an outer-ring NUP93. Whereas the N-terminal NUP93 assembly sensor motif anchors the properly assembled related coiled‑coil channel nucleoporin heterotrimer to the inner ring, biochemical reconstitution confirmed that the NUP93 assembly sensor is reused in anchoring the CFNC to the cytoplasmic face of the human NPC. By contrast, two CFNCs are anchored by a divergent mechanism that involves assembly sensors located in unstructured portions of two CNC nucleoporins. Whereas unassigned cryo‑ET density occupies the NUP358 and CFNC binding sites on the nuclear face, docking of the nuclear basket component ELYS established that the equivalent position on the cytoplasmic face is unoccupied, suggesting that mechanisms other than steric competition promote asymmetric distribution of nucleoporins. CONCLUSION We have substantially advanced the biochemical and structural characterization of the asymmetric nucleoporins' architecture and attachment at the cytoplasmic and nuclear faces of the NPC. Our near‑atomic composite structure of the human NPC's cytoplasmic face provides a biochemical and structural framework for elucidating the molecular basis of mRNP remodeling, viral virulence factor interference with NPC function, and the underlying mechanisms of nucleoporin diseases at the cytoplasmic face of the NPC. [Figure: see text].
履歴
登録2021年5月1日登録サイト: RCSB / 処理サイト: RCSB
改定 1.02022年6月15日Provider: repository / タイプ: Initial release
改定 1.12022年6月22日Group: Database references / カテゴリ: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID / _citation_author.name
改定 1.22024年10月16日Group: Data collection / Structure summary
カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / 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

ダウンロードとリンク

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集合体

登録構造単位
A: GTP-binding nuclear protein Ran
B: Nuclear pore complex protein Nup50
C: GTP-binding nuclear protein Ran
D: Nuclear pore complex protein Nup50
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)81,0939
ポリマ－79,9044
非ポリマー1,1895
水1,13563
1
A: GTP-binding nuclear protein Ran
B: Nuclear pore complex protein Nup50
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)40,4984
ポリマ－39,9522
非ポリマー5472
水362
タイプ名称対称操作数
identity operation1_555x,y,z1
Buried area5160 Å2
ΔGint-36 kcal/mol
Surface area17010 Å2
手法PISA
2
C: GTP-binding nuclear protein Ran
D: Nuclear pore complex protein Nup50
ヘテロ分子


分子量 (理論値)分子数
合計 (水以外)40,5945
ポリマ－39,9522
非ポリマー6433
水362
タイプ名称対称操作数
identity operation1_555x,y,z1
Buried area5310 Å2
ΔGint-55 kcal/mol
Surface area16710 Å2
手法PISA
単位格子
Length a, b, c (Å)66.590, 73.170, 152.940
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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要素

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タンパク質 , 2種, 4分子 ACBD

#1: タンパク質 GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


分子量: 24730.764 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: RAN, ARA24, OK/SW-cl.81 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P62826
#2: タンパク質 Nuclear pore complex protein Nup50 / 50 kDa nucleoporin / Nuclear pore-associated protein 60 kDa-like / Nucleoporin Nup50


分子量: 15221.078 Da / 分子数: 2
Fragment: RAN-binding domain of NUP50 (UNP residues 337-468)
由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: NUP50, NPAP60L, PRO1146 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q9UKX7

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非ポリマー , 4種, 68分子

#3: 化合物 ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Gpp(NH)p


分子量: 522.196 Da / 分子数: 2 / 由来タイプ: 合成 / 式: C10H17N6O13P3
コメント: GppNHp, GMPPNP, エネルギー貯蔵分子類似体*YM
#4: 化合物 ChemComp-MG / MAGNESIUM ION / マグネシウムジカチオン


分子量: 24.305 Da / 分子数: 2 / 由来タイプ: 合成 / 式: Mg
#5: 化合物 ChemComp-SO4 / SULFATE ION / 硫酸ジアニオン


分子量: 96.063 Da / 分子数: 1 / 由来タイプ: 合成 / 式: SO4
#6: 水 ChemComp-HOH / water


分子量: 18.015 Da / 分子数: 63 / 由来タイプ: 天然 / 式: H2O

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詳細

研究の焦点であるリガンドがあるかN
Has protein modificationY

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実験情報

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実験

実験手法: X線回折 / 使用した結晶の数: 1

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試料調製

結晶マシュー密度: 2.35 Å3/Da / 溶媒含有率: 47.68 %
結晶化温度: 294 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 7.5
詳細: 25% w/v PEG3350, 0.2 M ammonium sulfate, 0.1 M HEPES

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データ収集

回折平均測定温度: 100 K / Serial crystal experiment: N
放射光源由来: シンクロトロン / サイト: APS / ビームライン: 23-ID-D / 波長: 0.97942 Å
検出器タイプ: DECTRIS PILATUS 6M / 検出器: PIXEL / 日付: 2019年8月7日
放射プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長波長: 0.97942 Å / 相対比: 1
反射解像度: 2.45→29.73 Å / Num. obs: 52982 / % possible obs: 100 % / 冗長度: 13.1 % / Biso Wilson estimate: 56.22 Å2 / Rpim(I) all: 0.034 / Rrim(I) all: 0.125 / Net I/σ(I): 15.3
反射 シェル

Diffraction-ID: 1 / % possible all: 100

解像度 (Å)冗長度 (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all
2.45-2.5413.31.13662927620.7332.693
5.27-29.7312.340.63715530220.0160.058

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解析

ソフトウェア
名称バージョン分類
xia2データスケーリング
PHENIX1.18.2精密化
PDB_EXTRACT3.27データ抽出
Cootモデル構築
AutoSol位相決定
XDSデータ削減
精密化構造決定の手法: 単波長異常分散 / 解像度: 2.45→29.73 Å / SU ML: 0.33 / 交差検証法: THROUGHOUT / σ(F): 1.34 / 位相誤差: 30.01 / 立体化学のターゲット値: ML
Rfactor反射数%反射
Rfree0.2387 2618 4.94 %
Rwork0.212 50364 -
obs0.2134 52982 99.93 %
溶媒の処理減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL
原子変位パラメータBiso max: 203.36 Å2 / Biso mean: 87.1956 Å2 / Biso min: 36.84 Å2
精密化ステップサイクル: final / 解像度: 2.45→29.73 Å
タンパク質核酸リガンド溶媒全体
原子数5345 0 95 63 5503
Biso mean--69.97 58.58 -
残基数----671
LS精密化 シェル

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 19

解像度 (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.45-2.490.4018960.38122674277099
2.49-2.540.34511310.348626572788100
2.54-2.590.32881050.354826752780100
2.59-2.650.32261230.322926462769100
2.65-2.710.34921260.329226572783100
2.71-2.780.39681420.316926742816100
2.78-2.860.33691300.307426282758100
2.86-2.940.29361450.283926792824100
2.94-3.030.28841840.266726462830100
3.03-3.140.29111500.260826022752100
3.14-3.270.32821800.252426042784100
3.27-3.420.31761240.234526932817100
3.42-3.60.23241470.220226042751100
3.6-3.820.2881500.210926672817100
3.82-4.110.17741250.179826762801100
4.12-4.530.18781640.156426102774100
4.53-5.180.15281410.154526572798100
5.18-6.520.22261290.187126582787100
6.52-29.730.21161260.182326572783100
精密化 TLS

手法: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.9513-0.73270.30242.95230.28633.1298-0.1507-0.15970.07560.25930.1725-0.28430.2220.1689-0.00890.5090.05290.01420.4737-0.00880.53248.0796-13.605818.8852
22.8356-3.0234-0.10635.4532-0.36985.6387-0.27250.10840.27730.31230.1726-0.2592-0.10040.11350.15480.5430.0001-0.03680.4785-0.00920.64215.0105-1.768715.0275
31.5446-0.00950.41730.8311-0.07270.682-0.108-0.5182-0.59310.4097-0.32570.20250.5504-0.40110.44950.9819-0.26140.15081.22320.09741.0338-26.5511-16.915521.9122
44.8041-0.00150.55941.23680.30031.6578-0.425-0.037-0.11350.21520.18390.0755-0.3987-0.26520.17270.71360.11270.06490.592-0.01320.6833-14.11213.189221.7534
52.26360.56140.65283.44850.1853.37680.2186-0.4297-0.34580.3022-0.13220.07660.6373-0.6459-0.07830.7259-0.07310.05610.74620.07520.6416-21.3379-10.587218.9155
63.6963-0.39240.36454.4745-0.00383.60310.1321-0.9712-0.46710.4076-0.11270.63770.7609-0.63460.02580.7819-0.22120.1030.84840.03290.7128-26.9063-10.972821.2452
72.98290.14810.33652.33161.0253.0290.0291-0.26050.11890.30210.058-0.1367-0.21770.063-0.05970.55370.0603-0.0170.46530.01890.516517.7598-40.94314.3856
83.1071-0.0915-0.45372.9346-0.61012.6831-0.1493-0.0603-0.28470.14630.10140.27340.2538-0.45730.05690.5635-0.0261-0.00010.5095-0.00120.55077.2493-47.52799.7622
91.7397-0.9905-0.57141.3850.47082.5201-0.2307-0.16120.2087-0.0135-0.0572-0.141-0.24010.3570.20390.9054-0.0765-0.11430.75130.08920.756840.4792-45.89128.8117
103.84681.40720.7984.8569-0.11278.4697-0.12730.1637-0.1665-0.24120.0493-0.08130.63570.14640.0870.51650.11880.03980.44290.05010.498235.9724-51.136516.7895
114.87441.2407-0.17473.9242-2.12727.3258-0.1833-0.5824-0.18130.1806-0.2725-0.37030.18541.07270.46220.57690.0991-0.02730.69020.05460.553442.2724-48.592125.6437
精密化 TLSグループ
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 140 )A6 - 140
2X-RAY DIFFRACTION2chain 'A' and (resid 141 through 179 )A141 - 179
3X-RAY DIFFRACTION3chain 'A' and (resid 180 through 216 )A180 - 216
4X-RAY DIFFRACTION4chain 'B' and (resid 343 through 362 )B343 - 362
5X-RAY DIFFRACTION5chain 'B' and (resid 363 through 435 )B363 - 435
6X-RAY DIFFRACTION6chain 'B' and (resid 436 through 468 )B436 - 468
7X-RAY DIFFRACTION7chain 'C' and (resid 4 through 66 )C4 - 66
8X-RAY DIFFRACTION8chain 'C' and (resid 67 through 178 )C67 - 178
9X-RAY DIFFRACTION9chain 'C' and (resid 179 through 216 )C179 - 216
10X-RAY DIFFRACTION10chain 'D' and (resid 345 through 408 )D345 - 408
11X-RAY DIFFRACTION11chain 'D' and (resid 409 through 468 )D409 - 468

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2020年8月12日: 新型コロナ情報

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2020年3月5日: 新型コロナウイルスの構造データ

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2019年1月31日: EMDBのIDの桁数の変更

EMDBのIDの桁数の変更

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2017年7月12日: PDB大規模アップデート

PDB大規模アップデート

  • 新バージョンのPDBx/mmCIF辞書形式に基づくデータがリリースされました。
  • 今回の更新はバージョン番号が4から5になる大規模なもので、全エントリデータの書き換えが行われる「Remediation」というアップデートに該当します。
  • 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

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