+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-8679 | |||||||||
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タイトル | Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle | |||||||||
マップデータ | Final map of human proteasome RP in the TA3 state corrected with a B-factor of -350 | |||||||||
試料 |
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キーワード | p28 / 26S proteasome / regulatory particle / 19S / gankyrin / HYDROLASE | |||||||||
機能・相同性 | 機能・相同性情報 cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle / cytosolic proteasome complex / proteasome-activating activity ...cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle / cytosolic proteasome complex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / negative regulation of programmed cell death / positive regulation of cyclin-dependent protein serine/threonine kinase activity / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / intermediate filament cytoskeleton / Somitogenesis / negative regulation of NF-kappaB transcription factor activity / negative regulation of MAPK cascade / regulation of protein catabolic process / negative regulation of release of cytochrome c from mitochondria / proteasome storage granule / negative regulation of DNA damage response, signal transduction by p53 class mediator / transcription factor binding / blastocyst development / general transcription initiation factor binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / enzyme regulator activity / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / ERAD pathway / inclusion body / cytoskeletal protein binding / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / positive regulation of protein ubiquitination / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / protein localization to plasma membrane / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / CDK-mediated phosphorylation and removal of Cdc6 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / SCF(Skp2)-mediated degradation of p27/p21 / Degradation of AXIN / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / Vif-mediated degradation of APOBEC3G / Autodegradation of the E3 ubiquitin ligase COP1 / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / P-body / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / Orc1 removal from chromatin / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CLEC7A (Dectin-1) signaling / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / cytoplasmic ribonucleoprotein granule / Regulation of RAS by GAPs / osteoblast differentiation / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / The role of GTSE1 in G2/M progression after G2 checkpoint / UCH proteinases / KEAP1-NFE2L2 pathway / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / positive regulation of cell growth / protein-macromolecule adaptor activity / ER-Phagosome pathway / cytoplasmic vesicle / DNA-binding transcription factor binding / ubiquitin-dependent protein catabolic process 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 7.3 Å | |||||||||
データ登録者 | Lu Y / Wu J | |||||||||
引用 | ジャーナル: Mol Cell / 年: 2017 タイトル: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle. 著者: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao / 要旨: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly. | |||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_8679.map.gz | 81.8 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-8679-v30.xml emd-8679.xml | 20.9 KB 20.9 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_8679.png | 67.8 KB | ||
Filedesc metadata | emd-8679.cif.gz | 6.6 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-8679 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8679 | HTTPS FTP |
-関連構造データ
関連構造データ | 5vhnMC 8672C 8674C 8675C 8676C 8677C 8678C 8680C 8681C 8682C 8683C 8684C 5vgzC 5vhfC 5vhhC 5vhiC 5vhjC 5vhmC 5vhoC 5vhpC 5vhqC 5vhrC 5vhsC C: 同じ文献を引用 (文献) M: このマップから作成された原子モデル |
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類似構造データ | |
電子顕微鏡画像生データ | EMPIAR-10091 (タイトル: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Data size: 70.0 Data #1: Classified single-particle datasets for multiple conformations of p28-bound human regulatory complex [picked particles - multiframe - processed]) |
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_8679.map.gz / 形式: CCP4 / 大きさ: 178 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Final map of human proteasome RP in the TA3 state corrected with a B-factor of -350 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-試料の構成要素
-全体 : Proteasome regulatory particle
全体 | 名称: Proteasome regulatory particle |
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要素 |
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-超分子 #1: Proteasome regulatory particle
超分子 | 名称: Proteasome regulatory particle / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: 26S proteasome non-ATPase regulatory subunit 10
分子 | 名称: 26S proteasome non-ATPase regulatory subunit 10 / タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 24.14249 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE ...文字列: CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE GNTPLHLACD EERVEEAKLL VSQGASIYIE NKEEKTPLQV AKGGLGLILK RMVEG UniProtKB: 26S proteasome non-ATPase regulatory subunit 10 |
-分子 #2: 26S proteasome regulatory subunit 7
分子 | 名称: 26S proteasome regulatory subunit 7 / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 29.746465 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: PTVTMMQVEE KPDVTYSDVG GCKEQIEKLR EVVETPLLHP ERFVNLGIEP PKGVLLFGPP GTGKTLCARA VANRTDACFI RVIGSELVQ KYVGEGARMV RELFEMARTK KACLIFFDEI DAIGGARFDD GAGGDNEVQR TMLELINQLD GFDPRGNIKV L MATNRPDT ...文字列: PTVTMMQVEE KPDVTYSDVG GCKEQIEKLR EVVETPLLHP ERFVNLGIEP PKGVLLFGPP GTGKTLCARA VANRTDACFI RVIGSELVQ KYVGEGARMV RELFEMARTK KACLIFFDEI DAIGGARFDD GAGGDNEVQR TMLELINQLD GFDPRGNIKV L MATNRPDT LDPALMRPGR LDRKIEFSLP DLEGRTHIFK IHARSMSVER DIRFELLARL CPNSTGAEIR SVCTEAGMFA IR ARRKIAT EKDFLEAVNK VIKSYAKFS UniProtKB: 26S proteasome regulatory subunit 7 |
-分子 #3: 26S proteasome regulatory subunit 4
分子 | 名称: 26S proteasome regulatory subunit 4 / タイプ: protein_or_peptide / ID: 3 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 29.901344 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ...文字列: TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ETLDPALIRP GRIDRKIEFP LPDEKTKKRI FQIHTSRMTL ADDVTLDDLI MAKDDLSGAD IKAICTEAGL MA LRERRMK VTNEDFKKSK ENVLYKKQE UniProtKB: 26S proteasome regulatory subunit 4 |
-分子 #4: 26S proteasome regulatory subunit 6B
分子 | 名称: 26S proteasome regulatory subunit 6B / タイプ: protein_or_peptide / ID: 4 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 29.497975 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN ...文字列: PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN RADTLDPALL RPGRLDRKIE FPLPDRRQKR LIFSTITSKM NLSEEVDLED YVARPDKISG ADINSICQES GM LAVRENR YIVLAKDFEK AYKTV UniProtKB: 26S proteasome regulatory subunit 6B |
-分子 #5: 26S proteasome regulatory subunit 10B
分子 | 名称: 26S proteasome regulatory subunit 10B / タイプ: protein_or_peptide / ID: 5 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 30.933523 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: VDPLVYNMSH EDPGNVSYSE IGGLSEQIRE LREVIELPLT NPELFQRVGI IPPKGCLLYG PPGTGKTLLA RAVASQLDCN FLKVVSSSI VDKYIGESAR LIREMFNYAR DHQPCIIFMD EIDAIGGRRF SEGTSADREI QRTLMELLNQ MDGFDTLHRV K MIMATNRP ...文字列: VDPLVYNMSH EDPGNVSYSE IGGLSEQIRE LREVIELPLT NPELFQRVGI IPPKGCLLYG PPGTGKTLLA RAVASQLDCN FLKVVSSSI VDKYIGESAR LIREMFNYAR DHQPCIIFMD EIDAIGGRRF SEGTSADREI QRTLMELLNQ MDGFDTLHRV K MIMATNRP DTLDPALLRP GRLDRKIHID LPNEQARLDI LKIHAGPITK HGEIDYEAIV KLSDGFNGAD LRNVCTEAGM FA IRADHDF VVQEDFMKAV RKVADSKKLE SKLDYKPV UniProtKB: 26S proteasome regulatory subunit 10B |
-分子 #6: 26S proteasome regulatory subunit 6A
分子 | 名称: 26S proteasome regulatory subunit 6A / タイプ: protein_or_peptide / ID: 6 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 29.773246 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN ...文字列: TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN RVDILDPALL RSGRLDRKIE FPMPNEEARA RIMQIHSRKM NVSPDVNYEE LARCTDDFNG AQCKAVCVEA GM IALRRGA TELTHEDYME GILEVQAKKK UniProtKB: 26S proteasome regulatory subunit 6A |
-分子 #7: 26S proteasome regulatory subunit 8
分子 | 名称: 26S proteasome regulatory subunit 8 / タイプ: protein_or_peptide / ID: 7 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 29.501363 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR ...文字列: KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR IDILDSALLR PGRIDRKIEF PPPNEEARLD ILKIHSRKMN LTRGINLRKI AELMPGASGA EVKGVCTEAG MY ALRERRV HVTQEDFEMA VAKVMQKDS UniProtKB: 26S proteasome regulatory subunit 8 |
-分子 #8: 26S proteasome non-ATPase regulatory subunit 2
分子 | 名称: 26S proteasome non-ATPase regulatory subunit 2 / タイプ: protein_or_peptide / ID: 8 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 93.790188 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL ...文字列: RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL DDAEKVQREP LLTLVKEIVP YNMAHNAEHE ACDLLMEIEQ VDMLEKDIDE NAYAKVCLYL TSCVNYVPEP EN SALLRCA LGVFRKFSRF PEALRLALML NDMELVEDIF TSCKDVVVQK QMAFMLGRHG VFLELSEDVE EYEDLTEIMS NVQ LNSNFL ALARELDIME PKVPDDIYKT HLENNRFGGS GSQVDSARMN LASSFVNGFV NAAFGQDKLL TDDGNKWLYK NKDH GMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGL GLAY AGSNREDVLT LLLPVMGDSK SSMEVAGVTA LACGMIAVGS CNGDVTSTIL QTIMEKSETE LKDTYARWLP LGLGLN HLG KGEAIEAILA ALEVVSEPFR SFANTLVDVC AYAGSGNVLK VQQLLHICSE HFDSKEKEED KDKKEKKDKD KKEAPAD MG AHQGVAVLGI ALIAMGEEIG AEMALRTFGH LLRYGEPTLR RAVPLALALI SVSNPRLNIL DTLSKFSHDA DPEVSYNS I FAMGMVGSGT NNARLAAMLR QLAQYHAKDP NNLFMVRLAQ GLTHLGKGTL TLCPYHSDRQ LMSQVAVAGL LTVLVSFLD VRNIILGKSH YVLYGLVAAM QPRMLVTFDE ELRPLPVSVR VGQAVDVV UniProtKB: 26S proteasome non-ATPase regulatory subunit 2 |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.5 |
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凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TECNAI ARCTICA |
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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
実験機器 | モデル: Talos Arctica / 画像提供: FEI Company |
-画像解析
初期モデル | モデルのタイプ: INSILICO MODEL |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 7.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 21031 |
初期 角度割当 | タイプ: ANGULAR RECONSTITUTION |
最終 角度割当 | タイプ: PROJECTION MATCHING |