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- EMDB-12932: Mouse RNF213, with mixed nucleotides bound -

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Basic information

Entry
Database: EMDB / ID: EMD-12932
TitleMouse RNF213, with mixed nucleotides bound
Map datafull non-sharpened map
Sample
  • Complex: RNF213 incubated with ATPgS
    • Protein or peptide: E3 ubiquitin-protein ligase RNF213
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Keywordsnucleotide / AAA / RNF213 / E3 ligase / SIGNALING PROTEIN
Function / homology
Function and homology information


lipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / lipid droplet formation / xenophagy / Transferases; Acyltransferases; Aminoacyltransferases / Antigen processing: Ubiquitination & Proteasome degradation / sprouting angiogenesis / immune system process / regulation of lipid metabolic process / protein K63-linked ubiquitination ...lipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / lipid droplet formation / xenophagy / Transferases; Acyltransferases; Aminoacyltransferases / Antigen processing: Ubiquitination & Proteasome degradation / sprouting angiogenesis / immune system process / regulation of lipid metabolic process / protein K63-linked ubiquitination / protein autoubiquitination / lipid droplet / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / RING-type E3 ubiquitin transferase / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / ubiquitin-dependent protein catabolic process / angiogenesis / defense response to bacterium / protein ubiquitination / nucleolus / ATP hydrolysis activity / ATP binding / metal ion binding / cytosol / cytoplasm
Similarity search - Function
E3 ubiquitin-protein ligase RNF213 / Zinc finger, RZ-type / RZ type zinc finger domain / Zinc finger RZ-type profile. / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. ...E3 ubiquitin-protein ligase RNF213 / Zinc finger, RZ-type / RZ type zinc finger domain / Zinc finger RZ-type profile. / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RNF213
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsAhel J / Clausen T
Funding support Austria, United Kingdom, 4 items
OrganizationGrant numberCountry
European Research Council (ERC)694978 Austria
Austrian Research Promotion Agency852936 Austria
Medical Research Council (MRC, United Kingdom)MC_UU_12016/8 United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BB/ P003982/1 United Kingdom
CitationJournal: To Be Published
Title: E3 ubiquitin ligase RNF213 employs a non-canonical zinc finger active site and is allosterically regulated by ATP
Authors: Ahel J / Fletcher AJ / Grabarczyk D / Roitinger E / Deszcz L / Lehner A / Virdee S / Clausen T
History
DepositionMay 11, 2021-
Header (metadata) releaseJun 1, 2022-
Map releaseJun 1, 2022-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_12932.png

Downloads & links

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Map

FileDownload / File: emd_12932.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfull non-sharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 352 pix.
= 370.656 Å		1.05 Å/pix.
x 352 pix.
= 370.656 Å		1.05 Å/pix.
x 352 pix.
= 370.656 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.053 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.005
Minimum - Maximum-0.009532791 - 0.033896964
Average (Standard dev.)0.0000075062817 (±0.0011747222)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 370.656 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_12932_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Mask #2

Fileemd_12932_msk_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Additional map: full sharpened map

Fileemd_12932_additional_1.map
Annotationfull sharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: sharpened focused map, focused on AAA core

Fileemd_12932_additional_2.map
Annotationsharpened focused map, focused on AAA core
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: non-sharpened focused map, focused on AAA core

Fileemd_12932_additional_3.map
Annotationnon-sharpened focused map, focused on AAA core
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: non-sharpened focused half map 1, focused on AAA cpre

Fileemd_12932_additional_4.map
Annotationnon-sharpened focused half map 1, focused on AAA cpre
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: non-sharpened focused half map 2, focused on AAA cpre

Fileemd_12932_additional_5.map
Annotationnon-sharpened focused half map 2, focused on AAA cpre
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: full non-sharpened map, half volume 2

Fileemd_12932_half_map_1.map
Annotationfull non-sharpened map, half volume 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: full non-sharpened map, half volume 1

Fileemd_12932_half_map_2.map
Annotationfull non-sharpened map, half volume 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : RNF213 incubated with ATPgS

EntireName: RNF213 incubated with ATPgS
Components
  • Complex: RNF213 incubated with ATPgS
    • Protein or peptide: E3 ubiquitin-protein ligase RNF213
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER

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Supramolecule #1: RNF213 incubated with ATPgS

SupramoleculeName: RNF213 incubated with ATPgS / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 580 KDa

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Macromolecule #1: E3 ubiquitin-protein ligase RNF213

MacromoleculeName: E3 ubiquitin-protein ligase RNF213 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 552.623375 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MASWSHPQFE KGSTSAFNPR DTVTVYFHAI VSRHFGFNPE EHKVYVRGGE GLGQKGWTDA CEMYCTQDLH DLGSLVEGKM DIPRQSLDK PIPYKYVIHR GGSSKDTVEY EFIYEQAQKK GEHVNRCLRV VSTSLGNGDW HQYDDIICMR STGFFQQAKN R ILDSTRKE ...String:
MASWSHPQFE KGSTSAFNPR DTVTVYFHAI VSRHFGFNPE EHKVYVRGGE GLGQKGWTDA CEMYCTQDLH DLGSLVEGKM DIPRQSLDK PIPYKYVIHR GGSSKDTVEY EFIYEQAQKK GEHVNRCLRV VSTSLGNGDW HQYDDIICMR STGFFQQAKN R ILDSTRKE LLKGKKQAAV VMLDRIFSVL QPWSDINLQS FMTQFLQFYS VVREPMIHDG RARKWTSLQY EEKEVWTNLW EH VKKQMAP FLEGKSGESL PADCPVRSKL TLGLSILFMV EAAEFTVPKK DLDSLCYLLI PSAGSPEALH SDLSPVLRIR QRW RIYLTN LCLRCIDERC DRWLGILPLL HTCMQKSPPK KNSKSQPEDT WAGLEGISFS EFRDKAPTRS QPLQFMQSKM ALLR VDEYL FRSWLSVVPL ESLSSYLENS IDYLSDVPVR VLDCLQGISY RLPGLRKISN QNMKKDVENV FKMLMHLVDI YQHRI FGEN LLQIYLTECL TLHETVCNIT ANHQFFEIPA LSAELICKLL ELSPPGHTDE GLPEKSYEDL VTSTLQEALA TTRNWL RSL FKSRMLSISS AYVRLTYSEE MAVWRRLVEI GFPEKHGWKG SLLGDMEGRL KQEPPRLQIS FFCSSQCRDG GLHDSVS RS FEKCVIEAVS SACQSQTSVL EGLSCQDLQK FGTLLSAVIT KSWPVHNGEP VFDVDEIFKY LLKWPDVRQL FELCGTNE K IIDNITEEGR QLMATAESVF QKVAGELENG TIVVGQLELI LEHQSQFLDI WNLNRRRLPS QEKACDVRSL LKRRRDDLL FLKQEKRYVE SLLRQLGRVK HLVQVDFGNI EIIHSQDLSN KKLNEAVIKL PNSSSYKRET HYCLSPDIRE MASKLDSLKD SHIFQDFWQ ETAESLNTLD KDPRELKVSL PEVLEYLYNP CYDNFYTLYE NLKSGKITFA EVDAIFKDFV DKYDELKNDL K FMCTMNPQ DQKGWISERV GQIKEYHTLH QAVSSAKVIL QVRRALGVTG DFSVLNPLLN FADSFEDFGN EKLDQISPQF IK AKQLLQD ISEPRQRCLE ELARQTELVA WLHKALEDIN ELKVFVDLAS ISAGENDIDV DRVACFHDAV QGYASLLYKM DER TNFSDF MNHLQELWRA LDNDQHLPDK LKDSARNLEW LKTVKESHGS VELSSLSLAT AINSRGVYVI EAPKDGQKIS PDTV LRLLL PDGHGYPEAL RTYSTEELKE LLNKLMLMSG KKDHNSNTEV EKFSEVFSNM QRLVHVFIKL HCAGNMLFRT WTAKV YCCP DGGIFMNFGL ELLSQLTEKG DVIQLLGALC RQMEDFLDNW KTVVAQKRAE HFYLNFYTAE QLVYLSSELR KPRPSE AAL MMLSFIKGKC TVQDLVQATS ACESKADRYC LREVMKKLPQ QLLSEPSLMG KLQVIMMQSL VYMSAFLPHC LDLDALG RC LAHLATMGGT PVERPLPKGL QAGQPNLILC GHSEVLPAAL AIYMQAPRQP LPTFDEVLLC TPATTIEEVE LLLRRCLT S GSQGHKVYSL LFADQLSYEV GCQAEEFFQS LCTRAHREDY QLVILCDAAR EHCYIPSTFS QYKVPLVPQA PLPNIQAYL QSHYQVPKRL LSAATVFRDG LCVGIVTSER AGVGKSLYVN TLHTKLKAKL RDETVPLKII RLTEPHLDEN QVLSALLPFL KEKYQKMPV IFHIDISTSV QTGIPIFLFK LLILQYLMDI NGKIWRRSPG HLYLVEIPQG LSVQPKRSSK LNARAPLFKF L DLFPKVTC RPPKEVIDME LTPERSHTDP AMDPVEFCSE AFQRPYQYLK RFHQQQNLDT FQYEKGSVEG SPEECLQHFL IY CGLINPS WSELRNFAWF LNCQLKDCEA SIFCKSAFTG DTLRGFKNFV VTFMILMARD FATPTLHTSD QSPGRQSVTI GEV VEEDLA PFSLRKRWES EPHPYVFFNG DHMTMTFIGF HLETNNNGYV DAINPSNGKV IKKDVMTKEL FDGLRLQRVP FNID FDNLP RYEKLERLCL ALGIEWPIDP DETYELTTDN MLKILAIEMR FRCGIPVIIM GETGCGKTRL IKFLSDLKRG SVEAE TMKL VKVHGGTTPS MIYSKVKEAE RTAFSNKAQH KLDTILFFDE ANTTEAVSCI KEILCDRTVD GEHLHEDSGL HIIAAC NPY RKHSQEMILR LESAGLGYRV SAEETADRLG SIPLRQLVYR VHALPPSLIP LVWDFGQLND SAEKLYIQQI VQRLVDS VS VNPSETCVIA DVLSASQMFM RKRENECGFV SLRDVERCVK VFRWFHDHSD MLLKELDKFL HESSDSTHTF ERDPVLWS L VMAIGVCYHA SLEEKASYRT AIARCFPKPY NSSRAILDEV THVQDLFLRG APIRTNIARN LALKENVFMM VICIELKIP LFLVGKPGSS KSLAKIIVAD AMQGQAAFSE LFRCLKQVHL VSFQCSPHST PQGIISTFKQ CARFQQGKDL GQYVSVVVLD EVGLAEDSP KMPLKTLHPL LEDGCIEDDP APYKKVGFVG ISNWALDPAK MNRGIFVSRG SPNEKELIES AEGICSSDRL V QDKIRGYF APFAKAYETV CQKQDKEFFG LRDYYSLIKM VFAKAKASKR GLSPQDITHA VLRNFSGKDN IQALSIFTAS LP EARYKEE VSTVELIKQN IYPGPQASSR GLDGAESRYL LVLTRNYVAL QILQQTFFEG QQPEIIFGSS FPQDQEYTQI CRN INRVKI CMETGKMVVL LNLQNLYESL YDALNQYYVY LGGQKYVDLG LGTHRVKCRV HTAFRLIVIE EKDVVYKQFP VPLI NRLEK HYLDMNTVLQ PWQKSIVQEL QQWAHEFADV KADQFIARHK YSPADVFIGY HSDACASVVL QAVERQGCRD LTEEL YRKV SEEARSILLD CATPDAVVRL SGSSLGSFTA KQLSQEYYYA QQHNSFVDFL QAHLRMTHHE CRAVFTEITT FSRLLT GND CDVLASELRG LASKPVVLSL QQYDTEYSFL KDVRSWLTNP GKRKVLVIQA DFDDGTRSAQ LVASAKYTAI NEINKTQ GT KDFVFVYFVT KLSRMGSGTS YVGFHGGLWR SVHIDDLRRS TIMASDVTKL QNVTISQLFK PEDKPEQEEM EIETSQSK E LAEEQMEVED SEEMKKASDP RSCDCSQFLD TTRLVQSCVQ GAVGMLRDQN ESCARNMRRV TILLDLLNED NTRNASFLR ESKMRLHVLL NKQEENQVRS LKEWVTREAA NQDALQEAGT FRHTLWKRVQ DVVTPILASM IAHIDRDGNL ELLAQPDSPA WVQDLWMFI YSDIKFLNIS LVLNNTRSNS EMSFILVQSH MNLLKDAYNA VPFSWRIRDY LEELWVQAQY ITDTEGLSKK F VEIFQKTP LGVFLAQFPV AQQQKLLQSY LKDFLLLTMK VSSREELMFL QMALWSCLRE LQEASGTPDE TYKFPLSLPW VH LAFQHFR TRLQNFSRIL TIHPQVLSSL SQAAEKHSLA GCEMTLDAFA AMACAEMLKG DLLKPSPKAW LQLVKNLSTP LEL VCSEGY LCDSGSMTRS VIQEVRALWN RIFSIALFVE HVLLGTESHI PELSPLVTTY VSLLDKCLEE DSNLKTCRPF VAVM TTLCD CKDKASKKFS RFGIQPCFIC HGDAQDPVCL PCDHVYCLRC IQTWLIPGQM MCPYCLTDLP DKFSPTVSQD HRKAI EKHA QFRHMCNSFF VDLVSTMCFK DNTPPEKSVI DTLLSLLFVQ KELLRDASQK HREHTKSLSP FDDVVDQTPV IRSVLL KLL LKYSFHEVKD YIQNYLTQLE KKAFLTEDKT ELYLLFISCL EDSVHQKTSA GCRNLEQVLR EEGHFLRTYS PGLQGQE PV RIASVEYLQE VARVRLCLDL AADFLSELQE GSELAEDKRR FLKHVEEFCT RVNNDWHRVY LVRKLSSQRG MEFVQSFS K QGHPCQWVFP RKVIAQQKDH VSLMDRYLVH GNEYKAVRDA TAKAVLECKT LDIGNALMAC RSPKPQQTAY LLLALYTEV AALYRSPNGS LHPEAKQLEA VNKFIKESKI LSDPNIRCFA RSLVDNTLPL LKIRSANSIL KGTVTEMAVH VATILLCGHN QILKPLRNL AFYPVNMANA FLPTMPEDLL VHARTWRGLE NVTWYTCPRG HPCSVGECGR PMQESTCLDC GLPVGGLNHT P HEGFSAIR NNEDRTQTGH VLGSPQSSGV AEVSDRGQSP VVFILTRLLT HLAMLVGATH NPQALTVIIK PWVQDPQGFL QQ HIQRDLE QLTKMLGRSA DETIHVVHLI LSSLLRVQSH GVLNFNAELS TKGCRNNWEK HFETLLLREL KHLDKNLPAI NAL ISQDER ISSNPVTKII YGDPATFLPH LPQKSIIHCS KIWSCRRKIT VEYLQHIVEQ KNGKETVPVL WHFLQKEAEL RLVK FLPEI LALQRDLVKQ FQNVSRVEYS SIRGFIHSHS SDGLRKLLHD RITIFLSTWN ALRRSLETNG EIKLPKDYCC SDLDL DAEF EVILPRRQGL GLCGTALVSY LISLHNNMVY TVQKFSNEDN SYSVDISEVA DLHVISYEVE RDLNPLILSN CQYQVQ QGG ETSQEFDLEK IQRQISSRFL QGKPRLTLKG IPTLVYRRDW NYEHLFMDIK NKMAQSSLPN LAISTISGQL QSYSDAC EA LSIIEITLGF LSTAGGDPGM DLNVYIEEVL RMCDQTAQVL KAFSRCQLRH IIALWQFLSA HKSEQRLRLN KELFREID V QYKEELSTQH QRLLGTFLNE AGLDAFLLEL HEMIVLKLKG PRAANSFNPN WSLKDTLVSY METKDSDILS EVESQFPEE ILMSSCISVW KIAATRKWDR QSRGGGHHHH HHHHHH

UniProtKB: E3 ubiquitin-protein ligase RNF213

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Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #6: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 6 / Number of copies: 1 / Formula: AGS
Molecular weightTheoretical: 523.247 Da
Chemical component information

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.2
Component:
ConcentrationFormula
200.0 mMKCl
25.0 mMHEPES
0.25 mMTCEP
GridModel: UltrAuFoil R2/2 / Material: GOLD / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Instrument: LEICA PLUNGER

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Electron microscopy

MicroscopeTFS KRIOS
Image recording#0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / #0 - Number grids imaged: 1 / #0 - Number real images: 3055 / #0 - Average exposure time: 2.0 sec. / #0 - Average electron dose: 45.0 e/Å2 / #0 - Details: grid tilted 30 degrees 1 image per "hole" / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K2 QUANTUM (4k x 4k) / #1 - Detector mode: COUNTING / #1 - Digitization - Dimensions - Width: 3838 pixel / #1 - Digitization - Dimensions - Height: 3710 pixel / #1 - Digitization - Frames/image: 1-40 / #1 - Number grids imaged: 1 / #1 - Number real images: 5950 / #1 - Average exposure time: 10.0 sec. / #1 - Average electron dose: 40.5 e/Å2 / #1 - Details: non-tilted dataset 10 images per "hole"
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: -2.5 µm / Nominal defocus min: -1.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Image recording ID1
Startup modelType of model: EMDB MAP
EMDB ID:

10429

Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 336000
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6tax


Chain - Chain ID: A / Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7oim:
Mouse RNF213, with mixed nucleotides bound

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