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- EMDB-4466: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, ... -

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Basic information

Entry
Database: EMDB / ID: EMD-4466
TitleCryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
Map dataunsharpened map
Sample
  • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
    • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
      • Protein or peptide: x 15 types
    • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
      • Protein or peptide: x 1 types
Function / homology
Function and homology information


metaphase/anaphase transition of cell cycle / metaphase/anaphase transition of meiosis I / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of anaphase-promoting complex-dependent catabolic process / regulation of mitotic cell cycle spindle assembly checkpoint / regulation of meiotic nuclear division / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / Inactivation of APC/C via direct inhibition of the APC/C complex ...metaphase/anaphase transition of cell cycle / metaphase/anaphase transition of meiosis I / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of anaphase-promoting complex-dependent catabolic process / regulation of mitotic cell cycle spindle assembly checkpoint / regulation of meiotic nuclear division / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / Phosphorylation of Emi1 / Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes / cyclin A2-CDK1 complex / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / cell cycle G1/S phase transition / anaphase-promoting complex-dependent catabolic process / regulation of meiotic cell cycle / positive regulation of mitotic metaphase/anaphase transition / cellular response to luteinizing hormone stimulus / metaphase/anaphase transition of mitotic cell cycle / regulation of exit from mitosis / positive regulation of synaptic plasticity / Phosphorylation of the APC/C / anaphase-promoting complex binding / mitotic cell cycle phase transition / ubiquitin ligase activator activity / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / positive regulation of ubiquitin protein ligase activity / protein K11-linked ubiquitination / cellular response to leptin stimulus / male pronucleus / enzyme-substrate adaptor activity / female pronucleus / regulation of mitotic metaphase/anaphase transition / response to glucagon / cellular response to cocaine / positive regulation of dendrite morphogenesis / ubiquitin-ubiquitin ligase activity / cyclin-dependent protein serine/threonine kinase regulator activity / cellular response to insulin-like growth factor stimulus / mitotic sister chromatid cohesion / positive regulation of DNA biosynthetic process / mitotic metaphase chromosome alignment / cochlea development / mitotic spindle assembly checkpoint signaling / cellular response to platelet-derived growth factor stimulus / cyclin A2-CDK2 complex / G2 Phase / p53-Dependent G1 DNA Damage Response / regulation of mitotic cell cycle / cullin family protein binding / regulation of DNA replication / Regulation of APC/C activators between G1/S and early anaphase / Telomere Extension By Telomerase / mitotic spindle assembly / G0 and Early G1 / Transcriptional Regulation by VENTX / cyclin-dependent protein kinase holoenzyme complex / cellular response to nitric oxide / positive regulation of axon extension / animal organ regeneration / heterochromatin / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Cyclin A:Cdk2-associated events at S phase entry / Resolution of Sister Chromatid Cohesion / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / nuclear periphery / post-translational protein modification / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / cellular response to estradiol stimulus / Assembly of the pre-replicative complex / RHO GTPases Activate Formins / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / brain development / G1/S transition of mitotic cell cycle / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / DNA Damage/Telomere Stress Induced Senescence / spindle / mitotic spindle / kinetochore / CDK-mediated phosphorylation and removal of Cdc6 / SCF(Skp2)-mediated degradation of p27/p21 / spindle pole / Orc1 removal from chromatin / ubiquitin-protein transferase activity / Separation of Sister Chromatids / ubiquitin protein ligase activity / microtubule cytoskeleton / positive regulation of fibroblast proliferation / G2/M transition of mitotic cell cycle / Antigen processing: Ubiquitination & Proteasome degradation
Similarity search - Function
Anaphase-promoting complex subunit 15 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 4, metazoa / : / Anaphase-promoting complex subunit 5, N-terminal domain / Anaphase-promoting complex subunit 1, C-terminal / Anaphase-promoting complex subunit 1, middle domain / : / : ...Anaphase-promoting complex subunit 15 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 4, metazoa / : / Anaphase-promoting complex subunit 5, N-terminal domain / Anaphase-promoting complex subunit 1, C-terminal / Anaphase-promoting complex subunit 1, middle domain / : / : / Anaphase-promoting complex subunit 1 WD40 beta-propeller domain / Anaphase-promoting complex sub unit 1 C-terminal domain / Anaphase-promoting complex subunit 1 middle domain / APC1 beta sandwich domain / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex, subunit 16 / Cdc23 / Apc13 / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 4 long domain / Anaphase promoting complex subunit 8 / Cdc23 / Apc13p protein / Anaphase-promoting complex, cyclosome, subunit 4 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 5 domain / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit APC10/Doc1 / Anaphase-promoting complex, subunit CDC26 / Anaphase-promoting complex APC subunit CDC26 / Anaphase-promoting complex subunit 11, RING-H2 finger / Anaphase-promoting complex subunit 11 RING-H2 finger / Anaphase-promoting complex subunit 2, C-terminal / Anaphase-promoting complex subunit 2 / Anaphase promoting complex (APC) subunit 2 / Anaphase promoting complex (APC) subunit 2 / Anaphase-promoting complex, cyclosome, subunit 3 / APC10/DOC domain / Anaphase-promoting complex, subunit 10 (APC10) / DOC domain profile. / Anaphase-promoting complex, subunit 10 (APC10) / TPR repeat / Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Tetratricopeptide repeat / Cyclin, C-terminal domain / Cyclin_C / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Tetratricopeptide repeat / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / Tetratricopeptide repeat / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Galactose-binding-like domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Armadillo-like helical / Tetratricopeptide-like helical domain superfamily / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
Cyclin-A2 / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 11 ...Cyclin-A2 / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 11 / Cell division cycle protein 23 homolog / Anaphase-promoting complex subunit 7 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 2 / Anaphase-promoting complex subunit 10
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsZhang S / Barford D
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)MC_UP_1021/6 United Kingdom
Cancer Research UKC576/A14109 United Kingdom
CitationJournal: Nat Commun / Year: 2019
Title: Cyclin A2 degradation during the spindle assembly checkpoint requires multiple binding modes to the APC/C.
Authors: Suyang Zhang / Thomas Tischer / David Barford /
Abstract: The anaphase-promoting complex/cyclosome (APC/C) orchestrates cell cycle progression by controlling the temporal degradation of specific cell cycle regulators. Although cyclin A2 and cyclin B1 are ...The anaphase-promoting complex/cyclosome (APC/C) orchestrates cell cycle progression by controlling the temporal degradation of specific cell cycle regulators. Although cyclin A2 and cyclin B1 are both targeted for degradation by the APC/C, during the spindle assembly checkpoint (SAC), the mitotic checkpoint complex (MCC) represses APC/C's activity towards cyclin B1, but not cyclin A2. Through structural, biochemical and in vivo analysis, we identify a non-canonical D box (D2) that is critical for cyclin A2 ubiquitination in vitro and degradation in vivo. During the SAC, cyclin A2 is ubiquitinated by the repressed APC/C-MCC, mediated by the cooperative engagement of its KEN and D2 boxes, ABBA motif, and the cofactor Cks. Once the SAC is satisfied, cyclin A2 binds APC/C-Cdc20 through two mutually exclusive binding modes, resulting in differential ubiquitination efficiency. Our findings reveal that a single substrate can engage an E3 ligase through multiple binding modes, affecting its degradation timing and efficiency.
History
DepositionDec 11, 2018-
Header (metadata) releaseSep 11, 2019-
Map releaseSep 11, 2019-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.008
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.008
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6q6h
  • Surface level: 0.008
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4466.png

Downloads & links

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Map

FileDownload / File: emd_4466.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationunsharpened map
Voxel sizeX=Y=Z: 1.047 Å
Density
Contour LevelBy AUTHOR: 0.008 / Movie #1: 0.008
Minimum - Maximum-0.015616445 - 0.04164528
Average (Standard dev.)-0.00000365593 (±0.0015757986)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 418.80002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0471.0471.047
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z418.800418.800418.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0160.042-0.000

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Supplemental data

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Additional map: sharpened map with B factor -30, lowpass filtered to 4A

Fileemd_4466_additional.map
Annotationsharpened map with B factor -30, lowpass filtered to 4A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: halfmap1

Fileemd_4466_half_map_1.map
Annotationhalfmap1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: halfmap2

Fileemd_4466_half_map_2.map
Annotationhalfmap2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, ...

EntireName: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
Components
  • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
    • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
      • Protein or peptide: Anaphase-promoting complex subunit 10
      • Protein or peptide: Anaphase-promoting complex subunit 15
      • Protein or peptide: Apc1
      • Protein or peptide: Anaphase-promoting complex subunit 2
      • Protein or peptide: Anaphase-promoting complex subunit 4
      • Protein or peptide: Anaphase-promoting complex subunit 5
      • Protein or peptide: Cell division cycle protein 16 homologCell cycle
      • Protein or peptide: Anaphase-promoting complex subunit 11
      • Protein or peptide: Anaphase-promoting complex subunit CDC26
      • Protein or peptide: Anaphase-promoting complex subunit 13
      • Protein or peptide: Anaphase-promoting complex subunit 16
      • Protein or peptide: Cell division cycle protein 27 homologCell cycle
      • Protein or peptide: Anaphase-promoting complex subunit 7
      • Protein or peptide: Cell division cycle protein 23 homologCell cycle
      • Protein or peptide: Cell division cycle protein 20 homologCell cycle
    • Complex: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
      • Protein or peptide: Cyclin-A2

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Supramolecule #1: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, ...

SupramoleculeName: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Molecular weightTheoretical: 1.3 MDa

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Supramolecule #2: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, ...

SupramoleculeName: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#15
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: unidentified baculovirus

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Supramolecule #3: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, ...

SupramoleculeName: Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
type: complex / ID: 3 / Parent: 1 / Macromolecule list: #16
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Esacherichia coli (E. coli)

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Macromolecule #1: Anaphase-promoting complex subunit 10

MacromoleculeName: Anaphase-promoting complex subunit 10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.282143 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MTTPNKTPPG ADPKQLERTG TVREIGSQAV WSLSSCKPGF GVDQLRDDNL ETYWQSDGSQ PHLVNIQFRR KTTVKTLCIY ADYKSDESY TPSKISVRVG NNFHNLQEIR QLELVEPSGW IHVPLTDNHK KPTRTFMIQI AVLANHQNGR DTHMRQIKIY T PVEESSIG KFPRCTTIDF MMYRSIR

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Macromolecule #2: Anaphase-promoting complex subunit 15

MacromoleculeName: Anaphase-promoting complex subunit 15 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.286727 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MSTLFPSLFP RVTETLWFNL DRPCVEETEL QQQEQQHQAW LQSIAEKDNN LVPIGKPASE HYDDEEEEDD EDDEDSEEDS EDDEDMQDM DEMNDYNESP DDGEVNEVDM EGNEQDQDQW MI

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Macromolecule #3: Apc1

MacromoleculeName: Apc1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 207.240234 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGEDVDY DEELYVAGNM VIWSKGSKSQ ALAVYKAFTV DSPVQQALWC DFIISQDKSE KAYSSNEVEK CICILQSSCI N MHSIEGKD ...String:
MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGEDVDY DEELYVAGNM VIWSKGSKSQ ALAVYKAFTV DSPVQQALWC DFIISQDKSE KAYSSNEVEK CICILQSSCI N MHSIEGKD YIASLPFQVA NVWPTKYGLL FERSASSHEV PPGSPREPLP TMFSMLHPLD EITPLVCKSG SLFGSSRVQY VV DHAMKIV FLNTDPSIVM TYDAVQNVHS VWTLRRVKSE EENVVLKFSE QGGTPQNVAT SSSLTAHLRL APETEPIVPE LCI DHLWTE TITNIRESNS QASKVFITSD LCGQKFLCFL VESQLQLRCV KFQESNDKTQ LIFGSVTNIP AKDAAPVEKI DTML VLEGS GNLVLYTGVV RVGKVFIPGL PAPSLTMSNT MPRPSTPLDG VSTPKPLSKL LGSLDEVVLL SPVPELRDSS KLHDS LYNE DCTFQQLGTY IHSIRDPVHN RVTLELSNGS MVRITIPEIA TSELVQTCLQ AIKFILPKEI AVQMLVKWYN VHSAPG GPS YHSEWNLFVT CLMNMMGYNT DRLAWTRNFD FEGSLSPVIA PKKARPSETG SDDDWEYLLN SDYHQNVESH LLNRSLC LS PSEASQMKDE DFSQNLSLDS STLLFTHIPA IFFVLHLVYE ELKLNTLMGE GICSLVELLV QLARDLKLGP YVDHYYRD Y PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVS DESSQYLTRI TIAPQKLQVE QEENRFSFRH STSVSSLAER LVVWMTNVGF TLRDLETLPF GIALPIRDAI YHCREQPASD WPEAVCLLI GRQDLSKQAC EGNLPKGKSV LSSDVPSGTE TEEEDDGMND MNHEVMSLIW SEDLRVQDVR RLLQSAHPVR V NVVQYPEL SDHEFIEEKE NRLLQLCQRT MALPVGRGMF TLFSYHPVPT EPLPIPKLNL TGRAPPRNTT VDLNSGNIDV PP NMTSWAS FHNGVAAGLK IAPASQIDSA WIVYNKPKHA ELANEYAGFL MALGLNGHLT KLATLNIHDY LTKGHEMTSI GLL LGVSAA KLGTMDMSIT RLLSIHIPAL LPPTSTELDV PHNVQVAAVV GIGLVYQGTA HRHTAEVLLA EIGRPPGPEM EYCT DRESY SLAAGLALGM VCLGHGSNLI GMSDLNVPEQ LYQYMVGGHR RFQTGMHREK HKSPSYQIKE GDTINVDVTC PGATL ALAM IYLKTNNRSI ADWLRAPDTM YLLDFVKPEF LLLRTLARCL ILWDDILPNS KWVDSNVPQI IRENSISLSE IELPCS EDL NLETLSQAHV YIIAGACLSL GFRFAGSENL SAFNCLHKFA KDFMTYLSAP NASVTGPHNL ETCLSVVLLS LAMVMAG SG NLKVLQLCRF LHMKTGGEMN YGFHLAHHMA LGLLFLGGGR YSLSTSNSSI AALLCALYPH FPAHSTDNRY HLQALRHL Y VLAAEPRLLV PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL SKGTQHLKS ILSKDGVLYV KLRAGQLSYK EDPMGWQSLL AQTVANRNSE ARAFKPETIS AFTSDPALLS FAEYFCKPTV NMGQKQEILD LFSSVLYEC VTQETPEMLP AYIAMDQAIR RLGRREMSET SELWQIKLVL EFFSSRSHQE RLQNHPKRGL FMNSEFLPVV K CTIDNTLD QWLQVGGDMC VHAYLSGQPL EESQLSMLAC FLVYHSVPAP QHLPPIGLEG STSFAELLFK FKQLKMPVRA LL RLAPLLL GNPQPMVM

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Macromolecule #4: Anaphase-promoting complex subunit 2

MacromoleculeName: Anaphase-promoting complex subunit 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.938977 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISP EFWNAISQCE NSADEPQCLL LLLDAFGLLE SRLDPYLRSL ELLEKWTRLG LLMGTGAQGL REEVHTMLRG V LFFSTPRT ...String:
MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISP EFWNAISQCE NSADEPQCLL LLLDAFGLLE SRLDPYLRSL ELLEKWTRLG LLMGTGAQGL REEVHTMLRG V LFFSTPRT FQEMIQRLYG CFLRVYMQSK RKGEGGTDPE LEGELDSRYA RRRYYRLLQS PLCAGCSSDK QQCWCRQALE QF HQLSQVL HRLSLLERVS AEAVTTTLHQ VTRERMEDRC RGEYERSFLR EFHKWIERVV GWLGKVFLQD GPARPASPEA GNT LRRWRC HVQRFFYRIY ASLRIEELFS IVRDFPDSRP AIEDLKYCLE RTDQRQQLLV SLKAALETRL LHPGVNTCDI ITLY ISAIK ALRVLDPSMV ILEVACEPIR RYLRTREDTV RQIVAGLTGD SDGTGDLAVE LSKTDPASLE TGQDSEDDSG EPEDW VPDP VDADPGKSSS KRRSSDIISL LVSIYGSKDL FINEYRSLLA DRLLHQFSFS PEREIRNVEL LKLRFGEAPM HFCEVM LKD MADSRRINAN IREEDEKRPA EEQPPFGVYA VILSSEFWPP FKDEKLEVPE DIRAALEAYC KKYEQLKAMR TLSWKHT LG LVTMDVELAD RTLSVAVTPV QAVILLYFQD QASWTLEELS KAVKMPVALL RRRMSVWLQQ GVLREEPPGT FSVIEEER P QDRDNMVLID SDDESDSGMA SQADQKEEEL LLFWTYIQAM LTNLESLSLD RIYNMLRMFV VTGPALAEID LQELQGYLQ KKVRDQQLVY SAGVYRLPKN CS

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Macromolecule #5: Anaphase-promoting complex subunit 4

MacromoleculeName: Anaphase-promoting complex subunit 4 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 92.219227 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKK IVLCDVEKPE SLHSFSVEAP VSCMHWMEVT VESSVLTSFY NAEDESNLLL PKLPTLPKNY SNTSKIFSEE N SDEIIKLL ...String:
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKK IVLCDVEKPE SLHSFSVEAP VSCMHWMEVT VESSVLTSFY NAEDESNLLL PKLPTLPKNY SNTSKIFSEE N SDEIIKLL GDVRLNILVL GGSSGFIELY AYGMFKIARV TGIAGTCLAL CLSSDLKSLS VVTEVSTNGA SEVSYFQLET NL LYSFLPE VTRMARKFTH ISALLQYINL SLTCMCEAWE EILMQMDSRL TKFVQEKNTT TSVQDEFMHL LLWGKASAEL QTL LMNQLT VKGLKKLGQS IESSYSSIQK LVISHLQSGS ESLLYHLSEL KGMASWKQKY EPLGLDAAGI EEAITAVGSF ILKA NELLQ VIDSSMKNFK AFFRWLYVAM LRMTEDHVLP ELNKMTQKDI TFVAEFLTEH FNEAPDLYNR KGKYFNVERV GQYLK DEDD DLVSPPNTEG NQWYDFLQNS SHLKESPLLF PYYPRKSLHF VKRRMENIID QCLQKPADVI GKSMNQAICI PLYRDT RSE DSTRRLFKFP FLWNNKTSNL HYLLFTILED SLYKMCILRR HTDISQSVSN GLIAIKFGSF TYATTEKVRR SIYSCLD AQ FYDDETVTVV LKDTVGREGR DRLLVQLPLS LVYNSEDSAE YQFTGTYSTR LDEQCSAIPT RTMHFEKHWR LLESMKAQ Y VAGNGFRKVS CVLSSNLRHV RVFEMDIDDE WELDESSDEE EEASNKPVKI KEEVLSESEA ENQQAGAAAL APEIVIKVE KLDPELDS

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Macromolecule #6: Anaphase-promoting complex subunit 5

MacromoleculeName: Anaphase-promoting complex subunit 5 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 85.179766 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQL ANSVQIRIKL MAEGELKDME QFFDDLSDSF SGTEPEVHKT SVVGLFLRHM ILAYSKLSFS QVFKLYTALQ Q YFQNGEKK ...String:
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQL ANSVQIRIKL MAEGELKDME QFFDDLSDSF SGTEPEVHKT SVVGLFLRHM ILAYSKLSFS QVFKLYTALQ Q YFQNGEKK TVEDADMELT SRDEGERKME KEELDVSVRE EEVSCSGPLS QKQAEFFLSQ QASLLKNDET KALTPASLQK EL NNLLKFN PDFAEAHYLS YLNNLRVQDV FSSTHSLLHY FDRLILTGAE SKSNGEEGYG RSLRYAALNL AALHCRFGHY QQA ELALQE AIRIAQESND HVCLQHCLSW LYVLGQKRSD SYVLLEHSVK KAVHFGLPYL ASLGIQSLVQ QRAFAGKTAN KLMD ALKDS DLLHWKHSLS ELIDISIAQK TAIWRLYGRS TMALQQAQML LSMNSLEAVN AGVQQNNTES FAVALCHLAE LHAEQ GCFA AASEVLKHLK ERFPPNSQHA QLWMLCDQKI QFDRAMNDGK YHLADSLVTG ITALNSIEGV YRKAVVLQAQ NQMSEA HKL LQKLLVHCQK LKNTEMVISV LLSVAELYWR SSSPTIALPM LLQALALSKE YRLQYLASET VLNLAFAQLI LGIPEQA LS LLHMAIEPIL ADGAILDKGR AMFLVAKCQV ASAASYDQPK KAEALEAAIE NLNEAKNYFA KVDCKERIRD VVYFQARL Y HTLGKTQERN RCAMLFRQLH QELPSHGVPL INHL

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Macromolecule #7: Cell division cycle protein 16 homolog

MacromoleculeName: Cell division cycle protein 16 homolog / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 71.747516 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQA LDVLDMEEPI NKRLFEKYLK DESGFKDPSS DWEMSQSSIK SSICLLRGKI YDALDNRTLA TYSYKEALKL D VYCFEAFD ...String:
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQA LDVLDMEEPI NKRLFEKYLK DESGFKDPSS DWEMSQSSIK SSICLLRGKI YDALDNRTLA TYSYKEALKL D VYCFEAFD LLTSHHMLTA QEEKELLESL PLSKLCNEEQ ELLRFLFENK LKKYNKPSET VIPESVDGLQ ENLDVVVSLA ER HYYNCDF KMCYKLTSVV MEKDPFHASC LPVHIGTLVE LNKANELFYL SHKLVDLYPS NPVSWFAVGC YYLMVGHKNE HAR RYLSKA TTLEKTYGPA WIAYGHSFAV ESEHDQAMAA YFTAAQLMKG CHLPMLYIGL EYGLTNNSKL AERFFSQALS IAPE DPFVM HEVGVVAFQN GEWKTAEKWF LDALEKIKAI GNEVTVDKWE PLLNNLGHVC RKLKKYAEAL DYHRQALVLI PQNAS TYSA IGYIHSLMGN FENAVDYFHT ALGLRRDDTF SVTMLGHCIE MYIGDSEAYI GADIKDKLKC YDFDVHTMKT LKNIIS PPW DFREFEVEKQ TAEETGLTPL ETSRKTPDSR PSLEETFEIE MNESDMMLET SMSDHST

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Macromolecule #8: Anaphase-promoting complex subunit 11

MacromoleculeName: Anaphase-promoting complex subunit 11 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.854647 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI LKWLHAQQVQ QHCPMCRQEW KFKE

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Macromolecule #9: Anaphase-promoting complex subunit CDC26

MacromoleculeName: Anaphase-promoting complex subunit CDC26 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.793999 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF

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Macromolecule #10: Anaphase-promoting complex subunit 13

MacromoleculeName: Anaphase-promoting complex subunit 13 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.528309 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLNELPEPE QDNGGTTESV KEQEMKWTDL ALQYLHENVP PIGN

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Macromolecule #11: Anaphase-promoting complex subunit 16

MacromoleculeName: Anaphase-promoting complex subunit 16 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.677995 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MAASSSSSSA GGVSGSSVTG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS ERFLCESVFS YQVASTLKQV KHDQQVARME KLAGLVEEL EADEWRFKPI EQLLGFTPSS G

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Macromolecule #12: Cell division cycle protein 27 homolog

MacromoleculeName: Cell division cycle protein 27 homolog / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 91.973125 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGE QILSGGVFNK QKSHDDIVTE FGDSACFTLS LLGHVYCKTD RLAKGSECYQ KSLSLNPFLW SPFESLCEIG E KPDPDQTF ...String:
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGE QILSGGVFNK QKSHDDIVTE FGDSACFTLS LLGHVYCKTD RLAKGSECYQ KSLSLNPFLW SPFESLCEIG E KPDPDQTF KFTSLQNFSN CLPNSCTTQV PNHSLSHRQP ETVLTETPQD TIELNRLNLE SSNSKYSLNT DSSVSYIDSA VI SPDTVPL GTGTSILSKQ VQNKPKTGRS LLGGPAALSP LTPSFGILPL ETPSPGDGSY LQNYTNTPPV IDVPSTGAPS KKS VARIGQ TGTKSVFSQS GNSREVTPIL AQTQSSGPQT STTPQVLSPT ITSPPNALPR RSSRLFTSDS STTKENSKKL KMKF PPKIP NRKTKSKTNK GGITQPNIND SLEITKLDSS IISEGKISTI TPQIQAFNLQ KAAAEGLMSL LREMGKGYLA LCSYN CKEA INILSHLPSH HYNTGWVLCQ IGRAYFELSE YMQAERIFSE VRRIENYRVE GMEIYSTTLW HLQKDVALSV LSKDLT DMD KNSPEAWCAA GNCFSLQREH DIAIKFFQRA IQVDPNYAYA YTLLGHEFVL TEELDKALAC FRNAIRVNPR HYNAWYG LG MIYYKQEKFS LAEMHFQKAL DINPQSSVLL CHIGVVQHAL KKSEKALDTL NKAIVIDPKN PLCKFHRASV LFANEKYK S ALQELEELKQ IVPKESLVYF LIGKVYKKLG QTHLALMNFS WAMDLDPKGA NNQIKEAIDK RYLPDDEEPI TQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF

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Macromolecule #13: Anaphase-promoting complex subunit 7

MacromoleculeName: Anaphase-promoting complex subunit 7 / type: protein_or_peptide / ID: 13 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 66.929367 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL LTMSNNNPEL FSPPQKYQLL VYHADSLFH DKEYRNAVSK YTMALQQKKA LSKTSKVRPS TGNSASTPQS QCLPSEIEVK YKMAECYTML KQDKDAIAIL D GIPSRQRT ...String:
MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL LTMSNNNPEL FSPPQKYQLL VYHADSLFH DKEYRNAVSK YTMALQQKKA LSKTSKVRPS TGNSASTPQS QCLPSEIEVK YKMAECYTML KQDKDAIAIL D GIPSRQRT PKINMMLANL YKKAGQERPS VTSYKEVLRQ CPLALDAILG LLSLSVKGAE VASMTMNVIQ TVPNLDWLSV WI KAYAFVH TGDNSRAIST ICSLEKKSLL RDNVDLLGSL ADLYFRAGDN KNSVLKFEQA QMLDPYLIKG MDVYGYLLAR EGR LEDVEN LGCRLFNISD QHAEPWVVSG CHSFYSKRYS RALYLGAKAI QLNSNSVQAL LLKGAALRNM GRVQEAIIHF REAI RLAPC RLDCYEGLIE CYLASNSIRE AMVMANNVYK TLGANAQTLT LLATVCLEDP VTQEKAKTLL DKALTQRPDY IKAVV KKAE LLSREQKYED GIALLRNALA NQSDCVLHRI LGDFLVAVNE YQEAMDQYSI ALSLDPNDQK SLEGMQKMEK EESPTD ATQ EEDVDDMEGS GEEGDLEGSD SEAAQWADQE QWFGMQ

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Macromolecule #14: Cell division cycle protein 23 homolog

MacromoleculeName: Cell division cycle protein 23 homolog / type: protein_or_peptide / ID: 14 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 68.921031 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTL AKAYFDVKEY DRAAHFLHGC NSKKAYFLYM YSRYLSGEKK KDDETVDSLG PLEKGQVKNE ALRELRVELS K KHQARELD ...String:
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTL AKAYFDVKEY DRAAHFLHGC NSKKAYFLYM YSRYLSGEKK KDDETVDSLG PLEKGQVKNE ALRELRVELS K KHQARELD GFGLYLYGVV LRKLDLVKEA IDVFVEATHV LPLHWGAWLE LCNLITDKEM LKFLSLPDTW MKEFFLAHIY TE LQLIEEA LQKYQNLIDV GFSKSSYIVS QIAVAYHNIR DIDKALSIFN ELRKQDPYRI ENMDTFSNLL YVRSMKSELS YLA HNLCEI DKYRVETCCV IGNYYSLRSQ HEKAALYFQR ALKLNPRYLG AWTLMGHEYM EMKNTSAAIQ AYRHAIEVNK RDYR AWYGL GQTYEILKMP FYCLYYYRRA HQLRPNDSRM LVALGECYEK LNQLVEAKKC YWRAYAVGDV EKMALVKLAK LHEQL TESE QAAQCYIKYI QDIYSCGEIV EHLEESTAFR YLAQYYFKCK LWDEASTCAQ KCCAFNDTRE EGKALLRQIL QLRNQG ETP TTEVPAPFFL PASLSANNTP TRRVSPLNLS SVTP

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Macromolecule #15: Cell division cycle protein 20 homolog

MacromoleculeName: Cell division cycle protein 20 homolog / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.796508 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP GKSSSKVQTT PSKPGGDRYI PHRSAAQME VASFLLSKEN QPENSQTPTK KEHQKAWALN LNGFDVEEAK ILRLSGKPQN APEGYQNRLK VLYSQKATPG S SRKTCRYI ...String:
MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP GKSSSKVQTT PSKPGGDRYI PHRSAAQME VASFLLSKEN QPENSQTPTK KEHQKAWALN LNGFDVEEAK ILRLSGKPQN APEGYQNRLK VLYSQKATPG S SRKTCRYI PSLPDRILDA PEIRNDYYLN LVDWSSGNVL AVALDNSVYL WSASSGDILQ LLQMEQPGEY ISSVAWIKEG NY LAVGTSS AEVQLWDVQQ QKRLRNMTSH SARVGSLSWN SYILSSGSRS GHIHHHDVRV AEHHVATLSG HSQEVCGLRW APD GRHLAS GGNDNLVNVW PSAPGEGGWV PLQTFTQHQG AVKAVAWCPW QSNVLATGGG TSDRHIRIWN VCSGACLSAV DAHS QVCSI LWSPHYKELI SGHGFAQNQL VIWKYPTMAK VAELKGHTSR VLSLTMSPDG ATVASAAADE TLRLWRCFEL DPARR RERE KASAAKSSLI HQGIR

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Macromolecule #16: Cyclin-A2

MacromoleculeName: Cyclin-A2 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.427766 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENIVAPLKDL PVNDEHVTVP PWKANSKQPA FTIHVDEAEK EAQKKPAESQ KIEREDALA FNSAISLPGP RKPLVPLDYP MDGSFESPHT MDMSIILEDE KPVSVNEVPD YHEDIHTYLR EMEVKCKPKV G YMKKQPDI ...String:
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENIVAPLKDL PVNDEHVTVP PWKANSKQPA FTIHVDEAEK EAQKKPAESQ KIEREDALA FNSAISLPGP RKPLVPLDYP MDGSFESPHT MDMSIILEDE KPVSVNEVPD YHEDIHTYLR EMEVKCKPKV G YMKKQPDI TNSMRAILVD WLVEVGEEYK LQNETLHLAV NYIDRFLSSM SVLRGKLQLV GTAAMLLASK FEEIYPPEVA EF VYITDDT YTKKQVLRME HLVLKVLTFD LAAPTVNQFL TQYFLHQQPA NCKVESLAMF LGELSLIDAD PYLKYLPSVI AGA AFHLAL YTVTGQSWPE SLIRKTGYTL ESLKPCLMDL HQTYLKAPQH AQQSIREKYK NSKYHGVSLL NPPETLNL

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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

Concentration0.15 mg/mL
BufferpH: 8 / Details: 20mM Hepes, 150mM NaCl, 0.5mM TCEP
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 28.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 117044
FSC plot (resolution estimation)

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