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- EMDB-4037: Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in... -

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Basic information

Entry
Database: EMDB / ID: EMD-4037
TitleCryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex (APC/C-MCC) at 4.2 angstrom resolution
Map dataNone
Sample
  • Complex: Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex in closed conformation (APC/C-MCC-closed) at 4.2 angstrom resolution
    • Protein or peptide: x 18 types
    • Unknown: x 3 types
KeywordsComplex / Ubiquitin / E3 ligase / Ubiquitin ligase / Cullin / RING / Cell cycle / Mitosis / Spindle checkpoint / Degron
Function / homology
Function and homology information


metaphase/anaphase transition of cell cycle / mitotic spindle assembly checkpoint MAD1-MAD2 complex / 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 / positive regulation of mitotic cell cycle spindle assembly checkpoint / regulation of meiotic nuclear division / establishment of centrosome localization / meiotic sister chromatid cohesion, centromeric ...metaphase/anaphase transition of cell cycle / mitotic spindle assembly checkpoint MAD1-MAD2 complex / 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 / positive regulation of mitotic cell cycle spindle assembly checkpoint / regulation of meiotic nuclear division / establishment of centrosome localization / meiotic sister chromatid cohesion, centromeric / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / regulation of mitotic cell cycle spindle assembly checkpoint / protein branched polyubiquitination / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / Phosphorylation of Emi1 / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of meiotic cell cycle / anaphase-promoting complex-dependent catabolic process / metaphase/anaphase transition of mitotic cell cycle / positive regulation of synaptic plasticity / regulation of exit from mitosis / anaphase-promoting complex binding / Phosphorylation of the APC/C / nuclear pore nuclear basket / outer kinetochore / protein localization to chromosome, centromeric region / positive regulation of mitotic metaphase/anaphase transition / positive regulation of ubiquitin protein ligase activity / ubiquitin ligase activator activity / protein K11-linked ubiquitination / enzyme-substrate adaptor activity / positive regulation of dendrite morphogenesis / regulation of mitotic metaphase/anaphase transition / ubiquitin-ubiquitin ligase activity / negative regulation of ubiquitin protein ligase activity / mitotic sister chromatid cohesion / mitotic metaphase chromosome alignment / mitotic spindle assembly checkpoint signaling / establishment of mitotic spindle orientation / Regulation of APC/C activators between G1/S and early anaphase / mitotic sister chromatid segregation / cullin family protein binding / Transcriptional Regulation by VENTX / negative regulation of mitotic cell cycle / mitotic spindle assembly / ubiquitin-like ligase-substrate adaptor activity / positive regulation of axon extension / protein K48-linked ubiquitination / heterochromatin / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / regulation of mitotic cell cycle / Resolution of Sister Chromatid Cohesion / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / nuclear periphery / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / Assembly of the pre-replicative complex / RHO GTPases Activate Formins / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / brain development / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / negative regulation of protein catabolic process / CDK-mediated phosphorylation and removal of Cdc6 / mitotic spindle / kinetochore / spindle pole / spindle / ubiquitin-protein transferase activity / Separation of Sister Chromatids / microtubule cytoskeleton / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / mitotic cell cycle / nervous system development / Senescence-Associated Secretory Phenotype (SASP) / ubiquitin-dependent protein catabolic process / protein phosphatase binding / molecular adaptor activity / cell differentiation / non-specific serine/threonine protein kinase / protein kinase activity / Ub-specific processing proteases / protein ubiquitination / cell division / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / ubiquitin protein ligase binding / negative regulation of apoptotic process / nucleolus / apoptotic process / perinuclear region of cytoplasm
Similarity search - Function
Mad3/Bub1 homology region 1 / Mitotic spindle checkpoint protein Bub1/Mad3 / Mad3/BUB1 homology region 1 / BUB1 N-terminal domain profile. / Mad3/BUB1 hoMad3/BUB1 homology region 1 / 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 1, C-terminal ...Mad3/Bub1 homology region 1 / Mitotic spindle checkpoint protein Bub1/Mad3 / Mad3/BUB1 homology region 1 / BUB1 N-terminal domain profile. / Mad3/BUB1 hoMad3/BUB1 homology region 1 / 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 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 5, N-terminal domain / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex, subunit 16 / Cdc23 / Apc13 / Anaphase promoting complex subunit 8 / Cdc23 / Apc13p protein / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 4 long domain / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 5 domain / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex, cyclosome, subunit 4 / 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 / Mad2-like / HORMA domain / HORMA domain / HORMA domain profile. / APC10/DOC domain / Anaphase-promoting complex, subunit 10 (APC10) / DOC domain profile. / Anaphase-promoting complex, subunit 10 (APC10) / Anaphase-promoting complex, cyclosome, subunit 3 / HORMA domain superfamily / TPR repeat / Tetratricopeptide repeat / : / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat / 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. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Winged helix-like DNA-binding domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Mitotic checkpoint serine/threonine-protein kinase BUB1 beta / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Mitotic spindle assembly checkpoint protein MAD2A / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 ...Mitotic checkpoint serine/threonine-protein kinase BUB1 beta / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Mitotic spindle assembly checkpoint protein MAD2A / 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: 4.2 Å
AuthorsAlfieri C / Chang L / Zhang Z / Yang J / Maslen S / Skehel M / Barford D
CitationJournal: Nature / Year: 2016
Title: Molecular basis of APC/C regulation by the spindle assembly checkpoint.
Authors: Claudio Alfieri / Leifu Chang / Ziguo Zhang / Jing Yang / Sarah Maslen / Mark Skehel / David Barford /
Abstract: In the dividing eukaryotic cell, the spindle assembly checkpoint (SAC) ensures that each daughter cell inherits an identical set of chromosomes. The SAC coordinates the correct attachment of sister ...In the dividing eukaryotic cell, the spindle assembly checkpoint (SAC) ensures that each daughter cell inherits an identical set of chromosomes. The SAC coordinates the correct attachment of sister chromatid kinetochores to the mitotic spindle with activation of the anaphase-promoting complex (APC/C), the E3 ubiquitin ligase responsible for initiating chromosome separation. In response to unattached kinetochores, the SAC generates the mitotic checkpoint complex (MCC), which inhibits the APC/C and delays chromosome segregation. By cryo-electron microscopy, here we determine the near-atomic resolution structure of a human APC/C–MCC complex (APC/C(MCC)). Degron-like sequences of the MCC subunit BubR1 block degron recognition sites on Cdc20, the APC/C coactivator subunit responsible for substrate interactions. BubR1 also obstructs binding of the initiating E2 enzyme UbcH10 to repress APC/C ubiquitination activity. Conformational variability of the complex enables UbcH10 association, and structural analysis shows how the Cdc20 subunit intrinsic to the MCC (Cdc20(MCC)) is ubiquitinated, a process that results in APC/C reactivation when the SAC is silenced.
History
DepositionJun 22, 2016-
Header (metadata) releaseJul 20, 2016-
Map releaseAug 10, 2016-
UpdateOct 9, 2024-
Current statusOct 9, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.08
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.08
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-5lcw
  • Surface level: 0.08
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4037_1.png

emd_4037_2.png

emd_4037_3.png

emd_4037_4.png

Downloads & links

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Map

FileDownload / File: emd_4037.map.gz / Format: CCP4 / Size: 70.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Projections & slices

Image control

Size
Brightness
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AxesZ (Sec.)Y (Row.)X (Col.)
1.36 Å/pix.
x 264 pix.
= 359.04 Å		1.36 Å/pix.
x 264 pix.
= 359.04 Å		1.36 Å/pix.
x 264 pix.
= 359.04 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.36 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.08 / Movie #1: 0.08
Minimum - Maximum-0.09435883 - 0.29182208
Average (Standard dev.)0.0025709714 (±0.015112975)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions264264264
Spacing264264264
CellA=B=C: 359.04 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.361.361.36
M x/y/z264264264
origin x/y/z0.0000.0000.000
length x/y/z359.040359.040359.040
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS264264264
D min/max/mean-0.0940.2920.003

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Supplemental data

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Additional map: None

Fileemd_4037_additional_1.map
AnnotationNone
Projections & Slices
AxesZYX

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Additional map: None

Fileemd_4037_additional_2.map
AnnotationNone
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Additional map: None

Fileemd_4037_additional_3.map
AnnotationNone
Projections & Slices
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Sample components

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Entire : Anaphase-promoting complex/Cyclosome, in complex with the Mitotic...

EntireName: Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex in closed conformation (APC/C-MCC-closed) at 4.2 angstrom resolution
Components
  • Complex: Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex in closed conformation (APC/C-MCC-closed) at 4.2 angstrom resolution
    • Protein or peptide: Anaphase-promoting complex subunit 1
    • Protein or peptide: Anaphase-promoting complex subunit 11
    • Protein or peptide: Cell division cycle protein 23 homolog
    • Protein or peptide: Anaphase-promoting complex subunit 15
    • Protein or peptide: Anaphase-promoting complex subunit 16
    • Protein or peptide: Cell division cycle protein 27 homolog
    • Protein or peptide: Anaphase-promoting complex subunit CDC26
    • Protein or peptide: Anaphase-promoting complex subunit 4
    • Protein or peptide: Cell division cycle protein 16 homolog
    • Protein or peptide: Anaphase-promoting complex subunit 10
    • Protein or peptide: Anaphase-promoting complex subunit 13
    • Protein or peptide: Anaphase-promoting complex subunit 2
    • Protein or peptide: Anaphase-promoting complex subunit 5
    • Protein or peptide: Cell division cycle protein 20 homolog
    • Protein or peptide: Cell division cycle protein 20 homolog
    • Protein or peptide: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta,Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
    • Protein or peptide: Anaphase-promoting complex subunit 7
    • Protein or peptide: Mitotic spindle assembly checkpoint protein MAD2A

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Supramolecule #1: Anaphase-promoting complex/Cyclosome, in complex with the Mitotic...

SupramoleculeName: Anaphase-promoting complex/Cyclosome, in complex with the Mitotic checkpoint complex in closed conformation (APC/C-MCC-closed) at 4.2 angstrom resolution
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#21
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.6 MDa

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Macromolecule #1: Anaphase-promoting complex subunit 1

MacromoleculeName: Anaphase-promoting complex subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 216.775516 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 SSSLTAHLRS LSKGDSPVTS PFQ NYSSIH SQSRSTSSPS LHSRSPSISN MAALSRAHSF ALGVHSFSGV QRFNISSHNQ SPKRHSISHS PNSNSNGSFL APET EPIVP ELCIDHLWTE TITNIREKNS QASKVFITSD LCGQKFLCFL VESQLQLRCV KFQESNDKTQ LIFGSVTNIP AKDAA PVEK IDTMLVLEGS GNLVLYTGVV RVGKVFIPGL PAPSLTMSNT MPRPSTPLDG VSTPKPLSKL LGSLDEVVLL SPVPEL RDS SKLHDSLYNE DCTFQQLGTY IHSIRDPVHN RVTLELSNGS MVRITIPEIA TSELVQTCLQ AIKFILPKEI AVQMLVK WY NVHSAPGGPS YHSEWNLFVT CLMNMMGYNT DRLAWTRNFD FEGSLSPVIA PKKARPSETG SDDDWEYLLN SDYHQNVE S HLLNRSLCLS PSEASQMKDE DFSQNLSLDS STLLFTHIPA IFFVLHLVYE ELKLNTLMGE GICSLVELLV QLARDLKLG PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVS DESSQYLTRI TIAPQKLQVE QEENRFSFRH STSVSSLAER LVVWMTNVGF TLRDLETLPF GIALPIRDAI Y HCREQPAS DWPEAVCLLI GRQDLSKQAC EGNLPKGKSV LSSDVPSGTE TEEEDDGMND MNHEVMSLIW SEDLRVQDVR RL LQSAHPV RVNVVQYPEL SDHEFIEEKE NRLLQLCQRT MALPVGRGMF TLFSYHPVPT EPLPIPKLNL TGRAPPRNTT VDL NSGNID VPPNMTSWAS FHNGVAAGLK IAPASQIDSA WIVYNKPKHA ELANEYAGFL MALGLNGHLT KLATLNIHDY LTKG HEMTS IGLLLGVSAA KLGTMDMSIT RLLSIHIPAL LPPTSTELDV PHNVQVAAVV GIGLVYQGTA HRHTAEVLLA EIGRP PGPE MEYCTDRESY SLAAGLALGM VCLGHGSNLI GMSDLNVPEQ LYQYMVGGHR RFQTGMHREK HKSPSYQIKE GDTINV DVT CPGATLALAM IYLKTNNRSI ADWLRAPDTM YLLDFVKPEF LLLRTLARCL ILWDDILPNS KWVDSNVPQI IRENSIS LS EIELPCSEDL NLETLSQAHV YIIAGACLSL GFRFAGSENL SAFNCLHKFA KDFMTYLSAP NASVTGPHNL ETCLSVVL L SLAMVMAGSG NLKVLQLCRF LHMKTGGEMN YGFHLAHHMA LGLLFLGGGR YSLSTSNSSI AALLCALYPH FPAHSTDNR YHLQALRHLY VLAAEPRLLV PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL SKGTQHLKS ILSKDGVLYV KLRAGQLSYK EDPMGWQSLL AQTVANRNSE ARAFKPETIS AFTSDPALLS FAEYFCKPTV N MGQKQEIL DLFSSVLYEC VTQETPEMLP AYIAMDQAIR RLGRREMSET SELWQIKLVL EFFSSRSHQE RLQNHPKRGL FM NSEFLPV VKCTIDNTLD QWLQVGGDMC VHAYLSGQPL EESQLSMLAC FLVYHSVPAP QHLPPIGLEG STSFAELLFK FKQ LKMPVR ALLRLAPLLL GNPQPMVM

UniProtKB: Anaphase-promoting complex subunit 1

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Macromolecule #2: Anaphase-promoting complex subunit 11

MacromoleculeName: Anaphase-promoting complex subunit 11 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.854647 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI LKWLHAQQVQ QHCPMCRQEW KFKE

UniProtKB: Anaphase-promoting complex subunit 11

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Macromolecule #3: Cell division cycle protein 23 homolog

MacromoleculeName: Cell division cycle protein 23 homolog / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 68.921031 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Cell division cycle protein 23 homolog

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Macromolecule #4: Anaphase-promoting complex subunit 15

MacromoleculeName: Anaphase-promoting complex subunit 15 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.286727 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MSTLFPSLFP RVTETLWFNL DRPCVEETEL QQQEQQHQAW LQSIAEKDNN LVPIGKPASE HYDDEEEEDD EDDEDSEEDS EDDEDMQDM DEMNDYNESP DDGEVNEVDM EGNEQDQDQW MI

UniProtKB: Anaphase-promoting complex subunit 15

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Macromolecule #5: Anaphase-promoting complex subunit 16

MacromoleculeName: Anaphase-promoting complex subunit 16 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.677995 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MAASSSSSSA GGVSGSSVTG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS ERFLCESVFS YQVASTLKQV KHDQQVARME KLAGLVEEL EADEWRFKPI EQLLGFTPSS G

UniProtKB: Anaphase-promoting complex subunit 16

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Macromolecule #6: Cell division cycle protein 27 homolog

MacromoleculeName: Cell division cycle protein 27 homolog / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 91.973125 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Cell division cycle protein 27 homolog

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Macromolecule #7: Anaphase-promoting complex subunit CDC26

MacromoleculeName: Anaphase-promoting complex subunit CDC26 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.793999 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF

UniProtKB: Anaphase-promoting complex subunit CDC26

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Macromolecule #8: Anaphase-promoting complex subunit 4

MacromoleculeName: Anaphase-promoting complex subunit 4 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 92.219227 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Anaphase-promoting complex subunit 4

+
Macromolecule #9: Cell division cycle protein 16 homolog

MacromoleculeName: Cell division cycle protein 16 homolog / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 71.747516 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Cell division cycle protein 16 homolog

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Macromolecule #10: Anaphase-promoting complex subunit 10

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

UniProtKB: Anaphase-promoting complex subunit 10

+
Macromolecule #11: Anaphase-promoting complex subunit 13

MacromoleculeName: Anaphase-promoting complex subunit 13 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.528309 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLNELPEPE QDNGGTTESV KEQEMKWTDL ALQYLHENVP PIGN

UniProtKB: Anaphase-promoting complex subunit 13

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Macromolecule #12: Anaphase-promoting complex subunit 2

MacromoleculeName: Anaphase-promoting complex subunit 2 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.938977 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Anaphase-promoting complex subunit 2

+
Macromolecule #13: Anaphase-promoting complex subunit 5

MacromoleculeName: Anaphase-promoting complex subunit 5 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 85.179766 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Anaphase-promoting complex subunit 5

+
Macromolecule #14: Cell division cycle protein 20 homolog

MacromoleculeName: Cell division cycle protein 20 homolog / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.226332 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: EEAKILRLSG KPQNAPEGYQ NRLKVLYSQK ATPGSSRKTC RYIPSLPDRI LDAPEIRNDY YLNLVDWSSG NVLAVALDNS VYLWSASSG DILQLLQMEQ PGEYISSVAW IKEGNYLAVG TSSAEVQLWD VQQQKRLRNM TSHSARVGSL SWNSYILSSG S RSGHIHHH ...String:
EEAKILRLSG KPQNAPEGYQ NRLKVLYSQK ATPGSSRKTC RYIPSLPDRI LDAPEIRNDY YLNLVDWSSG NVLAVALDNS VYLWSASSG DILQLLQMEQ PGEYISSVAW IKEGNYLAVG TSSAEVQLWD VQQQKRLRNM TSHSARVGSL SWNSYILSSG S RSGHIHHH DVRVAEHHVA TLSGHSQEVC GLRWAPDGRH LASGGNDNLV NVWPSAPGEG GWVPLQTFTQ HQGAVKAVAW CP WQSNVLA TGGGTSDRHI RIWNVCSGAC LSAVDAHSQV CSILWSPHYK ELISGHGFAQ NQLVIWKYPT MAKVAELKGH TSR VLSLTM SPDGATVASA AADETLRLWR CFELDPARRR EREKASAAKS SLIHQGIR

UniProtKB: Cell division cycle protein 20 homolog

+
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: Trichoplusia ni (cabbage looper)
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

UniProtKB: Cell division cycle protein 20 homolog

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Macromolecule #16: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta,Mito...

MacromoleculeName: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta,Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO / EC number: non-specific serine/threonine protein kinase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.055797 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAAVKKEGGA LSEAMSLEGD EWELSKENVQ PLRQGRIMST LQGALAQESA CNNTLQQQKR AFEYEIRFYT GNDPLDVWDR YISWTEQNY PQGGKESNMS TLLERAVEAL QGEKRYYSDP RFLNLWLKLG RLCNEPLDMY SYLHNQGIGV SLAQFYISWA E EYEARENF ...String:
MAAVKKEGGA LSEAMSLEGD EWELSKENVQ PLRQGRIMST LQGALAQESA CNNTLQQQKR AFEYEIRFYT GNDPLDVWDR YISWTEQNY PQGGKESNMS TLLERAVEAL QGEKRYYSDP RFLNLWLKLG RLCNEPLDMY SYLHNQGIGV SLAQFYISWA E EYEARENF RKADAIFQEG IQQKAEPLER LQSQHRQFQA RVSRQTLLAL EKEEEEEVFE SSVPQRSTLA ELKSKGKKTA RA PIIRVGG ALKAPSQNRG LQNPFPQQMQ NNSRITVFDE NADEASTAEL SKPTVQPWIA PPMPRAKENE LQASIFDEFL LSE KKNKSP PADPPRVLAQ RRPLAV

UniProtKB: Mitotic checkpoint serine/threonine-protein kinase BUB1 beta, Mitotic checkpoint serine/threonine-protein kinase BUB1 beta

+
Macromolecule #17: Anaphase-promoting complex subunit 7

MacromoleculeName: Anaphase-promoting complex subunit 7 / type: protein_or_peptide / ID: 17 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 66.929367 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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

UniProtKB: Anaphase-promoting complex subunit 7

+
Macromolecule #18: Mitotic spindle assembly checkpoint protein MAD2A

MacromoleculeName: Mitotic spindle assembly checkpoint protein MAD2A / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.533883 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVIS NIESGEVLER WQFDIECDKT AKDDSAPREK SQKAIQDEIR SVIRQITATV TFLPLLEVSC SFDLLIYTDK D LVVPEKWE ...String:
MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVIS NIESGEVLER WQFDIECDKT AKDDSAPREK SQKAIQDEIR SVIRQITATV TFLPLLEVSC SFDLLIYTDK D LVVPEKWE ESGPQFITNS EEVRLRSFTT TIHKVNSMVA YKIPVND

UniProtKB: Mitotic spindle assembly checkpoint protein MAD2A

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 27.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

2924

Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 155263
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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