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- EMDB-17814: Structure of the human outer kinetochore KMN network complex -

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Basic information

Entry
Database: EMDB / ID: EMD-17814
TitleStructure of the human outer kinetochore KMN network complex
Map dataMasked KMN network junction complex
Sample
  • Complex: Outer kinetochore KMN network junction complex
    • Protein or peptide: Kinetochore-associated protein DSN1 homolog
    • Protein or peptide: Protein MIS12 homolog
    • Protein or peptide: Kinetochore-associated protein NSL1 homolog
    • Protein or peptide: Polyamine-modulated factor 1
    • Protein or peptide: Kinetochore protein Spc24
    • Protein or peptide: Kinetochore protein Spc25
    • Protein or peptide: Kinetochore scaffold 1
    • Protein or peptide: ZW10 interactor
  • Ligand: water
KeywordsKinetochore / complex / KMN / CELL CYCLE
Function / homology
Function and homology information


regulation of meiosis I spindle assembly checkpoint / Knl1/Spc105 complex / positive regulation of meiosis I spindle assembly checkpoint / homologous chromosome orientation in meiotic metaphase I / MIS12/MIND type complex / skeletal muscle satellite cell proliferation / Ndc80 complex / leucine zipper domain binding / acrosome assembly / regulation of mitotic cell cycle spindle assembly checkpoint ...regulation of meiosis I spindle assembly checkpoint / Knl1/Spc105 complex / positive regulation of meiosis I spindle assembly checkpoint / homologous chromosome orientation in meiotic metaphase I / MIS12/MIND type complex / skeletal muscle satellite cell proliferation / Ndc80 complex / leucine zipper domain binding / acrosome assembly / regulation of mitotic cell cycle spindle assembly checkpoint / attachment of spindle microtubules to kinetochore / attachment of mitotic spindle microtubules to kinetochore / kinetochore assembly / protein localization to kinetochore / mitotic spindle assembly checkpoint signaling / mitotic sister chromatid segregation / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Deposition of new CENPA-containing nucleosomes at the centromere / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / acrosomal vesicle / chromosome segregation / RHO GTPases Activate Formins / establishment of localization in cell / kinetochore / fibrillar center / spindle pole / Separation of Sister Chromatids / azurophil granule lumen / transcription regulator complex / transcription by RNA polymerase II / transcription coactivator activity / nuclear body / nuclear speck / cell division / intracellular membrane-bounded organelle / dendrite / Neutrophil degranulation / nucleolus / Golgi apparatus / extracellular region / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
ZW10 interactor / ZW10 interactor / Knl1, C-terminal RWD domain / Knl1 RWD C-terminal domain / Chromosome segregation protein Spc25, C-terminal / Kinetochore Mis14/Nsl1 / Kinetochore scaffold 1 / KNL1 MELT repeat / Kinetochore protein Spc25 / Chromosome segregation protein Spc25 ...ZW10 interactor / ZW10 interactor / Knl1, C-terminal RWD domain / Knl1 RWD C-terminal domain / Chromosome segregation protein Spc25, C-terminal / Kinetochore Mis14/Nsl1 / Kinetochore scaffold 1 / KNL1 MELT repeat / Kinetochore protein Spc25 / Chromosome segregation protein Spc25 / Kinetochore protein Mis14 like / MELT motif / Nuclear MIS12/MIND complex subunit PMF1/Nnf1 / Centromere protein Mis12 / Nnf1 / Mis12 protein / Kinetochore-associated protein Dsn1/Mis13 / Mis12-Mtw1 protein family / Kinetochore-Ndc80 subunit Spc24 / Spc24 subunit of Ndc80
Similarity search - Domain/homology
ZW10 interactor / Polyamine-modulated factor 1 / Kinetochore protein Spc24 / Kinetochore scaffold 1 / Kinetochore-associated protein NSL1 homolog / Protein MIS12 homolog / Kinetochore-associated protein DSN1 homolog / Kinetochore protein Spc25
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsYatskevich S / Barford D
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/6 United Kingdom
Cancer Research UKC576/A14109 United Kingdom
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Structure of the human outer kinetochore KMN network complex.
Authors: Stanislau Yatskevich / Jing Yang / Dom Bellini / Ziguo Zhang / David Barford /
Abstract: Faithful chromosome segregation requires robust, load-bearing attachments of chromosomes to the mitotic spindle, a function accomplished by large macromolecular complexes termed kinetochores. In most ...Faithful chromosome segregation requires robust, load-bearing attachments of chromosomes to the mitotic spindle, a function accomplished by large macromolecular complexes termed kinetochores. In most eukaryotes, the constitutive centromere-associated network (CCAN) complex of the inner kinetochore recruits to centromeres the ten-subunit outer kinetochore KMN network that comprises the KNL1C, MIS12C and NDC80C complexes. The KMN network directly attaches CCAN to microtubules through MIS12C and NDC80C. Here, we determined a high-resolution cryo-EM structure of the human KMN network. This showed an intricate and extensive assembly of KMN subunits, with the central MIS12C forming rigid interfaces with NDC80C and KNL1C, augmented by multiple peptidic inter-subunit connections. We also observed that unphosphorylated MIS12C exists in an auto-inhibited state that suppresses its capacity to interact with CCAN. Ser100 and Ser109 of the N-terminal segment of the MIS12C subunit Dsn1, two key targets of Aurora B kinase, directly stabilize this auto-inhibition. Our study indicates how selectively relieving this auto-inhibition through Ser100 and Ser109 phosphorylation might restrict outer kinetochore assembly to functional centromeres during cell division.
History
DepositionJul 8, 2023-
Header (metadata) releaseMar 20, 2024-
Map releaseMar 20, 2024-
UpdateMar 20, 2024-
Current statusMar 20, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17814.png

Downloads & links

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Map

FileDownload / File: emd_17814.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMasked KMN network junction complex
Voxel sizeX=Y=Z: 1.059 Å
Density
Contour LevelBy AUTHOR: 0.0144
Minimum - Maximum-0.04112646 - 0.07635954
Average (Standard dev.)0.000018036246 (±0.0006068227)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 474.432 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Unmasked KMN network junction complex

Fileemd_17814_additional_1.map
AnnotationUnmasked KMN network junction complex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: MultiBody refined MIS12C heads

Fileemd_17814_additional_2.map
AnnotationMultiBody refined MIS12C heads
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: MultiBody refined KMN junction

Fileemd_17814_additional_3.map
AnnotationMultiBody refined KMN junction
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: MultiBody refined Spc24/Spc25 coiled-coils

Fileemd_17814_additional_4.map
AnnotationMultiBody refined Spc24/Spc25 coiled-coils
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 1

Fileemd_17814_half_map_1.map
AnnotationHalf-map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 2

Fileemd_17814_half_map_2.map
AnnotationHalf-map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Outer kinetochore KMN network junction complex

EntireName: Outer kinetochore KMN network junction complex
Components
  • Complex: Outer kinetochore KMN network junction complex
    • Protein or peptide: Kinetochore-associated protein DSN1 homolog
    • Protein or peptide: Protein MIS12 homolog
    • Protein or peptide: Kinetochore-associated protein NSL1 homolog
    • Protein or peptide: Polyamine-modulated factor 1
    • Protein or peptide: Kinetochore protein Spc24
    • Protein or peptide: Kinetochore protein Spc25
    • Protein or peptide: Kinetochore scaffold 1
    • Protein or peptide: ZW10 interactor
  • Ligand: water

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Supramolecule #1: Outer kinetochore KMN network junction complex

SupramoleculeName: Outer kinetochore KMN network junction complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Kinetochore-associated protein DSN1 homolog

MacromoleculeName: Kinetochore-associated protein DSN1 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.122195 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTSVTRSEII DEKGPVMSKT HDHQLESSLS PVEVFAKTSA SLEMNQGVSE ERIHLGSSPK KGGNCDLSHQ ERLQSKSLHL SPQEQSASY QDRRQSWRRA SMKETNRRKS LHPIHQGITE LSRSISVDLA ESKRLGCLLL SSFQFSIQKL EPFLRDTKGF S LESFRAKA ...String:
MTSVTRSEII DEKGPVMSKT HDHQLESSLS PVEVFAKTSA SLEMNQGVSE ERIHLGSSPK KGGNCDLSHQ ERLQSKSLHL SPQEQSASY QDRRQSWRRA SMKETNRRKS LHPIHQGITE LSRSISVDLA ESKRLGCLLL SSFQFSIQKL EPFLRDTKGF S LESFRAKA SSLSEELKHF ADGLETDGTL QKCFEDSNGK ASDFSLEASV AEMKEYITKF SLERQTWDQL LLHYQQEAKE IL SRGSTEA KITEVKVEPM TYLGSSQNEV LNTKPDYQKI LQNQSKVFDC MELVMDELQG SVKQLQAFMD ESTQCFQKVS VQL GKRSMQ QLDPSPARKL LKLQLQNPPA IHGSGSGSCQ

UniProtKB: Kinetochore-associated protein DSN1 homolog

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Macromolecule #2: Protein MIS12 homolog

MacromoleculeName: Protein MIS12 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.170922 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSVDPMTYEA QFFGFTPQTC MLRIYIAFQD YLFEVMQAVE QVILKKLDGI PDCDISPVQI RKCTEKFLCF MKGHFDNLFS KMEQLFLQL ILRIPSNILL PEDKCKETPY SEEDFQHLQK EIEQLQEKYK TELCTKQALL AELEEQKIVQ AKLKQTLTFF D ELHNVGRD ...String:
MSVDPMTYEA QFFGFTPQTC MLRIYIAFQD YLFEVMQAVE QVILKKLDGI PDCDISPVQI RKCTEKFLCF MKGHFDNLFS KMEQLFLQL ILRIPSNILL PEDKCKETPY SEEDFQHLQK EIEQLQEKYK TELCTKQALL AELEEQKIVQ AKLKQTLTFF D ELHNVGRD HGTSDFRESL VSLVQNSRKL QNIRDNVEKE SKRLKIS

UniProtKB: Protein MIS12 homolog

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Macromolecule #3: Kinetochore-associated protein NSL1 homolog

MacromoleculeName: Kinetochore-associated protein NSL1 homolog / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.208951 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAGSPELVVL DPPWDKELAA GTESQALVSA TPREDFRVRC TSKRAVTEML QLCGRFVQKL GDALPEEIRE PALRDAQWTF ESAVQENIS INGQAWQEAS DNCFMDSDIK VLEDQFDEII VDIATKRKQY PRKILECVIK TIKAKQEILK QYHPVVHPLD L KYDPDPAP ...String:
MAGSPELVVL DPPWDKELAA GTESQALVSA TPREDFRVRC TSKRAVTEML QLCGRFVQKL GDALPEEIRE PALRDAQWTF ESAVQENIS INGQAWQEAS DNCFMDSDIK VLEDQFDEII VDIATKRKQY PRKILECVIK TIKAKQEILK QYHPVVHPLD L KYDPDPAP HMENLKCRGE TVAKEISEAM KSLPALIEQG EGFSQVLRMQ PVIHLQRIHQ EVFSSCHRKP DAKPENFITQ IE TTPTETA SRKTSDMVLK RKQTKDCPQR KWYPLRPKKI NLDT

UniProtKB: Kinetochore-associated protein NSL1 homolog

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Macromolecule #4: Polyamine-modulated factor 1

MacromoleculeName: Polyamine-modulated factor 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.368311 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAEASSANLG SGCEEKRHEG SSSESVPPGT TISRVKLLDT MVDTFLQKLV AAGSYQRFTD CYKCFYQLQP AMTQQIYDKF IAQLQTSIR EEISDIKEEG NLEAVLNALD KIVEEGKVRK EPAWRPSGIP EKDLHSVMAP YFLQQRDTLR RHVQKQEAEN Q QLADAVLA ...String:
MAEASSANLG SGCEEKRHEG SSSESVPPGT TISRVKLLDT MVDTFLQKLV AAGSYQRFTD CYKCFYQLQP AMTQQIYDKF IAQLQTSIR EEISDIKEEG NLEAVLNALD KIVEEGKVRK EPAWRPSGIP EKDLHSVMAP YFLQQRDTLR RHVQKQEAEN Q QLADAVLA GRRQVEELQL QVQAQQQAWQ ALHREQRELV AVLREPE

UniProtKB: Polyamine-modulated factor 1

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Macromolecule #5: Kinetochore protein Spc24

MacromoleculeName: Kinetochore protein Spc24 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.469113 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAAFRDIEEV SQGLLSLLGA NRAEAQQRRL LGRHEQVVER LLETQDGAEK QLREILTMEK EVAQSLLNAK EQVHQGGVEL QQLEAGLQE AGEEDTRLKA SLLQLTRELE ELKEIEADLE RQEKEVDEDT TVTIPSAVYV AQLYHQVSKI EWDYECEPGM V KGIHHGPS ...String:
MAAFRDIEEV SQGLLSLLGA NRAEAQQRRL LGRHEQVVER LLETQDGAEK QLREILTMEK EVAQSLLNAK EQVHQGGVEL QQLEAGLQE AGEEDTRLKA SLLQLTRELE ELKEIEADLE RQEKEVDEDT TVTIPSAVYV AQLYHQVSKI EWDYECEPGM V KGIHHGPS VAQPIHLDST QLSRKFISDY LWSLVDTEW

UniProtKB: Kinetochore protein Spc24

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Macromolecule #6: Kinetochore protein Spc25

MacromoleculeName: Kinetochore protein Spc25 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.192832 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MVEDELALFD KSINEFWNKF KSTDTSCQMA GLRDTYKDSI KAFAEKLSVK LKEEERMVEM FLEYQNQISR QNKLIQEKKD NLLKLIAEV KGKKQELEVL TANIQDLKEE YSRKKETIST ANKANAERLK RLQKSADLYK DRLGLEIRKI YGEKLQFIFT N IDPKNPES ...String:
MVEDELALFD KSINEFWNKF KSTDTSCQMA GLRDTYKDSI KAFAEKLSVK LKEEERMVEM FLEYQNQISR QNKLIQEKKD NLLKLIAEV KGKKQELEVL TANIQDLKEE YSRKKETIST ANKANAERLK RLQKSADLYK DRLGLEIRKI YGEKLQFIFT N IDPKNPES PFMFSLHLNE ARDYEVSDSA PHLEGLAEFQ ENVRKTNNFS AFLANVRKAF TATVYN

UniProtKB: Kinetochore protein Spc25

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Macromolecule #7: Kinetochore scaffold 1

MacromoleculeName: Kinetochore scaffold 1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 265.722125 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MDGVSSEANE ENDNIERPVR RRHSSILKPP RSPLQDLRGG NERVQESNAL RNKKNSRRVS FADTIKVFQT ESHMKIVRKS EMEGCSAMV PSQLQLLPPG FKRFSCLSLP ETETGENLLL IQNKKLEDNY CEITGMNTLL SAPIHTQMQQ KEFSIIEHTR E RKHANDQT ...String:
MDGVSSEANE ENDNIERPVR RRHSSILKPP RSPLQDLRGG NERVQESNAL RNKKNSRRVS FADTIKVFQT ESHMKIVRKS EMEGCSAMV PSQLQLLPPG FKRFSCLSLP ETETGENLLL IQNKKLEDNY CEITGMNTLL SAPIHTQMQQ KEFSIIEHTR E RKHANDQT VIFSDENQMD LTSSHTVMIT KGLLDNPISE KSTKIDTTSF LANLKLHTED SRMKKEVNFS VDQNTSSENK ID FNDFIKR LKTGKCSAFP DVPDKENFEI PIYSKEPNSA SSTHQMHVSL KEDENNSNIT RLFREKDDGM NFTQCHTANI QTL IPTSSE TNSRESKGND ITIYGNDFMD LTFNHTLQIL PATGNFSEIE NQTQNAMDVT TGYGTKASGN KTVFKSKQNT AFQD LSINS ADKIHITRSH IMGAETHIVS QTCNQDARIL AMTPESIYSN PSIQGCKTVF YSSCNDAMEM TKCLSNMREE KNLLK HDSN YAKMYCNPDA MSSLTEKTIY SGEENMDITK SHTVAIDNQI FKQDQSNVQI AAAPTPEKEM MLQNLMTTSE DGKMNV NCN SVPHVSKERI QQSLSNPLSI SLTDRKTELL SGENMDLTES HTSNLGSQVP LAAYNLAPES TSESHSQSKS SSDECEE IT KSRNEPFQRS DIIAKNSLTD TWNKDKDWVL KILPYLDKDS PQSADCNQEI ATSHNIVYCG GVLDKQITNR NTVSWEQS L FSTTKPLFSS GQFSMKNHDT AISSHTVKSV LGQNSKLAEP LRKSLSNPTP DYCHDKMIIC SEEEQNMDLT KSHTVVIGF GPSELQELGK TNLEHTTGQL TTMNRQIAVK VEKCGKSPIE KSGVLKSNCI MDVLEDESVQ KPKFPKEKQN VKIWGRKSVG GPKIDKTIV FSEDDKNDMD ITKSYTIEIN HRPLLEKRDC HLVPLAGTSE TILYTCRQDD MEITRSHTTA LECKTVSPDE I TTRPMDKT VVFVDNHVEL EMTESHTVFI DYQEKERTDR PNFELSQRKS LGTPTVICTP TEESVFFPGN GESDRLVAND SQ LTPLEEW SNNRGPVEVA DNMELSKSAT CKNIKDVQSP GFLNEPLSSK SQRRKSLKLK NDKTIVFSEN HKNDMDITQS CMV EIDNES ALEDKEDFHL AGASKTILYS CGQDDMEITR SHTTALECKT LLPNEIAIRP MDKTVLFTDN YSDLEVTDSH TVFI DCQAT EKILEENPKF GIGKGKNLGV SFPKDNSCVQ EIAEKQALAV GNKIVLHTEQ KQQLFAATNR TTNEIIKFHS AAMDE KVIG KVVDQACTLE KAQVESCQLN NRDRRNVDFT SSHATAVCGS SDNYSCLPNV ISCTDNLEGS AMLLCDKDEE KANYCP VQN DLAYANDFAS EYYLESEGQP LSAPCPLLEK EEVIQTSTKG QLDCVITLHK DQDLIKDPRN LLANQTLVYS QDLGEMT KL NSKRVSFKLP KDQMKVYVDD IYVIPQPHFS TDQPPLPKKG QSSINKEEVI LSKAGNKSLN IIENSSAPIC ENKPKILN S EEWFAAACKK ELKENIQTTN YNTALDFHSN SDVTKQVIQT HVNAGEAPDP VITSNVPCFH SIKPNLNNLN GKTGEFLAF QTVHLPPLPE QLLELGNKAH NDMHIVQATE IHNINIISSN AKDSRDEENK KSHNGAETTS LPPKTVFKDK VRRCSLGIFL PRLPNKRNC SVTGIDDLEQ IPADTTDINH LETQPVSSKD SGIGSVAGKL NLSPSQYINE ENLPVYPDEI NSSDSINIET E EKALIETY QKEISPYENK MGKTCNSQKR TWVQEEEDIH KEKKIRKNEI KFSDTTQDRE IFDHHTEEDI DKSANSVLIK NL SRTPSSC SSSLDSIKAD GTSLDFSTYR SSQMESQFLR DTICEESLRE KLQDGRITIR EFFILLQVHI LIQKPRQSNL PGN FTVNTP PTPEDLMLSQ YVYRPKIQIY REDCEARRQK IEELKLSASN QDKLLVDINK NLWEKMRHCS DKELKAFGIY LNKI KSCFT KMTKVFTHQG KVALYGKLVQ SAQNEREKLQ IKIDEMDKIL KKIDNCLTEM ETETKNLEDE EKNNPVEEWD SEMRA AEKE LEQLKTEEEE LQRNLLELEV QKEQTLAQID FMQKQRNRTE ELLDQLSLSE WDVVEWSDDQ AVFTFVYDTI QLTITF EES VVGFPFLDKR YRKIVDVNFQ SLLDEDQAPP SSLLVHKLIF QYVEEKESWK KTCTTQHQLP KMLEEFSLVV HHCRLLG EE IEYLKRWGPN YNLMNIDINN NELRLLFSSS AAFAKFEITL FLSAYYPSVP LPSTIQNHVG NTSQDDIATI LSKVPLEN N YLKNVVKQIY QDLFQDCHFY H

UniProtKB: Kinetochore scaffold 1

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Macromolecule #8: ZW10 interactor

MacromoleculeName: ZW10 interactor / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 31.333359 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEAAETEAEA AALEVLAEVA GILEPVGLQE EAELPAKILV EFVVDSQKKD KLLCSQLQVA DFLQNILAQE DTAKGLDPLA SEDTSRQKA IAAKEQWKEL KATYREHVEA IKIGLTKALT QMEEAQRKRT QLREAFEQLQ AKKQMAMEKR RAVQNQWQLQ Q EKHLQHLA ...String:
MEAAETEAEA AALEVLAEVA GILEPVGLQE EAELPAKILV EFVVDSQKKD KLLCSQLQVA DFLQNILAQE DTAKGLDPLA SEDTSRQKA IAAKEQWKEL KATYREHVEA IKIGLTKALT QMEEAQRKRT QLREAFEQLQ AKKQMAMEKR RAVQNQWQLQ Q EKHLQHLA EVSAEVRERK TGTQQELDRV FQKLGNLKQQ AEQERDKLQR YQTFLQLLYT LQGKLLFPEA EAEAENLPDD KP QQPTRPQ EQSTGDTMGR DPGVSFKAVG LQPAGDVNLP

UniProtKB: ZW10 interactor

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Macromolecule #9: water

MacromoleculeName: water / type: ligand / ID: 9 / Number of copies: 1 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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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: 8
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 / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.2 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 599831

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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