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- EMDB-12607: Human TRiC complex in closed state with nanobody and tubulin bound -

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Basic information

Entry
Database: EMDB / ID: EMD-12607
TitleHuman TRiC complex in closed state with nanobody and tubulin bound
Map data
Sample
  • Complex: Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and tubulin bound
    • Complex: Human type II chaperonin TRiC/CCT complex
      • Protein or peptide: x 8 types
    • Complex: Nanobody
      • Protein or peptide: x 1 types
    • Complex: T-complex protein 1 subunit epsilon
      • Protein or peptide: x 1 types
  • Ligand: x 4 types
Function / homology
Function and homology information


Post-chaperonin tubulin folding pathway / zona pellucida receptor complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / scaRNA localization to Cajal body / Carboxyterminal post-translational modifications of tubulin / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly ...Post-chaperonin tubulin folding pathway / zona pellucida receptor complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / scaRNA localization to Cajal body / Carboxyterminal post-translational modifications of tubulin / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / Sealing of the nuclear envelope (NE) by ESCRT-III / chaperonin-containing T-complex / Intraflagellar transport / binding of sperm to zona pellucida / positive regulation of telomerase RNA localization to Cajal body / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / COPI-independent Golgi-to-ER retrograde traffic / Gap junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / Kinesins / Assembly and cell surface presentation of NMDA receptors / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / COPI-dependent Golgi-to-ER retrograde traffic / WD40-repeat domain binding / intercellular bridge / pericentriolar material / beta-tubulin binding / : / Association of TriC/CCT with target proteins during biosynthesis / Recycling pathway of L1 / chaperone-mediated protein complex assembly / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / Hedgehog 'off' state / COPI-mediated anterograde transport / heterochromatin / Activation of AMPK downstream of NMDARs / Mitotic Prometaphase / chaperone-mediated protein folding / EML4 and NUDC in mitotic spindle formation / Recruitment of NuMA to mitotic centrosomes / protein folding chaperone / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / positive regulation of telomere maintenance via telomerase / MHC class II antigen presentation / Resolution of Sister Chromatid Cohesion / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / ATP-dependent protein folding chaperone / response to virus / PKR-mediated signaling / cilium / structural constituent of cytoskeleton / cerebral cortex development / mitotic spindle / mRNA 5'-UTR binding / microtubule cytoskeleton organization / Aggrephagy / HCMV Early Events / Separation of Sister Chromatids / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / The role of GTSE1 in G2/M progression after G2 checkpoint / azurophil granule lumen / microtubule cytoskeleton / G-protein beta-subunit binding / unfolded protein binding / extracellular vesicle / melanosome / protein folding / mitotic cell cycle / cell body / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / cytoskeleton / protein stabilization / cadherin binding / GTPase activity / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / GTP binding / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / : ...T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / : / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily
Similarity search - Domain/homology
T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / T-complex protein 1 subunit beta / Tubulin beta-2A chain / T-complex protein 1 subunit eta
Similarity search - Component
Biological speciesHomo sapiens (human) / Lama glama (llama) / Human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsKelly JJ / Chi G / Bulawa C / Paavilainen VO / Bountra C / Huiskonen JT / Yue W
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Authors: John J Kelly / Dale Tranter / Els Pardon / Gamma Chi / Holger Kramer / Lotta Happonen / Kelly M Knee / Jay M Janz / Jan Steyaert / Christine Bulawa / Ville O Paavilainen / Juha T Huiskonen / Wyatt W Yue /
Abstract: The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, ...The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC.
History
DepositionMar 15, 2021-
Header (metadata) releaseMar 2, 2022-
Map releaseMar 2, 2022-
UpdateJun 1, 2022-
Current statusJun 1, 2022Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.025
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.025
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7nvn
  • Surface level: 0.025
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12607.png

Downloads & links

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Map

FileDownload / File: emd_12607.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 400 pix.
= 424. Å		1.06 Å/pix.
x 400 pix.
= 424. Å		1.06 Å/pix.
x 400 pix.
= 424. Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.025 / Movie #1: 0.025
Minimum - Maximum-0.08860754 - 0.18727382
Average (Standard dev.)1.5498836e-05 (±0.0071762307)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 423.99997 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z424.000424.000424.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ512512512
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0890.1870.000

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Supplemental data

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Mask #1

Fileemd_12607_msk_1.map
Projections & Slices
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Histogram (log scale)

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Half map: #2

Fileemd_12607_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_12607_half_map_2.map
Projections & Slices
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Sample components

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Entire : Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and ...

EntireName: Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and tubulin bound
Components
  • Complex: Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and tubulin bound
    • Complex: Human type II chaperonin TRiC/CCT complex
      • Protein or peptide: T-complex protein 1 subunit alpha
      • Protein or peptide: T-complex protein 1 subunit beta
      • Protein or peptide: T-complex protein 1 subunit delta
      • Protein or peptide: T-complex protein 1 subunit gamma
      • Protein or peptide: T-complex protein 1 subunit eta
      • Protein or peptide: T-complex protein 1 subunit theta
      • Protein or peptide: T-complex protein 1 subunit zeta
      • Protein or peptide: Tubulin beta-2A chain
    • Complex: Nanobody
      • Protein or peptide: Nanobody
    • Complex: T-complex protein 1 subunit epsilon
      • Protein or peptide: T-complex protein 1 subunit epsilon
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ALUMINUM FLUORIDE
  • Ligand: water

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Supramolecule #1: Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and ...

SupramoleculeName: Human type II chaperonin TRiC/CCT complex with nanobody Nb18 and tubulin bound
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10

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Supramolecule #2: Human type II chaperonin TRiC/CCT complex

SupramoleculeName: Human type II chaperonin TRiC/CCT complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#3, #5-#6, #8-#10
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Nanobody

SupramoleculeName: Nanobody / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #7
Source (natural)Organism: Lama glama (llama)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #4: T-complex protein 1 subunit epsilon

SupramoleculeName: T-complex protein 1 subunit epsilon / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: T-complex protein 1 subunit alpha

MacromoleculeName: T-complex protein 1 subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 60.418477 KDa
SequenceString: MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDG TTSVVIIAAE LLKNADELVK QKIHPTSVIS GYRLACKEAV RYINENLIVN TDELGRDCLI NAAKTSMSSK I IGINGDFF ...String:
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDG TTSVVIIAAE LLKNADELVK QKIHPTSVIS GYRLACKEAV RYINENLIVN TDELGRDCLI NAAKTSMSSK I IGINGDFF ANMVVDAVLA IKYTDIRGQP RYPVNSVNIL KAHGRSQMES MLISGYALNC VVGSQGMPKR IVNAKIACLD FS LQKTKMK LGVQVVITDP EKLDQIRQRE SDITKERIQK ILATGANVIL TTGGIDDMCL KYFVEAGAMA VRRVLKRDLK RIA KASGAT ILSTLANLEG EETFEAAMLG QAEEVVQERI CDDELILIKN TKARTSASII LRGANDFMCD EMERSLHDAL CVVK RVLES KSVVPGGGAV EAALSIYLEN YATSMGSREQ LAIAEFARSL LVIPNTLAVN AAQDSTDLVA KLRAFHNEAQ VNPER KNLK WIGLDLSNGK PRDNKQAGVF EPTIVKVKSL KFATEAAITI LRIDDLIKLH PESKDDKHGS YEDAVHSGAL ND

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Macromolecule #2: T-complex protein 1 subunit beta

MacromoleculeName: T-complex protein 1 subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 57.567141 KDa
SequenceString: MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSR VQDDEVGDGT TSVTVLAAEL LREAESLIAK KIHPQTIIAG WREATKAARE ALLSSAVDHG SDEVKFRQDL M NIAGTTLS ...String:
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSR VQDDEVGDGT TSVTVLAAEL LREAESLIAK KIHPQTIIAG WREATKAARE ALLSSAVDHG SDEVKFRQDL M NIAGTTLS SKLLTHHKDH FTKLAVEAVL RLKGSGNLEA IHIIKKLGGS LADSYLDEGF LLDKKIGVNQ PKRIENAKIL IA NTGMDTD KIKIFGSRVR VDSTAKVAEI EHAEKEKMKE KVERILKHGI NCFINRQLIY NYPEQLFGAA GVMAIEHADF AGV ERLALV TGGEIASTFD HPELVKLGSC KLIEEVMIGE DKLIHFSGVA LGEACTIVLR GATQQILDEA ERSLHDALCV LAQT VKDSR TVYGGGCSEM LMAHAVTQLA NRTPGKEAVA MESYAKALRM LPTIIADNAG YDSADLVAQL RAAHSEGNTT AGLDM REGT IGDMAILGIT ESFQVKRQVL LSAAEAAEVI LRVDNIIKAA PRKRVPDHHP C

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Macromolecule #3: T-complex protein 1 subunit delta

MacromoleculeName: T-complex protein 1 subunit delta / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 57.996113 KDa
SequenceString: MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAAR MLVELSKAQD IEAGDGTTSV VIIAGSLLDS CTKLLQKGIH PTIISESFQK ALEKGIEILT DMSRPVELSD R ETLLNSAT ...String:
MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAAR MLVELSKAQD IEAGDGTTSV VIIAGSLLDS CTKLLQKGIH PTIISESFQK ALEKGIEILT DMSRPVELSD R ETLLNSAT TSLNSKVVSQ YSSLLSPMSV NAVMKVIDPA TATSVDLRDI KIVKKLGGTI DDCELVEGLV LTQKVSNSGI TR VEKAKIG LIQFCLSAPK TDMDNQIVVS DYAQMDRVLR EERAYILNLV KQIKKTGCNV LLIQKSILRD ALSDLALHFL NKM KIMVIK DIEREDIEFI CKTIGTKPVA HIDQFTADML GSAELAEEVN LNGSGKLLKI TGCASPGKTV TIVVRGSNKL VIEE AERSI HDALCVIRCL VKKRALIAGG GAPEIELALR LTEYSRTLSG MESYCVRAFA DAMEVIPSTL AENAGLNPIS TVTEL RNRH AQGEKTAGIN VRKGGISNIL EELVVQPLLV SVSALTLATE TVRSILKIDD VVNTR

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Macromolecule #4: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 59.749957 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAK LMVELSKSQD DEIGDGTTGV VVLAGALLEE AEQLLDRGIH PIRIADGYEQ AARVAIEHLD KISDSVLVDI K DTEPLIQT ...String:
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAK LMVELSKSQD DEIGDGTTGV VVLAGALLEE AEQLLDRGIH PIRIADGYEQ AARVAIEHLD KISDSVLVDI K DTEPLIQT AKTTLGSKVV NSCHRQMAEI AVNAVLTVAD MERRDVDFEL IKVEGKVGGR LEDTKLIKGV IVDKDFSHPQ MP KKVEDAK IAILTCPFEP PKPKTKHKLD VTSVEDYKAL QKYEKEKFEE MIQQIKETGA NLAICQWGFD DEANHLLLQN NLP AVRWVG GPEIELIAIA TGGRIVPRFS ELTAEKLGFA GLVQEISFGT TKDKMLVIEQ CKNSRAVTIF IRGGNKMIIE EAKR SLHDA LCVIRNLIRD NRVVYGGGAA EISCALAVSQ EADKCPTLEQ YAMRAFADAL EVIPMALSEN SGMNPIQTMT EVRAR QVKE MNPALGIDCL HKGTNDMKQQ HVIETLIGKK QQISLATQMV RMILKIDDIR KPGESEE

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Macromolecule #5: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 60.613855 KDa
SequenceString: MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDE EVGDGTTSVI ILAGEMLSVA EHFLEQQMHP TVVISAYRKA LDDMISTLKK ISIPVDISDS DMMLNIINSS I TTKAISRW ...String:
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDE EVGDGTTSVI ILAGEMLSVA EHFLEQQMHP TVVISAYRKA LDDMISTLKK ISIPVDISDS DMMLNIINSS I TTKAISRW SSLACNIALD AVKMVQFEEN GRKEIDIKKY ARVEKIPGGI IEDSCVLRGV MINKDVTHPR MRRYIKNPRI VL LDSSLEY KKGESQTDIE ITREEDFTRI LQMEEEYIQQ LCEDIIQLKP DVVITEKGIS DLAQHYLMRA NITAIRRVRK TDN NRIARA CGARIVSRPE ELREDDVGTG AGLLEIKKIG DEYFTFITDC KDPKACTILL RGASKEILSE VERNLQDAMQ VCRN VLLDP QLVPGGGASE MAVAHALTEK SKAMTGVEQW PYRAVAQALE VIPRTLIQNC GASTIRLLTS LRAKHTQENC ETWGV NGET GTLVDMKELG IWEPLAVKLQ TYKTAVETAV LLLRIDDIVS GHKKKGDDQS RQGGAPDAGQ E

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Macromolecule #6: T-complex protein 1 subunit eta

MacromoleculeName: T-complex protein 1 subunit eta / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 59.443535 KDa
SequenceString: MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI ...String:
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI SQQKAFFAKM VVDAVMMLDD LLQLKMIGIK KVQGGALEDS QLVAGVAFKK TFSYAGFEMQ PKKYHNPKIA LL NVELELK AEKDNAEIRV HTVEDYQAIV DAEWNILYDK LEKIHHSGAK VVLSKLPIGD VATQYFADRD MFCAGRVPEE DLK RTMMAC GGSIQTSVNA LSADVLGRCQ VFEETQIGGE RYNFFTGCPK AKTCTFILRG GAEQFMEETE RSLHDAIMIV RRAI KNDSV VAGGGAIEME LSKYLRDYSR TIPGKQQLLI GAYAKALEII PRQLCDNAGF DATNILNKLR ARHAQGGTWY GVDIN NEDI ADNFEAFVWE PAMVRINALT AASEAACLIV SVDETIKNPR STVDAPTAAG RGRGRGRPH

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Macromolecule #7: Nanobody

MacromoleculeName: Nanobody / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Lama glama (llama)
Molecular weightTheoretical: 14.412816 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
QVQLVESGGG LVQAGGSLRL SCGASGTFFR INDMGWYRQA SGKQRELVAS ITRGGTTDYA DSVKGRFTIS RDNAKNTVYL QMNSLKPED TAVYYCKANR NWGREWDDYW GQGTQVTVSS HHHHHHEPEA

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Macromolecule #8: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 59.691422 KDa
SequenceString: MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMA SHMQEQEVGD GTNFVLVFAG ALLELAEELL RIGLSVSEVI EGYEIACRKA HEILPNLVCC SAKNLRDIDE V SSLLRTSI ...String:
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMA SHMQEQEVGD GTNFVLVFAG ALLELAEELL RIGLSVSEVI EGYEIACRKA HEILPNLVCC SAKNLRDIDE V SSLLRTSI MSKQYGNEVF LAKLIAQACV SIFPDSGHFN VDNIRVCKIL GSGISSSSVL HGMVFKKETE GDVTSVKDAK IA VYSCPFD GMITETKGTV LIKTAEELMN FSKGEENLMD AQVKAIADTG ANVVVTGGKV ADMALHYANK YNIMLVRLNS KWD LRRLCK TVGATALPRL TPPVLEEMGH CDSVYLSEVG DTQVVVFKHE KEDGAISTIV LRGSTDNLMD DIERAVDDGV NTFK VLTRD KRLVPGGGAT EIELAKQITS YGETCPGLEQ YAIKKFAEAF EAIPRALAEN SGVKANEVIS KLYAVHQEGN KNVGL DIEA EVPAVKDMLE AGILDTYLGK YWAIKLATNA AVTVLRVDQI IMAKPAGGPK PPSGKKDWDD DQND

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Macromolecule #9: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 58.106086 KDa
SequenceString: MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL ...String:
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL TEAVVDSILA IKKQDEPIDL FMIEIMEMKH KSETDTSLIR GLVLDHGARH PDMKKRVEDA YILTCNVSLE YE KTEVNSG FFYKSAEERE KLVKAERKFI EDRVKKIIEL KRKVCGDSDK GFVVINQKGI DPFSLDALSK EGIVALRRAK RRN MERLTL ACGGVALNSF DDLSPDCLGH AGLVYEYTLG EEKFTFIEKC NNPRSVTLLI KGPNKHTLTQ IKDAVRDGLR AVKN AIDDG CVVPGAGAVE VAMAEALIKH KPSVKGRAQL GVQAFADALL IIPKVLAQNS GFDLQETLVK IQAEHSESGQ LVGVD LNTG EPMVAAEVGV WDNYCVKKQL LHSCTVIATN ILLVDEIMRA GMSSLKG

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Macromolecule #10: Tubulin beta-2A chain

MacromoleculeName: Tubulin beta-2A chain / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 49.92173 KDa
SequenceString: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS ...String:
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS VHQLVENTDE TYSIDNEALY DICFRTLKLT TPTYGDLNHL VSATMSGVTT CL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTSRG SQQYRALTVP ELTQQMFDSK NMMAACDPRH GRYLTVAAIF RGR MSMKEV DEQMLNVQNK NSSYFVEWIP NNVKTAVCDI PPRGLKMSAT FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDATADEQGE FEEEEGEDEA

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Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 16 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Macromolecule #12: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 12 / Number of copies: 16 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #13: ALUMINUM FLUORIDE

MacromoleculeName: ALUMINUM FLUORIDE / type: ligand / ID: 13 / Number of copies: 16 / Formula: AF3
Molecular weightTheoretical: 83.977 Da
Chemical component information

ChemComp-AF3:
ALUMINUM FLUORIDE

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Macromolecule #14: water

MacromoleculeName: water / type: ligand / ID: 14 / Number of copies: 19 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 43.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 93758
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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