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- EMDB-66028: Tti1-Telo2 complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-66028
TitleTti1-Telo2 complex
Map data
Sample
  • Complex: Tti1-Telo2
    • Protein or peptide: Tti1
    • Protein or peptide: Telomere length regulation protein TEL2 homolog
KeywordsTti1 / Telo2 / CRYO-EM / TTT / CHAPERONE
Function / homology
Function and homology information


protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / telomeric repeat DNA binding / Hsp90 protein binding / kinase binding / molecular adaptor activity / nuclear body / chromosome, telomeric region / protein stabilization ...protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / telomeric repeat DNA binding / Hsp90 protein binding / kinase binding / molecular adaptor activity / nuclear body / chromosome, telomeric region / protein stabilization / protein kinase binding / protein-containing complex binding / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
: / TELO2 ARM repeat domain / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / : / Telomere length regulation protein / Armadillo-type fold
Similarity search - Domain/homology
Telomere length regulation protein TEL2 homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.83 Å
AuthorsQin Y / Wang P / Xu G
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: GNB1L Chaperone Activity Licenses SAGA-Mediated Immune Evasion in Tumors
Authors: Qin Y / Xu G
History
DepositionAug 31, 2025-
Header (metadata) releaseSep 2, 2026-
Map releaseSep 2, 2026-
UpdateSep 2, 2026-
Current statusSep 2, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_66028.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.)
1.07 Å/pix.
x 400 pix.
= 428. Å
1.07 Å/pix.
x 400 pix.
= 428. Å
1.07 Å/pix.
x 400 pix.
= 428. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.16
Minimum - Maximum-6.3489337 - 5.544168
Average (Standard dev.)0.00038334957 (±0.025369326)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 428.00003 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_66028_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_66028_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Tti1-Telo2

EntireName: Tti1-Telo2
Components
  • Complex: Tti1-Telo2
    • Protein or peptide: Tti1
    • Protein or peptide: Telomere length regulation protein TEL2 homolog

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Supramolecule #1: Tti1-Telo2

SupramoleculeName: Tti1-Telo2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Tti1

MacromoleculeName: Tti1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 82.665156 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: ELEQKQLGDL FASFLPGIST ALTRLITGDF KQGHSIVVSS LKIFYKTVSF IMADEQLKRI SKMVYREADW VKKTGDKLTI LIKKIIECV SVHPHWKVRL ELVELVEDLL LKCSQSLVEC AGPLLKALVG LVNDESPEIQ AQCNKVLRHF ADQKVVVGNK A LADILSES ...String:
ELEQKQLGDL FASFLPGIST ALTRLITGDF KQGHSIVVSS LKIFYKTVSF IMADEQLKRI SKMVYREADW VKKTGDKLTI LIKKIIECV SVHPHWKVRL ELVELVEDLL LKCSQSLVEC AGPLLKALVG LVNDESPEIQ AQCNKVLRHF ADQKVVVGNK A LADILSES LHSLATSLPR LMNSQDDQGK FSTLSLLLGY LKLLGPKINF VLNSVAHLQR LSKALIQVLE LDVADIKIVE ER RWNSDDL NASPKTSATQ PWNRIQRRYF RFFTDERIFM LLRQVCQLLG YYGNLYLLVD HFMELYHQSV VYRKQAAMIL NEL VTGAAG LEVEDLHEKH IKTNPEELRE IVTSILEEYT SQENWYLVTC NSNIWQICIQ LEGIGQFAYA LGKDFCLLLM SALY PVLEK AGDQTLLISQ VATSTMMDVC RACGYDSLQH LINQNSDYLV NGISLNLRHL ALHPHTPKVL EVMLRNSDAN LLPLV ADVV QDVLATLDQF YDKRAASFVS VLHALMAALA QWFPDLQIQI AMDVMERCIH LLSDKNLQIR LKVLDVLDLC VVVLQS HKN QLLPLAHQAW PSLVHRLTRD APLAVLRAFK VLRTLGSKCG DFLRSRFCKD VLPKLAGSLV TQAPISARAG PVYSHTL AF KLQLAVLQGL GPLCERLDLG EGDLNKVADA CLIYLSVKQP VKLQEAARSV FLHLMKVDPD STWFLLNELH GASGQQNP Y TTNVLQLLKE LQ

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Macromolecule #2: Telomere length regulation protein TEL2 homolog

MacromoleculeName: Telomere length regulation protein TEL2 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.705742 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: EVRLAVREAI HALSSSEDGG HIFCTLESLK RYLGEMEPPA LPREKEEFAS AHFSPVLRCL ASRLSPAWLE LLPHGRLEEL WASFFLEGP ADQAFLVLME TIEGAAGPSF RLMKMARLLA RFLREGRLAV LMEAQCRQQT QPGFILLRET LLGKVVALPD H LGNRLQQE ...String:
EVRLAVREAI HALSSSEDGG HIFCTLESLK RYLGEMEPPA LPREKEEFAS AHFSPVLRCL ASRLSPAWLE LLPHGRLEEL WASFFLEGP ADQAFLVLME TIEGAAGPSF RLMKMARLLA RFLREGRLAV LMEAQCRQQT QPGFILLRET LLGKVVALPD H LGNRLQQE NLAEFFPQNY FRLLGEEVVR VLQAVVDSLQ GGLDSSVSFV SQVLGKACVH GRQQEILGVL VPRLAALTQG SY LHQRVCW RLVEQVPDRA MEAVLTGLVE AALGPEVLSR LLGNLVVKNK KAQFVMTQKL LFLQSRLTTP MLQSLLGHLA MDS QRRPLL LQVLKELLET WGSSSAIRHT PLPQQRHVSK AVLICLAQLG EPELRDSRDE LLASMMAGVK CRLDSSLPPV RRLG MIVAE VVSARIHPEG PPLKFQYEED ELSLELLALA SP

UniProtKB: Telomere length regulation protein TEL2 homolog

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statecell

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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 K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.83 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 287635
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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