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- EMDB-66034: Tti2-Tti1-C -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-66034
TitleTti2-Tti1-C
Map data
Sample
  • Complex: Tti1-Tti2 complex
    • Protein or peptide: TELO2-interacting protein 1 homolog
    • Protein or peptide: TELO2-interacting protein 2
KeywordsTti1 / Tti2 / TTT / CHAPERONE
Function / homology
Function and homology information


protein-containing complex stabilizing activity / positive regulation of DNA damage checkpoint / TTT Hsp90 cochaperone complex / TORC2 complex / TORC1 complex / regulation of TOR signaling / kinase binding / protein stabilization / nucleus / cytoplasm
Similarity search - Function
Tti2 family / Tti2 family / TEL2-interacting protein 1 / : / : / : / : / TELO2-interacting protein 1 / TTI1 N-terminal TPR domain / TELO2-interacting protein 1 homologue second TPR domain ...Tti2 family / Tti2 family / TEL2-interacting protein 1 / : / : / : / : / TELO2-interacting protein 1 / TTI1 N-terminal TPR domain / TELO2-interacting protein 1 homologue second TPR domain / TTI1 C-terminal TPR domain / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
TELO2-interacting protein 1 homolog / TELO2-interacting protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsQin Y / 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

emd_66034.png

Downloads & links

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Map

FileDownload / File: emd_66034.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

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.37
Minimum - Maximum-2.29593 - 6.547174
Average (Standard dev.)-0.0009987348 (±0.04198065)
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_66034_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_66034_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Tti1-Tti2 complex

EntireName: Tti1-Tti2 complex
Components
  • Complex: Tti1-Tti2 complex
    • Protein or peptide: TELO2-interacting protein 1 homolog
    • Protein or peptide: TELO2-interacting protein 2

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Supramolecule #1: Tti1-Tti2 complex

SupramoleculeName: Tti1-Tti2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: TELO2-interacting protein 1 homolog

MacromoleculeName: TELO2-interacting protein 1 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.620535 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: DQTLLISQVA TSTMMDVCRA CGYDSLQHLI NQNSDYLVNG ISLNLRHLAL HPHTPKVLEV MLRNSDANLL PLVADVVQDV LATLDQFYD KRAASFVSVL HALMAALAQW FPDTGNLGHL QEQSLGEEGS HLNQRPAALE KSTTTAEDIE QFLLNYLKEK D VADGNVSD ...String:
DQTLLISQVA TSTMMDVCRA CGYDSLQHLI NQNSDYLVNG ISLNLRHLAL HPHTPKVLEV MLRNSDANLL PLVADVVQDV LATLDQFYD KRAASFVSVL HALMAALAQW FPDTGNLGHL QEQSLGEEGS HLNQRPAALE KSTTTAEDIE QFLLNYLKEK D VADGNVSD FDNEEEEQSV PPKVDENDTR PDVEPPLPLQ IQIAMDVMER CIHLLSDKNL QIRLKVLDVL DLCVVVLQSH KN QLLPLAH QAWPSLVHRL TRDAPLAVLR AFKVLRTLGS KCGDFLRSRF CKDVLPKLAG SLVTQAPISA RAGPVYSHTL AFK LQLAVL QGLGPLCERL DLGEGDLNKV ADACLIYLSV KQPVKLQEAA RSVFLHLMKV DPDSTWFLLN ELYCPVQFTP PHPS LHPVQ LHGASGQQNP YTTNVLQLLK ELQ

UniProtKB: TELO2-interacting protein 1 homolog

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Macromolecule #2: TELO2-interacting protein 2

MacromoleculeName: TELO2-interacting protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.948457 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: ELSHSAFGQA FSKILHCLAR PEARRGNVKD AVLKDLGDLI EATEFDRLFE GTGARLRGMP ETLGQVAKAL EKYAAPSKEE EGGGDGHSE AAEKAAQVGL LFLKLLGKVE TAKNSLVGPA WQTGLHHLAG PVYIFAITHS LEQPWTTPRS REVAREVLTS L LQVTECGS ...String:
ELSHSAFGQA FSKILHCLAR PEARRGNVKD AVLKDLGDLI EATEFDRLFE GTGARLRGMP ETLGQVAKAL EKYAAPSKEE EGGGDGHSE AAEKAAQVGL LFLKLLGKVE TAKNSLVGPA WQTGLHHLAG PVYIFAITHS LEQPWTTPRS REVAREVLTS L LQVTECGS VAGFLHGENE DEKGRLSVIL GLLKPDLYKE SWKNNPAIKH VFSWTLQQVT RPWLSQHLER VLPASLVISD DY QTENKIL GVHCLHHIVL NVPAADLLQY NRAQVLYHAI SNHLYTPEHH LIQAVLLCLL DLFPILEKTL HWKGDGARPT THC DEVLRL ILTHMEPEHR LLLRRTYARN LPAFVNRLGI LTVRHLKRLE RVIIGYLEVY DGPEEEARLK ILETLKLLMQ HTWP RVSCR LVVLLKALLK LICDVARDPN LTPESVKSAL LQEATDCLIL LDRCSQGRVK GLLAKIPQSC EDRKVVNYIR KVQQV SEGA PYNGT

UniProtKB: TELO2-interacting protein 2

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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 BIOCONTINUUM (6k x 4k) / Average electron dose: 300.0 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: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 107543
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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