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Yorodumi- EMDB-39454: structure of phage T6 full-length topoisomerase II bound with DNA -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-39454 | |||||||||
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Title | structure of phage T6 full-length topoisomerase II bound with DNA | |||||||||
Map data | T6 Topoisomerase II full-length bound with DNA map | |||||||||
Sample |
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Keywords | topoisomerase II / ISOMERASE | |||||||||
Function / homology | Function and homology information sister chromatid segregation / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / protein-containing complex / DNA binding / ATP binding Similarity search - Function | |||||||||
Biological species | Enterobacteria phage T6 (virus) / Escherichia phage T4 (virus) / DNA molecule (others) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.73 Å | |||||||||
Authors | Chen YT / Xin YH / Xian RQ | |||||||||
Funding support | China, 1 items
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Citation | Journal: To be published Title: structure of phage T6 full-length topoisomerase II bound with DNA Authors: Chen YT / Xin YH / Xian RQ | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_39454.map.gz | 97.1 MB | EMDB map data format | |
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Header (meta data) | emd-39454-v30.xml emd-39454.xml | 16.8 KB 16.8 KB | Display Display | EMDB header |
Images | emd_39454.png | 63.8 KB | ||
Filedesc metadata | emd-39454.cif.gz | 6.1 KB | ||
Others | emd_39454_half_map_1.map.gz emd_39454_half_map_2.map.gz | 95.5 MB 95.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39454 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39454 | HTTPS FTP |
-Validation report
Summary document | emd_39454_validation.pdf.gz | 904.6 KB | Display | EMDB validaton report |
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Full document | emd_39454_full_validation.pdf.gz | 904.1 KB | Display | |
Data in XML | emd_39454_validation.xml.gz | 13.4 KB | Display | |
Data in CIF | emd_39454_validation.cif.gz | 15.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39454 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-39454 | HTTPS FTP |
-Related structure data
Related structure data | 8yonMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_39454.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | T6 Topoisomerase II full-length bound with DNA map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: T6 Topoisomerase II full-length bound with DNA half map
File | emd_39454_half_map_1.map | ||||||||||||
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Annotation | T6 Topoisomerase II full-length bound with DNA half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: T6 Topoisomerase II full-length bound with DNA half map
File | emd_39454_half_map_2.map | ||||||||||||
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Annotation | T6 Topoisomerase II full-length bound with DNA half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Phage T6 full-length topoisomerase II bound with DNA
Entire | Name: Phage T6 full-length topoisomerase II bound with DNA |
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Components |
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-Supramolecule #1: Phage T6 full-length topoisomerase II bound with DNA
Supramolecule | Name: Phage T6 full-length topoisomerase II bound with DNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: Enterobacteria phage T6 (virus) |
-Macromolecule #1: DNA topoisomerase medium subunit
Macromolecule | Name: DNA topoisomerase medium subunit / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: DNA topoisomerase (ATP-hydrolysing) |
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Source (natural) | Organism: Escherichia phage T4 (virus) |
Molecular weight | Theoretical: 51.951973 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MQLNNRDLKS IIDNEALAYA MYTVENRAIP NMIDGFKPVQ RFVIARALDL ARGNKDKFHK LASIAGGVAD LGYHHGENSA QDAGALMAN TWNNNFPLLD GQGNFGSRTV QKAAASRYIF ARVSKNFYNV YKDTEYAPVH QDKEHIPPAF YLPIIPTVLL N GVSGIATG ...String: MQLNNRDLKS IIDNEALAYA MYTVENRAIP NMIDGFKPVQ RFVIARALDL ARGNKDKFHK LASIAGGVAD LGYHHGENSA QDAGALMAN TWNNNFPLLD GQGNFGSRTV QKAAASRYIF ARVSKNFYNV YKDTEYAPVH QDKEHIPPAF YLPIIPTVLL N GVSGIATG YATYILPHSV SSVKKAVLQA LQGKKVTKPK VEFPEFRGEV VEIDGQYEIR GTYKFTSRTQ MHITEIPYKY DR ETYVSKI LDPLENKGFI TWDDACGEHG FGFKVKFRKE YSLSDNEEER HAKIMKDFGL IERRSQNITV INEKGKLQVY DNV VDLIKD FVEVRKTYVQ KRIDNKIKET ESAFRLAFAK AHFIKKVISG EIVVQGKTRK ELTEELSKID MYSSYVDKLV GMNI FHMTS DEAKKLAEEA KAKKEENEYW KTTDVVTEYT KDLEEIKHHH HHHHHHH UniProtKB: DNA topoisomerase medium subunit |
-Macromolecule #2: DNA topoisomerase (ATP-hydrolyzing)
Macromolecule | Name: DNA topoisomerase (ATP-hydrolyzing) / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: DNA topoisomerase (ATP-hydrolysing) |
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Source (natural) | Organism: Enterobacteria phage T6 (virus) |
Molecular weight | Theoretical: 69.237289 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MIKNEIKILS DIEHIKKRSG MYIGSSANEM HERFLFGKWE SVQYVPGLVK LIDEIIDNSV DEGIRTKFKF ANKINVTIKN NQVTVEDNG RGIPQAMVKT PTGEEIPGPV AAWTIPKAGG NFGDDKERVT GGMNGVGSSL TNIFSVMFVG ETGDGQNNIV V RCSNGMEN ...String: MIKNEIKILS DIEHIKKRSG MYIGSSANEM HERFLFGKWE SVQYVPGLVK LIDEIIDNSV DEGIRTKFKF ANKINVTIKN NQVTVEDNG RGIPQAMVKT PTGEEIPGPV AAWTIPKAGG NFGDDKERVT GGMNGVGSSL TNIFSVMFVG ETGDGQNNIV V RCSNGMEN KSWETIPGKW KGTRVTFIPD FMSFETNELS QVYLDITLDR LQTLAVVYPD IQFTFNGKKV QGNFKKYARQ YD EHAIVQE QENCSIAVGR SPDGFRQLTY VNNIHTKNGG HHIDCVMDDI CEDLIPQIKR KFKIDVTKAR VKECLTIVMF VRD MKNMRF DSQTKERLTS PFGEIRSHIQ LDAKKISRAI LNNEAILMPI IEAALARKLA AEKAAETKAA KKASKAKVHK HIKA NLCGK DADTTLFLTE GDSAIGYLID VRDKELHGGY PLRGKVLNSW GMSYADMLKN KELFDICAIT GLVLGEKAEN LNYHN IAIM TDADHDGLGS IYPSLLGFFS NWPELFEQGR IRFVKTPVII AHVGKKQEWF YTVAEYESAK DALPKHSIRY IKGLGS LEK SEYREMIQNP VYDVVKLPEN WKELFEMLMG DNADLRKEWM SQHHHHHH UniProtKB: DNA topoisomerase (ATP-hydrolyzing) |
-Macromolecule #3: DNA (50-MER)
Macromolecule | Name: DNA (50-MER) / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: DNA molecule (others) |
Molecular weight | Theoretical: 16.058391 KDa |
Sequence | String: (DA)(DT)(DG)(DC)(DA)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DG)(DT)(DA)(DT)(DA)(DT)(DG)(DT) (DA)(DT)(DG)(DT)(DG)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DA)(DC)(DA)(DC)(DA) (DT) (DA)(DT)(DA)(DT)(DA)(DT) ...String: (DA)(DT)(DG)(DC)(DA)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DG)(DT)(DA)(DT)(DA)(DT)(DG)(DT) (DA)(DT)(DG)(DT)(DG)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DA)(DC)(DA)(DC)(DA) (DT) (DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DA)(DT) |
-Macromolecule #4: DNA (50-MER)
Macromolecule | Name: DNA (50-MER) / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: DNA molecule (others) |
Molecular weight | Theoretical: 15.965361 KDa |
Sequence | String: (DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DA)(DT)(DG)(DT)(DG)(DT)(DA)(DT) (DA)(DT)(DA)(DT)(DA)(DC)(DA)(DC)(DA) (DC)(DA)(DT)(DA)(DC)(DA)(DT)(DA)(DT)(DA) (DC) (DA)(DT)(DA)(DT)(DA)(DT) ...String: (DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DA)(DT)(DG)(DT)(DG)(DT)(DA)(DT) (DA)(DT)(DA)(DT)(DA)(DC)(DA)(DC)(DA) (DC)(DA)(DT)(DA)(DC)(DA)(DT)(DA)(DT)(DA) (DC) (DA)(DT)(DA)(DT)(DA)(DT)(DA)(DT) (DG)(DC)(DA)(DT) |
-Macromolecule #5: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 5 / Number of copies: 2 / Formula: ANP |
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Molecular weight | Theoretical: 506.196 Da |
Chemical component information | ChemComp-ANP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 6 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination 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 |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.73 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 11206 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |