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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Hetero-hexameric Hsp70-Hsp40-DafA complex | |||||||||
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Sample |
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Keywords | Chaperone / Hsp70 / Hsp40 / protein folding | |||||||||
| Function / homology | Function and homology informationATP-dependent protein folding chaperone / unfolded protein binding / protein refolding / DNA replication / ATP binding / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() Thermus thermophilus (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.37 Å | |||||||||
Authors | Ibrahim Z / Kalodimos C | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: To Be PublishedTitle: hetero-hexameric Hsp70-Hsp40-DafA complex Authors: Ibrahim Z / Kalodimos C | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_47203.map.gz | 59.6 MB | EMDB map data format | |
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| Header (meta data) | emd-47203-v30.xml emd-47203.xml | 16.8 KB 16.8 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_47203_fsc.xml | 11.7 KB | Display | FSC data file |
| Images | emd_47203.png | 52 KB | ||
| Masks | emd_47203_msk_1.map | 64 MB | Mask map | |
| Filedesc metadata | emd-47203.cif.gz | 5.6 KB | ||
| Others | emd_47203_half_map_1.map.gz emd_47203_half_map_2.map.gz | 59.3 MB 59.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-47203 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-47203 | HTTPS FTP |
-Validation report
| Summary document | emd_47203_validation.pdf.gz | 791.6 KB | Display | EMDB validaton report |
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| Full document | emd_47203_full_validation.pdf.gz | 791.4 KB | Display | |
| Data in XML | emd_47203_validation.xml.gz | 15.7 KB | Display | |
| Data in CIF | emd_47203_validation.cif.gz | 21.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47203 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-47203 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9dviMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_47203.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.652 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_47203_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_47203_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_47203_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : hetero-hexameric Hsp70-Hsp40-DafA complex
| Entire | Name: hetero-hexameric Hsp70-Hsp40-DafA complex |
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| Components |
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-Supramolecule #1: hetero-hexameric Hsp70-Hsp40-DafA complex
| Supramolecule | Name: hetero-hexameric Hsp70-Hsp40-DafA complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: it is a heterohexameric complex containing two copies of each of the chaperone proteins: Hsp70, Hsp40 and DafA |
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| Source (natural) | Organism: ![]() Thermus thermophilus (bacteria) |
| Molecular weight | Theoretical: 211.1 KDa |
-Macromolecule #1: Hsp70-Hsp40-DafA
| Macromolecule | Name: Hsp70-Hsp40-DafA / type: protein_or_peptide / ID: 1 Details: it is a heterohexameric complex containing two copies of each of the proteins: Hsp70, Hsp40 and DafA Enantiomer: DEXTRO |
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| Source (natural) | Organism: ![]() Thermus thermophilus (bacteria) |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAKAVGIDLG TTNSVIAVLE GGKPVVLENA EGERVTPSVV AFRDGETLVG RMAKRQAVLN PEGTIFEIKR FIGRRFEEVQ EEAKRVPYKV VPGPDGGVRV EVKGKLYTPE EISAMILRKL VEDASKKLGE KITKAVITVP AYFNNAQREA TANAGRIAGL EVLRIINEPT ...String: MAKAVGIDLG TTNSVIAVLE GGKPVVLENA EGERVTPSVV AFRDGETLVG RMAKRQAVLN PEGTIFEIKR FIGRRFEEVQ EEAKRVPYKV VPGPDGGVRV EVKGKLYTPE EISAMILRKL VEDASKKLGE KITKAVITVP AYFNNAQREA TANAGRIAGL EVLRIINEPT AAALAYGLDK KGNETVLVFD LGGGTFDVTI LEIGEGVFEV KATSGDTHLG GSDMDHAIVN WLAEEFKKEH GVDLKADRQA LQRLIEAAEK AKIELSSTLE TTISLPFIAL DPASKTPLHL EKKLTRAKFE ELIQPLLKRL RGPVEQALKD AGLTPAQIDE VILVGGATRV PAVQQVVREL LGKEPNRSVN PDEVVAMGAA IQAGVLMGEV RDVVLLDVTP LSLGVETKGG VMTVLIPRNT TIPTRKCEIF TTAEHNQTAV EIHVLQGERP MAQDNKSLGR FRLEGIPPMP AGVPQIEVCF DIDANGILHV TAKERSTGRE ASITIQNTTT LSEEEIQRII EEAKRHAEED RRRREHAELK NALDSARVQA ERVLQERQGA PEARARLEAA IGKAKELVER DAPDPELKAA TEELLKAVEE YEKGAQAASG KGPDDVIDAD YKPAD MAAK KDYYAILGVP RNATQEEIKR AYKRLARQYH PDVNKSPEAE EKFKEINEAY AVLSDPEKRR IYDTYGTTEA PPPPPPGGYD FSGFDVEDFS EFFQELFGPG LFGGFGRRSR KGRDLRAELP LTLEEAFHGG ERVVEVAGRR VSVRIPPGVR EGSVIRVPGM GGQGNPPGDL LLVVRLLPHP VFRLEGQDLY ATLDVPAPIA VVGGKVRAMT LEGPVEVAVP PRTQAGRKLR LKGKGFPGPA GRGDLYLEVR ITIPERLTPE EEALWKKLAE AYYARA MLA RSGWLSLEAL SEYGLSLAAV RAYVEIGFVE PLEVGGAWYF REEDLLRMAK AERIRKDLGA NLIGAALVVE ILERT UniProtKB: Chaperone protein DnaK |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.1 mg/mL |
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| Buffer | pH: 7.5 / Details: 50 mM HEPES, 75 mM NaCl at pH 7.5 |
| Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 60 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
| Details | Gradient Fixation method was used to stabilize the Hsp70-Hsp40-DafA complex for single particle cryoEM |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 77.8 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 5.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Thermus thermophilus (bacteria)
Authors
United States, 2 items
Citation





Z (Sec.)
Y (Row.)
X (Col.)












































Processing
FIELD EMISSION GUN

