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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Yeast Blm10 apo Structure | |||||||||
Map data | Final Sharpened Map Blm10 | |||||||||
Sample |
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Keywords | Proteasome Regulator / PROTEIN BINDING | |||||||||
| Function / homology | Function and homology informationproteasome core complex import into nucleus / proteasome storage granule assembly / peptidase activator activity / proteasome binding / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / proteasome assembly / regulation of proteasomal protein catabolic process / DNA repair / DNA damage response ...proteasome core complex import into nucleus / proteasome storage granule assembly / peptidase activator activity / proteasome binding / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / proteasome assembly / regulation of proteasomal protein catabolic process / DNA repair / DNA damage response / nucleus / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Walsh Jr RM / Rawson S / Fermin Perez E / Venclovaite U / Hanna J | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: To Be PublishedTitle: Blm10 and PI31 Compromise a Failsafe Mechanism for Proteasome Inhibition Authors: Darlene F / Rawson S / Walsh Jr RM / Fermin Perez E / Venclovaite U / Velez B / Rajakumar T / Hanna J | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_75163.map.gz | 11.1 MB | EMDB map data format | |
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| Header (meta data) | emd-75163-v30.xml emd-75163.xml | 25.3 KB 25.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_75163_fsc.xml | 11.3 KB | Display | FSC data file |
| Images | emd_75163.png | 79.4 KB | ||
| Filedesc metadata | emd-75163.cif.gz | 8 KB | ||
| Others | emd_75163_additional_1.map.gz emd_75163_half_map_1.map.gz emd_75163_half_map_2.map.gz | 116.2 MB 98.5 MB 98.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-75163 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-75163 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 10gxMC ![]() 10mtC ![]() 10ogC ![]() 10qtC ![]() 10sjC 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_75163.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Final Sharpened Map Blm10 | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.19 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Final Unsharpened Map Blm10
| File | emd_75163_additional_1.map | ||||||||||||
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| Annotation | Final Unsharpened Map Blm10 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half Map1 Blm10
| File | emd_75163_half_map_1.map | ||||||||||||
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| Annotation | Half Map1 Blm10 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half Map2 Blm10
| File | emd_75163_half_map_2.map | ||||||||||||
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| Annotation | Half Map2 Blm10 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Apo Blm10
| Entire | Name: Apo Blm10 |
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| Components |
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-Supramolecule #1: Apo Blm10
| Supramolecule | Name: Apo Blm10 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 240 KDa |
-Macromolecule #1: Proteasome activator BLM10
| Macromolecule | Name: Proteasome activator BLM10 / type: protein_or_peptide / ID: 1 Details: First 24 residues "MHHHHHHHHHHHHTANNDDDIKSP" are part of Histdine tag and linker sequence Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 249.243672 KDa |
| Sequence | String: MHHHHHHHHH HHHTANNDDD IKSPMTANND DDIKSPIPIT NKTLSQLKRF ERSPGRPSSS QGEIKRKKSR LYAADGRPHS PLRARSATP TLQDQKLFNG MDSTSLLNER LQHYTLDYVS DRAQHMKNIY DPSSRWFSRS VRPEFPIEEF LPYKTESHED Q AKYLCHVL ...String: MHHHHHHHHH HHHTANNDDD IKSPMTANND DDIKSPIPIT NKTLSQLKRF ERSPGRPSSS QGEIKRKKSR LYAADGRPHS PLRARSATP TLQDQKLFNG MDSTSLLNER LQHYTLDYVS DRAQHMKNIY DPSSRWFSRS VRPEFPIEEF LPYKTESHED Q AKYLCHVL VNLYIAISSL DIQGLISISS KDLADLKKEV DDLALKTDLF RLSNNTAEND LLGNDIADYD DAEGLEDELD EY FDLAGPD FNATGKITAK SATIVNVNHW TNELKNCLHF DFPVALRKSL ATVYYYLSLV QGQKVYRQMH VDMFERLVSL DDD RTNFTE LLQKQGLLLD HQIMLNFLCE FLPYPDPDYA RYELSSKEDL QLFRLLLKHA HNAKPFFDKS KESLLVDTMN FLLS SLAPS TMMAVMPIVT SVVPYHYHIH SKIIDYFPFC YSIWSSVSAN VAIDTHMYDF VGSISKDVHN KILSSEHEKD VVGVE FGEF GIFTDDQMTF MFNRLQGHLR TDGQIHSYSR TVKPFVYAIN GSKKDRFFEK LVSLAKAIET FIHPSNNGFW TKPNAK FVH AFIKSYHGRV KYEEDICARG VTNGICLTSF CHEEIVEIFL NIISLGSQNK NPDIANYYIS CFAYLLELDP SNAYLIY DK ILIDLYDTLA DQFINSRHRI ISSLKQFTRV IRFIVMDKLY RVHITNVLSM LVSKLDMNDT NLTSNLINGI VSIAAFIP I QDLTGEDDYI SFESDTLPLV QQHFYHIKCG ESSKTFRVDD ELLNNAFKAS TTVFQSMLKV YVEKIFQLVD VDLEDSLVT KINQTTMILQ ESMDDKIFNY FASLLQRNFW SNDSFKEKDP NYELVTIPLA ALVRRNNGLS KELVRTLLFH IKEQIKRGAG SVRSTSEIQ QRDVKLVLYL TALNDVLRQC HESLLEYSDE LITFMKYLYD NVTNPPLDVI TSIVIHSALA TLCTTEITDC R LFPEDSKI PEKDRWGGLQ FDPRRFDKQH LSFQWHVPSS DEITLSISIL ESLSEYCINN VEELMKAPRH DSEYGDMIQK YV LVMTHTL SGSSLLFDPD FNKYRTQSNL SYREKLILLK NIRENNCDPQ ELDIDIEQIR SGKDDEDYIE SKDIEAGLNA GVS DVVQLR DEFPDELIVD EEVVSEMPSG VNTPIAGTHG TDNSAMSSDL AFRDLDIYTC NYYFGNTTEE KLQNPQYLQV HRVR ARIGH FFHKLYVFLS TNFENNTNMF QILLHGLKVW FTDLGQETVF NEDPNAFIDV DFLENVQSLS HVNEPFTRTN FAIRA NSLH QSRVLLHSTN RKASKLENLL LVDIIQLATS LYPDIYKPAQ GTLVHCMKQL VGSYGVVINK IIPSLEKAIK DHDYMK IQV ILNVLLIKKI HRKLMTDYKD IGRLIFLLIE CCRVNELEIG MYADKILTDI VIGIKIPSSV CVISDQAFLP LAPPDGT IN LQVEAVKLAK KKKREYYLSL LVDLQDKLLD KLDNEKDMGW KIRMFILRFV TQIQSNLESK PDKRAVFSII SQISTKHP E IIHLVVKSLL STCNKIISLS DYEYDITRAY KNEFNPSFVE ILDTSTTSFP KTFTEEMNNF DNPKYFIDLR AYVGWLCWG RLMYVMSPKA LKLNLRENEL EVLKTAGHLL TREFLRDVTM NLVQDNETRG VFSSGNVSFF SLVILLISSG FCELNMSDLF ELCESYYNK DDKASMIMSV EIVAGLVCGS KFMSVSDLDK RDTFIENFLA KCLDYELNHD AFEIWSTLAW WLPAVVDLRR S KTFFCHFI NADGMFDRES DAATHQTSKI YMLRSILMSM EFRAPDVGKL FDELVFDHPY DQVRQAVAKL LTTLVQNQSN PS ISDPTTL LEAERNDPDG LGLPLKSVPE KVDAYIKKQF EIIKNLEDSV VGLNPQQFIK TDYFYRTSTI FYWIKEMARG PNK VLLVPY LVDYVLPFLI GLVKHKDVCA LASLDPVRLY AGLGYMPIRK NHVAAIVDYV CSSNVALSSN QTKLQLAFIQ HFLS AELLQ LTEEEKNKIL EFVVSNLYNE QFVEVRVRAA SILSDIVHNW KEEQPLLSLI ERFAKGLDVN KYTSKERQKL SKTDI KIHG NVLGLGAIIS AFPYVFPLPP WIPKQLSNLS SWARTSGMTG QAAKNTISEF KKVRADTWKF DRASFNTEEL EDLEGV LWR SYYA UniProtKB: Proteasome activator BLM10 |
-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 | 1 mg/mL | ||||||||||||
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| Buffer | pH: 7.5 Component:
Details: Sample was mixed with RvLEAMshort peptide to a final concentration of 1mg/ml sample and 30 micromolar RvLEAMshort immediately before preparation. | ||||||||||||
| Grid | Model: Quantifoil / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295.15 K / Instrument: FEI VITROBOT MARK IV Details: wait time of 8 s, blot time of 12 s and a blot force of 8. | ||||||||||||
| Details | Sample was mixed with RvLEAMshort peptide to a final concentration of 1mg/ml sample and 30 micromolar RvLEAMshort immediately before preparation. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV |
| Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: TFS FALCON 4i (4k x 4k) / #0 - Digitization - Dimensions - Width: 4096 pixel / #0 - Digitization - Dimensions - Height: 4096 pixel / #0 - Number grids imaged: 1 / #0 - Number real images: 11278 / #0 - Average exposure time: 6.32 sec. / #0 - Average electron dose: 50.253 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: FEI FALCON IV (4k x 4k) / #1 - Average electron dose: 50.253 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: experimental model / Details: Model Angelo generated |
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| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
| Output model | ![]() PDB-10gx: |
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About Yorodumi




Keywords
Authors
United States, 1 items
Citation









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FIELD EMISSION GUN

