+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-19113 | |||||||||
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Title | BmrA E504-apo | |||||||||
Map data | ||||||||||
Sample |
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Keywords | BmrA / multidrug transporter / drug resistance / ABC transporter / TRANSPORT PROTEIN | |||||||||
Function / homology | Function and homology information ABC-type transporter activity / ATP hydrolysis activity / ATP binding / membrane Similarity search - Function | |||||||||
Biological species | Bacillus subtilis (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Gobet A / Zarkadas E / Schoehn G / Falson P / Chaptal V | |||||||||
Funding support | France, 1 items
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Citation | Journal: To Be Published Title: BmrA E504-apo Authors: Gobet A / Zarkadas E / Schoehn G / Falson P / Chaptal V | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_19113.map.gz | 59.6 MB | EMDB map data format | |
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Header (meta data) | emd-19113-v30.xml emd-19113.xml | 15.7 KB 15.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_19113_fsc.xml | 8.4 KB | Display | FSC data file |
Images | emd_19113.png | 34.6 KB | ||
Filedesc metadata | emd-19113.cif.gz | 5.8 KB | ||
Others | emd_19113_half_map_1.map.gz emd_19113_half_map_2.map.gz | 59.1 MB 59.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19113 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19113 | HTTPS FTP |
-Validation report
Summary document | emd_19113_validation.pdf.gz | 788.5 KB | Display | EMDB validaton report |
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Full document | emd_19113_full_validation.pdf.gz | 788 KB | Display | |
Data in XML | emd_19113_validation.xml.gz | 16.2 KB | Display | |
Data in CIF | emd_19113_validation.cif.gz | 21.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19113 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19113 | HTTPS FTP |
-Related structure data
Related structure data | 8rezMC 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_19113.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: 0.839 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: half map A
File | emd_19113_half_map_1.map | ||||||||||||
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Annotation | half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map B
File | emd_19113_half_map_2.map | ||||||||||||
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Annotation | half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Multidrug resistance ABC transporter ATP-binding/permease protein BmrA
Entire | Name: Multidrug resistance ABC transporter ATP-binding/permease protein BmrA |
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Components |
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-Supramolecule #1: Multidrug resistance ABC transporter ATP-binding/permease protein BmrA
Supramolecule | Name: Multidrug resistance ABC transporter ATP-binding/permease protein BmrA type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Apo form, mutant E504A |
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Source (natural) | Organism: Bacillus subtilis (bacteria) |
Molecular weight | Theoretical: 130 KDa |
-Macromolecule #1: Lipid A export ATP-binding/permease protein MsbA
Macromolecule | Name: Lipid A export ATP-binding/permease protein MsbA / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances |
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Source (natural) | Organism: Bacillus subtilis (bacteria) |
Molecular weight | Theoretical: 65.747141 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MSSSHHHHHH MPTKKQKSKS KLKPFFALVR RTNPSYGKLA FALALSVVTT LVSLLIPLLT KQLVDGFSMS NLSGTQIGLI ALVFFVQAG LSAYATYALN YNGQKIISGL RELLWKKLIK LPVSYFDTNA SGETVSRVTN DTMVVKELIT THISGFITGI I SVIGSLTI ...String: MSSSHHHHHH MPTKKQKSKS KLKPFFALVR RTNPSYGKLA FALALSVVTT LVSLLIPLLT KQLVDGFSMS NLSGTQIGLI ALVFFVQAG LSAYATYALN YNGQKIISGL RELLWKKLIK LPVSYFDTNA SGETVSRVTN DTMVVKELIT THISGFITGI I SVIGSLTI LFIMNWKLTL LVLVVVPLAA LILVPIGRKM FSISRETQDE TARFTGLLNQ ILPEIRLVKA SNAEDVEYGR GK MGISSLF KLGVREAKVQ SLVGPLISLV LMAALVAVIG YGGMQVSSGE LTAGALVAFI LYLFQIIMPM GQITTFFTQL QKS IGATER MIEILAEEEE DTVTGKQIEN AHLPIQLDRV SFGYKPDQLI LKEVSAVIEA GKVTAIVGPS GGGKTTLFKL LERF YSPTA GTIRLGDEPV DTYSLESWRE HIGYVSQESP LMSGTIRENI CYGLERDVTD AEIEKAAEMA YALNFIKELP NQFDT EVGE RGIMLSGGQR QRIAIARALL RNPSILMLDA ATSSLDSQSE KSVQQALEVL MEGRTTIVIA HRLSTVVDAD QLLFVE KGE ITGRGTHHEL MASHGLYRDF AEQQLKMNAD LENKAG UniProtKB: Lipid A export ATP-binding/permease protein MsbA |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 4 mg/mL |
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Buffer | pH: 7.5 |
Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 25123 / Average exposure time: 1.9 sec. / Average electron dose: 40.12 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 105000 / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |