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- EMDB-37938: Partially closed Falcilysin bound to MK-4815, from MK-4815-treate... -

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Basic information

Entry
Database: EMDB / ID: EMD-37938
TitlePartially closed Falcilysin bound to MK-4815, from MK-4815-treated dataset
Map datamap after 'auto-refine' in RELION, after 'Bayesian polishing'
Sample
  • Complex: Falcilysin
    • Protein or peptide: Falcilysin
  • Ligand: 2-(aminomethyl)-3,5-ditert-butyl-phenol
  • Ligand: ZINC ION
Keywordsfalcilysin partially closed conformation / MK-4815 binding / HYDROLASE
Function / homology
Function and homology information


hemoglobin catabolic process / apicoplast / food vacuole / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / vacuolar membrane / protein processing / metalloendopeptidase activity / metal ion binding
Similarity search - Function
Peptidase M16C associated / Peptidase M16C associated / Peptidase M16C associated / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like
Similarity search - Domain/homology
Biological speciesPlasmodium falciparum 3D7 (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.7 Å
AuthorsLin JQ / Yan XF / Lescar J
Funding support Singapore, 1 items
OrganizationGrant numberCountry
Not funded Singapore
CitationJournal: To Be Published
Title: Partially closed Falcilysin bound to MK-4815, from MK-4815-treated dataset
Authors: Lin JQ / Yan XF / Lescar J
History
DepositionOct 31, 2023-
Header (metadata) releaseAug 7, 2024-
Map releaseAug 7, 2024-
UpdateAug 7, 2024-
Current statusAug 7, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_37938.map.gz / Format: CCP4 / Size: 8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmap after 'auto-refine' in RELION, after 'Bayesian polishing'
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.16 Å/pix.
x 128 pix.
= 148.48 Å
1.16 Å/pix.
x 128 pix.
= 148.48 Å
1.16 Å/pix.
x 128 pix.
= 148.48 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.16 Å
Density
Contour LevelBy AUTHOR: 0.016
Minimum - Maximum-0.03654081 - 0.08960914
Average (Standard dev.)0.00009574618 (±0.0045482237)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions128128128
Spacing128128128
CellA=B=C: 148.48 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_37938_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: unmasked map from 'Post-processing' in RELION

Fileemd_37938_additional_1.map
Annotationunmasked map from 'Post-processing' in RELION
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: masked map from 'Post-processing' in RELION

Fileemd_37938_additional_2.map
Annotationmasked map from 'Post-processing' in RELION
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: half map 2

Fileemd_37938_half_map_1.map
Annotationhalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: half map 1

Fileemd_37938_half_map_2.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Falcilysin

EntireName: Falcilysin
Components
  • Complex: Falcilysin
    • Protein or peptide: Falcilysin
  • Ligand: 2-(aminomethyl)-3,5-ditert-butyl-phenol
  • Ligand: ZINC ION

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Supramolecule #1: Falcilysin

SupramoleculeName: Falcilysin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)

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Macromolecule #1: Falcilysin

MacromoleculeName: Falcilysin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
Source (natural)Organism: Plasmodium falciparum 3D7 (eukaryote)
Molecular weightTheoretical: 135.039359 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHSSG VDLGTENLYF QSMEWIHEKS PKHNSYDIIE KRYNEEFKMT YTVYQHKKAK TQVISLGTND PLDVEQAFAF YVKTLTHSG KGIPHILEHS VLSGSKNYNY KNSIGLLEKG TLHTHLNAYT FNDRTVYMAG SMNNKDFFNI MGVYMDSVFQ P NVLENKYI ...String:
MHHHHHHSSG VDLGTENLYF QSMEWIHEKS PKHNSYDIIE KRYNEEFKMT YTVYQHKKAK TQVISLGTND PLDVEQAFAF YVKTLTHSG KGIPHILEHS VLSGSKNYNY KNSIGLLEKG TLHTHLNAYT FNDRTVYMAG SMNNKDFFNI MGVYMDSVFQ P NVLENKYI FETEGWTYEV EKLKEDEKGK AEIPQMKDYK VSFNGIVYNE MKGALSSPLE DLYHEEMKYM FPDNVHSNNS GG DPKEITN LTYEEFKEFY YKNYNPKKVK VFFFSKNNPT ELLNFVDQYL GQLDYSKYRD DAVESVEYQT YKKGPFYIKK KYG DHSEEK ENLVSVAWLL NPKVDKTNNH NNNHSNNQSS ENNGYSNGSH SSDLSLENPT DYFVLLIINN LLIHTPESVL YKAL TDCGL GNNVIDRGLN DSLVQYIFSI GLKGIKRNNE KIKNFDKVHY EVEDVIMNAL KKVVKEGFNK SAVEASINNI EFILK EANL KTSKSIDFVF EMTSKLNYNR DPLLIFEFEK YLNIVKNKIK NEPMYLEKFV EKHFINNAHR SVILLEGDEN YAQEQE NLE KQELKKRIEN FNEQEKEQVI KNFEELSKYK NAEESPEHLN KFPIISISDL NKKTLEVPVN VYFTNINENN NIMETYN KL KTNEHMLKDN MDVFLKKYVL KNDKHNTNNN NNNNNNMDYS FTETKYEGNV PILVYEMPTT GIVYLQFVFS LDHLTVDE L AYLNLFKTLI LENKTNKRSS EDFVILREKN IGSMSANVAL YSKDDHLNVT DKYNAQALFN LEMHVLSHKC NDALNIALE AVKESDFSNK KKVIDILKRK INGMKTTFSE KGYAILMKYV KAHLNSKHYA HNIIYGYENY LKLQEQLELA ENDFKTLENI LVRIRNKIF NKKNLMVSVT SDYGALKHLF VNSNESLKNL VSYFEENDKY INDMQNKVND PTVMGWNEEI KSKKLFDEEK V KKEFFVLP TFVNSVSMSG ILFKPGEYLD PSFTVIVAAL KNSYLWDTVR GLNGAYGVFA DIEYDGSVVF LSARDPNLEK TL ATFRESA KGLRKMADTM TENDLLRYII NTIGTIDKPR RGIELSKLSF LRLISNESEQ DRVEFRKRIM NTKKEDFYKF ADL LESKVN EFEKNIVIIT TKEKANEYIA NVDGEFKKVL IE

UniProtKB: Falcilysin

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Macromolecule #2: 2-(aminomethyl)-3,5-ditert-butyl-phenol

MacromoleculeName: 2-(aminomethyl)-3,5-ditert-butyl-phenol / type: ligand / ID: 2 / Number of copies: 1 / Formula: H8F
Molecular weightTheoretical: 235.365 Da
Chemical component information

ChemComp-H8F:
2-(aminomethyl)-3,5-ditert-butyl-phenol

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.5 mg/mL
BufferpH: 7.5 / Details: 20 mM Na HEPES, 300 mM NaCl, 0.5 mM TCEP, pH 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 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: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 98298
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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