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- EMDB-52571: Cryo-EM structure of mouse RNF213:UBE2L3 transthiolation intermed... -

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Basic information

Entry
Database: EMDB / ID: EMD-52571
TitleCryo-EM structure of mouse RNF213:UBE2L3 transthiolation intermediate, chemically stabilized, and ATPgS
Map data
Sample
  • Complex: Mouse RNF213:UBE2L3 transthiolation intermediate
    • Protein or peptide: E3 ubiquitin-protein ligase RNF213
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 L3
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsE3 ligase / ubiquitin / AAA ATPase / LIGASE
Function / homology
Function and homology information


lipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / lipid droplet formation / cell cycle phase transition / ubiquitin-protein transferase activator activity / xenophagy / Antigen processing: Ubiquitination & Proteasome degradation / protein K11-linked ubiquitination / sprouting angiogenesis / Transferases; Acyltransferases; Aminoacyltransferases ...lipid ubiquitination / negative regulation of non-canonical Wnt signaling pathway / lipid droplet formation / cell cycle phase transition / ubiquitin-protein transferase activator activity / xenophagy / Antigen processing: Ubiquitination & Proteasome degradation / protein K11-linked ubiquitination / sprouting angiogenesis / Transferases; Acyltransferases; Aminoacyltransferases / : / cellular response to glucocorticoid stimulus / E2 ubiquitin-conjugating enzyme / cellular response to steroid hormone stimulus / ubiquitin conjugating enzyme activity / regulation of lipid metabolic process / protein K63-linked ubiquitination / immune system process / ubiquitin ligase complex / protein autoubiquitination / lipid droplet / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / positive regulation of protein ubiquitination / PINK1-PRKN Mediated Mitophagy / Regulation of TNFR1 signaling / RING-type E3 ubiquitin transferase / protein modification process / Regulation of necroptotic cell death / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / E3 ubiquitin ligases ubiquitinate target proteins / angiogenesis / ubiquitin-dependent protein catabolic process / transcription coactivator activity / cell population proliferation / defense response to bacterium / protein ubiquitination / ubiquitin protein ligase binding / regulation of DNA-templated transcription / enzyme binding / ATP hydrolysis activity / RNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
E3 ubiquitin-protein ligase RNF213 / Zinc finger, RZ-type / RZ type zinc finger domain / Zinc finger RZ-type profile. / : / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 ...E3 ubiquitin-protein ligase RNF213 / Zinc finger, RZ-type / RZ type zinc finger domain / Zinc finger RZ-type profile. / : / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RNF213 / Ubiquitin-conjugating enzyme E2 L3
Similarity search - Component
Biological speciesMus musculus (house mouse) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsGrabarczyk DB / Ahel J / Clausen T
Funding support Austria, 1 items
OrganizationGrant numberCountry
Austrian Research Promotion Agency852936 Austria
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionJan 16, 2025-
Header (metadata) releaseDec 10, 2025-
Map releaseDec 10, 2025-
UpdateDec 10, 2025-
Current statusDec 10, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52571.png

Downloads & links

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Map

FileDownload / File: emd_52571.map.gz / Format: CCP4 / Size: 127.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.18 Å/pix.
x 322 pix.
= 379.96 Å		1.18 Å/pix.
x 322 pix.
= 379.96 Å		1.18 Å/pix.
x 322 pix.
= 379.96 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.18 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0047
Minimum - Maximum-0.011574847 - 0.023762409
Average (Standard dev.)0.000003470573 (±0.0010302135)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions322322322
Spacing322322322
CellA=B=C: 379.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_52571_msk_1.map
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AxesZYX

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Additional map: AAA focused map

Fileemd_52571_additional_1.map
AnnotationAAA focused map
Projections & Slices
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Half map: #2

Fileemd_52571_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_52571_half_map_2.map
Projections & Slices
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Sample components

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Entire : Mouse RNF213:UBE2L3 transthiolation intermediate

EntireName: Mouse RNF213:UBE2L3 transthiolation intermediate
Components
  • Complex: Mouse RNF213:UBE2L3 transthiolation intermediate
    • Protein or peptide: E3 ubiquitin-protein ligase RNF213
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 L3
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Mouse RNF213:UBE2L3 transthiolation intermediate

SupramoleculeName: Mouse RNF213:UBE2L3 transthiolation intermediate / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: E3 ubiquitin-protein ligase RNF213

MacromoleculeName: E3 ubiquitin-protein ligase RNF213 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 552.623375 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MASWSHPQFE KGSTSAFNPR DTVTVYFHAI VSRHFGFNPE EHKVYVRGGE GLGQKGWTDA CEMYCTQDLH DLGSLVEGKM DIPRQSLDK PIPYKYVIHR GGSSKDTVEY EFIYEQAQKK GEHVNRCLRV VSTSLGNGDW HQYDDIICMR STGFFQQAKN R ILDSTRKE ...String:
MASWSHPQFE KGSTSAFNPR DTVTVYFHAI VSRHFGFNPE EHKVYVRGGE GLGQKGWTDA CEMYCTQDLH DLGSLVEGKM DIPRQSLDK PIPYKYVIHR GGSSKDTVEY EFIYEQAQKK GEHVNRCLRV VSTSLGNGDW HQYDDIICMR STGFFQQAKN R ILDSTRKE LLKGKKQAAV VMLDRIFSVL QPWSDINLQS FMTQFLQFYS VVREPMIHDG RARKWTSLQY EEKEVWTNLW EH VKKQMAP FLEGKSGESL PADCPVRSKL TLGLSILFMV EAAEFTVPKK DLDSLCYLLI PSAGSPEALH SDLSPVLRIR QRW RIYLTN LCLRCIDERC DRWLGILPLL HTCMQKSPPK KNSKSQPEDT WAGLEGISFS EFRDKAPTRS QPLQFMQSKM ALLR VDEYL FRSWLSVVPL ESLSSYLENS IDYLSDVPVR VLDCLQGISY RLPGLRKISN QNMKKDVENV FKMLMHLVDI YQHRI FGEN LLQIYLTECL TLHETVCNIT ANHQFFEIPA LSAELICKLL ELSPPGHTDE GLPEKSYEDL VTSTLQEALA TTRNWL RSL FKSRMLSISS AYVRLTYSEE MAVWRRLVEI GFPEKHGWKG SLLGDMEGRL KQEPPRLQIS FFCSSQCRDG GLHDSVS RS FEKCVIEAVS SACQSQTSVL EGLSCQDLQK FGTLLSAVIT KSWPVHNGEP VFDVDEIFKY LLKWPDVRQL FELCGTNE K IIDNITEEGR QLMATAESVF QKVAGELENG TIVVGQLELI LEHQSQFLDI WNLNRRRLPS QEKACDVRSL LKRRRDDLL FLKQEKRYVE SLLRQLGRVK HLVQVDFGNI EIIHSQDLSN KKLNEAVIKL PNSSSYKRET HYCLSPDIRE MASKLDSLKD SHIFQDFWQ ETAESLNTLD KDPRELKVSL PEVLEYLYNP CYDNFYTLYE NLKSGKITFA EVDAIFKDFV DKYDELKNDL K FMCTMNPQ DQKGWISERV GQIKEYHTLH QAVSSAKVIL QVRRALGVTG DFSVLNPLLN FADSFEDFGN EKLDQISPQF IK AKQLLQD ISEPRQRCLE ELARQTELVA WLHKALEDIN ELKVFVDLAS ISAGENDIDV DRVACFHDAV QGYASLLYKM DER TNFSDF MNHLQELWRA LDNDQHLPDK LKDSARNLEW LKTVKESHGS VELSSLSLAT AINSRGVYVI EAPKDGQKIS PDTV LRLLL PDGHGYPEAL RTYSTEELKE LLNKLMLMSG KKDHNSNTEV EKFSEVFSNM QRLVHVFIKL HCAGNMLFRT WTAKV YCCP DGGIFMNFGL ELLSQLTEKG DVIQLLGALC RQMEDFLDNW KTVVAQKRAE HFYLNFYTAE QLVYLSSELR KPRPSE AAL MMLSFIKGKC TVQDLVQATS ACESKADRYC LREVMKKLPQ QLLSEPSLMG KLQVIMMQSL VYMSAFLPHC LDLDALG RC LAHLATMGGT PVERPLPKGL QAGQPNLILC GHSEVLPAAL AIYMQAPRQP LPTFDEVLLC TPATTIEEVE LLLRRCLT S GSQGHKVYSL LFADQLSYEV GCQAEEFFQS LCTRAHREDY QLVILCDAAR EHCYIPSTFS QYKVPLVPQA PLPNIQAYL QSHYQVPKRL LSAATVFRDG LCVGIVTSER AGVGKSLYVN TLHTKLKAKL RDETVPLKII RLTEPHLDEN QVLSALLPFL KEKYQKMPV IFHIDISTSV QTGIPIFLFK LLILQYLMDI NGKIWRRSPG HLYLVEIPQG LSVQPKRSSK LNARAPLFKF L DLFPKVTC RPPKEVIDME LTPERSHTDP AMDPVEFCSE AFQRPYQYLK RFHQQQNLDT FQYEKGSVEG SPEECLQHFL IY CGLINPS WSELRNFAWF LNCQLKDCEA SIFCKSAFTG DTLRGFKNFV VTFMILMARD FATPTLHTSD QSPGRQSVTI GEV VEEDLA PFSLRKRWES EPHPYVFFNG DHMTMTFIGF HLETNNNGYV DAINPSNGKV IKKDVMTKEL FDGLRLQRVP FNID FDNLP RYEKLERLCL ALGIEWPIDP DETYELTTDN MLKILAIEMR FRCGIPVIIM GETGCGKTRL IKFLSDLKRG SVEAE TMKL VKVHGGTTPS MIYSKVKEAE RTAFSNKAQH KLDTILFFDE ANTTEAVSCI KEILCDRTVD GEHLHEDSGL HIIAAC NPY RKHSQEMILR LESAGLGYRV SAEETADRLG SIPLRQLVYR VHALPPSLIP LVWDFGQLND SAEKLYIQQI VQRLVDS VS VNPSETCVIA DVLSASQMFM RKRENECGFV SLRDVERCVK VFRWFHDHSD MLLKELDKFL HESSDSTHTF ERDPVLWS L VMAIGVCYHA SLEEKASYRT AIARCFPKPY NSSRAILDEV THVQDLFLRG APIRTNIARN LALKENVFMM VICIELKIP LFLVGKPGSS KSLAKIIVAD AMQGQAAFSE LFRCLKQVHL VSFQCSPHST PQGIISTFKQ CARFQQGKDL GQYVSVVVLD EVGLAEDSP KMPLKTLHPL LEDGCIEDDP APYKKVGFVG ISNWALDPAK MNRGIFVSRG SPNEKELIES AEGICSSDRL V QDKIRGYF APFAKAYETV CQKQDKEFFG LRDYYSLIKM VFAKAKASKR GLSPQDITHA VLRNFSGKDN IQALSIFTAS LP EARYKEE VSTVELIKQN IYPGPQASSR GLDGAESRYL LVLTRNYVAL QILQQTFFEG QQPEIIFGSS FPQDQEYTQI CRN INRVKI CMETGKMVVL LNLQNLYESL YDALNQYYVY LGGQKYVDLG LGTHRVKCRV HTAFRLIVIE EKDVVYKQFP VPLI NRLEK HYLDMNTVLQ PWQKSIVQEL QQWAHEFADV KADQFIARHK YSPADVFIGY HSDACASVVL QAVERQGCRD LTEEL YRKV SEEARSILLD CATPDAVVRL SGSSLGSFTA KQLSQEYYYA QQHNSFVDFL QAHLRMTHHE CRAVFTEITT FSRLLT GND CDVLASELRG LASKPVVLSL QQYDTEYSFL KDVRSWLTNP GKRKVLVIQA DFDDGTRSAQ LVASAKYTAI NEINKTQ GT KDFVFVYFVT KLSRMGSGTS YVGFHGGLWR SVHIDDLRRS TIMASDVTKL QNVTISQLFK PEDKPEQEEM EIETSQSK E LAEEQMEVED SEEMKKASDP RSCDCSQFLD TTRLVQSCVQ GAVGMLRDQN ESCARNMRRV TILLDLLNED NTRNASFLR ESKMRLHVLL NKQEENQVRS LKEWVTREAA NQDALQEAGT FRHTLWKRVQ DVVTPILASM IAHIDRDGNL ELLAQPDSPA WVQDLWMFI YSDIKFLNIS LVLNNTRSNS EMSFILVQSH MNLLKDAYNA VPFSWRIRDY LEELWVQAQY ITDTEGLSKK F VEIFQKTP LGVFLAQFPV AQQQKLLQSY LKDFLLLTMK VSSREELMFL QMALWSCLRE LQEASGTPDE TYKFPLSLPW VH LAFQHFR TRLQNFSRIL TIHPQVLSSL SQAAEKHSLA GCEMTLDAFA AMACAEMLKG DLLKPSPKAW LQLVKNLSTP LEL VCSEGY LCDSGSMTRS VIQEVRALWN RIFSIALFVE HVLLGTESHI PELSPLVTTY VSLLDKCLEE DSNLKTCRPF VAVM TTLCD CKDKASKKFS RFGIQPCFIC HGDAQDPVCL PCDHVYCLRC IQTWLIPGQM MCPYCLTDLP DKFSPTVSQD HRKAI EKHA QFRHMCNSFF VDLVSTMCFK DNTPPEKSVI DTLLSLLFVQ KELLRDASQK HREHTKSLSP FDDVVDQTPV IRSVLL KLL LKYSFHEVKD YIQNYLTQLE KKAFLTEDKT ELYLLFISCL EDSVHQKTSA GCRNLEQVLR EEGHFLRTYS PGLQGQE PV RIASVEYLQE VARVRLCLDL AADFLSELQE GSELAEDKRR FLKHVEEFCT RVNNDWHRVY LVRKLSSQRG MEFVQSFS K QGHPCQWVFP RKVIAQQKDH VSLMDRYLVH GNEYKAVRDA TAKAVLECKT LDIGNALMAC RSPKPQQTAY LLLALYTEV AALYRSPNGS LHPEAKQLEA VNKFIKESKI LSDPNIRCFA RSLVDNTLPL LKIRSANSIL KGTVTEMAVH VATILLCGHN QILKPLRNL AFYPVNMANA FLPTMPEDLL VHARTWRGLE NVTWYTCPRG HPCSVGECGR PMQESTCLDC GLPVGGLNHT P HEGFSAIR NNEDRTQTGH VLGSPQSSGV AEVSDRGQSP VVFILTRLLT HLAMLVGATH NPQALTVIIK PWVQDPQGFL QQ HIQRDLE QLTKMLGRSA DETIHVVHLI LSSLLRVQSH GVLNFNAELS TKGCRNNWEK HFETLLLREL KHLDKNLPAI NAL ISQDER ISSNPVTKII YGDPATFLPH LPQKSIIHCS KIWSCRRKIT VEYLQHIVEQ KNGKETVPVL WHFLQKEAEL RLVK FLPEI LALQRDLVKQ FQNVSRVEYS SIRGFIHSHS SDGLRKLLHD RITIFLSTWN ALRRSLETNG EIKLPKDYCC SDLDL DAEF EVILPRRQGL GLCGTALVSY LISLHNNMVY TVQKFSNEDN SYSVDISEVA DLHVISYEVE RDLNPLILSN CQYQVQ QGG ETSQEFDLEK IQRQISSRFL QGKPRLTLKG IPTLVYRRDW NYEHLFMDIK NKMAQSSLPN LAISTISGQL QSYSDAC EA LSIIEITLGF LSTAGGDPGM DLNVYIEEVL RMCDQTAQVL KAFSRCQLRH IIALWQFLSA HKSEQRLRLN KELFREID V QYKEELSTQH QRLLGTFLNE AGLDAFLLEL HEMIVLKLKG PRAANSFNPN WSLKDTLVSY METKDSDILS EVESQFPEE ILMSSCISVW KIAATRKWDR QSRGGGHHHH HHHHHH

UniProtKB: E3 ubiquitin-protein ligase RNF213

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Macromolecule #2: Ubiquitin-conjugating enzyme E2 L3

MacromoleculeName: Ubiquitin-conjugating enzyme E2 L3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: E2 ubiquitin-conjugating enzyme
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 19.197908 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GWSHPQFEKP GSMAASRRLM KELEEIRKSG MKNFRNIQVD EANLLTWQGL IVPDNPPYDK GAFRIEINFP AEYPFKPPKI TFKTKIYHP NIDEKGQVCL PVISAENWKP ATKTDQVIQS LIALVNDPQP EHPLRADLAE EYSKDRKKFS KNAEEFTKKY G EKRPVD

UniProtKB: Ubiquitin-conjugating enzyme E2 L3

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Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #5: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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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

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 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: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 31607
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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