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- EMDB-27841: Cryo-EM structure of BIRC6/HtrA2-S306A -

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Basic information

Entry
Database: EMDB / ID: EMD-27841
TitleCryo-EM structure of BIRC6/HtrA2-S306A
Map datamain map
Sample
  • Complex: Baculoviral IAP repeat-containing protein 6
    • Protein or peptide: Baculoviral IAP repeat-containing protein 6
    • Protein or peptide: Serine protease HTRA2, mitochondrial
Function / homology
Function and homology information


HtrA2 peptidase / pentacyclic triterpenoid metabolic process / negative regulation of mitophagy in response to mitochondrial depolarization / spongiotrophoblast layer development / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / regulation of autophagy of mitochondrion / ceramide metabolic process / CD40 receptor complex / : / labyrinthine layer development ...HtrA2 peptidase / pentacyclic triterpenoid metabolic process / negative regulation of mitophagy in response to mitochondrial depolarization / spongiotrophoblast layer development / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / regulation of autophagy of mitochondrion / ceramide metabolic process / CD40 receptor complex / : / labyrinthine layer development / programmed cell death / ALK mutants bind TKIs / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / Flemming body / serine-type endopeptidase complex / adult walking behavior / response to herbicide / microtubule organizing center / positive regulation of protein targeting to mitochondrion / execution phase of apoptosis / cysteine-type endopeptidase inhibitor activity / ubiquitin conjugating enzyme activity / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / protein autoprocessing / Signaling by ALK fusions and activated point mutants / regulation of multicellular organism growth / negative regulation of cell cycle / neuron development / cellular response to interferon-beta / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / forebrain development / cellular response to retinoic acid / serine-type peptidase activity / mitochondrion organization / regulation of cytokinesis / mitochondrial membrane / negative regulation of extrinsic apoptotic signaling pathway / protein catabolic process / RING-type E3 ubiquitin transferase / trans-Golgi network / mitochondrial intermembrane space / cytoplasmic side of plasma membrane / cellular response to growth factor stimulus / spindle pole / ubiquitin-protein transferase activity / intrinsic apoptotic signaling pathway in response to DNA damage / unfolded protein binding / cellular response to oxidative stress / cellular response to heat / regulation of cell population proliferation / peptidase activity / midbody / neuron apoptotic process / cell population proliferation / negative regulation of neuron apoptotic process / protein ubiquitination / cytoskeleton / endosome / cell cycle / positive regulation of apoptotic process / cell division / protein phosphorylation / serine-type endopeptidase activity / centrosome / apoptotic process / positive regulation of cell population proliferation / chromatin / endoplasmic reticulum membrane / negative regulation of apoptotic process / endoplasmic reticulum / mitochondrion / proteolysis / membrane / identical protein binding / nucleus / cytosol
Similarity search - Function
Baculoviral IAP repeat-containing protein 6 / Baculoviral IAP repeat-containing protein 6 / PDZ domain 6 / PDZ domain / Peptidase S1C / Trypsin-like peptidase domain / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat ...Baculoviral IAP repeat-containing protein 6 / Baculoviral IAP repeat-containing protein 6 / PDZ domain 6 / PDZ domain / Peptidase S1C / Trypsin-like peptidase domain / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Peptidase S1, PA clan
Similarity search - Domain/homology
Serine protease HTRA2, mitochondrial / Baculoviral IAP repeat-containing protein 6
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.21 Å
AuthorsHunkeler M / Fischer ES
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)CA066996 United States
The Mark Foundation19-001-ELA United States
CitationJournal: Science / Year: 2023
Title: Structures of BIRC6-client complexes provide a mechanism of SMAC-mediated release of caspases.
Authors: Moritz Hunkeler / Cyrus Y Jin / Eric S Fischer /
Abstract: Tight regulation of apoptosis is essential for metazoan development and prevents diseases such as cancer and neurodegeneration. Caspase activation is central to apoptosis, and inhibitor of apoptosis ...Tight regulation of apoptosis is essential for metazoan development and prevents diseases such as cancer and neurodegeneration. Caspase activation is central to apoptosis, and inhibitor of apoptosis proteins (IAPs) are the principal actors that restrain caspase activity and are therefore attractive therapeutic targets. IAPs, in turn, are regulated by mitochondria-derived proapoptotic factors such as SMAC and HTRA2. Through a series of cryo-electron microscopy structures of full-length human baculoviral IAP repeat-containing protein 6 (BIRC6) bound to SMAC, caspases, and HTRA2, we provide a molecular understanding for BIRC6-mediated caspase inhibition and its release by SMAC. The architecture of BIRC6, together with near-irreversible binding of SMAC, elucidates how the IAP inhibitor SMAC can effectively control a processive ubiquitin ligase to respond to apoptotic stimuli.
History
DepositionAug 15, 2022-
Header (metadata) releaseFeb 15, 2023-
Map releaseFeb 15, 2023-
UpdateMar 29, 2023-
Current statusMar 29, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_27841.png

Downloads & links

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Map

FileDownload / File: emd_27841.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmain map
Voxel sizeX=Y=Z: 1.2 Å
Density
Contour LevelBy AUTHOR: 0.215
Minimum - Maximum-0.5303137 - 1.3841721
Average (Standard dev.)0.0012512876 (±0.04191831)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 422.40002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_27841_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Mask #2

Fileemd_27841_msk_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 1

Fileemd_27841_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_27841_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Baculoviral IAP repeat-containing protein 6

EntireName: Baculoviral IAP repeat-containing protein 6
Components
  • Complex: Baculoviral IAP repeat-containing protein 6
    • Protein or peptide: Baculoviral IAP repeat-containing protein 6
    • Protein or peptide: Serine protease HTRA2, mitochondrial

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Supramolecule #1: Baculoviral IAP repeat-containing protein 6

SupramoleculeName: Baculoviral IAP repeat-containing protein 6 / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.174 MDa

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Macromolecule #1: Baculoviral IAP repeat-containing protein 6

MacromoleculeName: Baculoviral IAP repeat-containing protein 6 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: Ligases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 535.317188 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGDYKDHDGD YKDHDIDYKD DDDKGGGSGG LEVLFQGPSR TMVTGGGAAP PGTVTEPLPS VIVLSAGRKM AAAAAAASGP GCSSAAGAG AAGVSEWLVL RDGCMHCDAD GLHSLSYHPA LNAILAVTSR GTIKVIDGTS GATLQASALS AKPGGQVKCQ Y ISAVDKVI ...String:
MGDYKDHDGD YKDHDIDYKD DDDKGGGSGG LEVLFQGPSR TMVTGGGAAP PGTVTEPLPS VIVLSAGRKM AAAAAAASGP GCSSAAGAG AAGVSEWLVL RDGCMHCDAD GLHSLSYHPA LNAILAVTSR GTIKVIDGTS GATLQASALS AKPGGQVKCQ Y ISAVDKVI FVDDYAVGCR KDLNGILLLD TALQTPVSKQ DDVVQLELPV TEAQQLLSAC LEKVDISSTE GYDLFITQLK DG LKNTSHE TAANHKVAKW ATVTFHLPHH VLKSIASAIV NELKKINQNV AALPVASSVM DRLSYLLPSA RPELGVGPGR SVD RSLMYS EANRRETFTS WPHVGYRWAQ PDPMAQAGFY HQPASSGDDR AMCFTCSVCL VCWEPTDEPW SEHERHSPNC PFVK GEHTQ NVPLSVTLAT SPAQFPCTDG TDRISCFGSG SCPHFLAAAT KRGKICIWDV SKLMKVHLKF EINAYDPAIV QQLIL SGDP SSGVDSRRPT LAWLEDSSSC SDIPKLEGDS DDLLEDSDSE EHSRSDSVTG HTSQKEAMEV SLDITALSIL QQPEKL QWE IVANVLEDTV KDLEELGANP CLTNSKSEKT KEKHQEQHNI PFPCLLAGGL LTYKSPATSP ISSNSHRSLD GLSRTQG ES ISEQGSTDNE SCTNSELNSP LVRRTLPVLL LYSIKESDEK AGKIFSQMNN IMSKSLHDDG FTVPQIIEME LDSQEQLL L QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSA INQVEALNNL NKLNSALCNR RKGELESNLA VVNGANISVI QHESPADVQT PLIIQPEQRN VSGGYLVLYK MNYATRIVTL EEEPIKIQH IKDPQDTITS LILLPPDILD NREDDCEEPI EDMQLTSKNG FEREKTSDIS TLGHLVITTQ GGYVKILDLS N FEILAKVE PPKKEGTEEQ DTFVSVIYCS GTDRLCACTK GGELHFLQIG GTCDDIDEAD ILVDGSLSKG IEPSSEGSKP LS NPSSPGI SGVDLLVDQP FTLEILTSLV ELTRFETLTP RFSATVPPCW VEVQQEQQQR RHPQHLHQQH HGDAAQHTRT WKL QTDSNS WDEHVFELVL PKACMVGHVD FKFVLNSNIT NIPQIQVTLL KNKAPGLGKV NALNIEVEQN GKPSLVDLNE EMQH MDVEE SQCLRLCPFL EDHKEDILCG PVWLASGLDL SGHAGMLTLT SPKLVKGMAG GKYRSFLIHV KAVNERGTEE ICNGG MRPV VRLPSLKHQS NKGYSLASLL AKVAAGKEKS SNVKNENTSG TRKSENLRGC DLLQEVSVTI RRFKKTSISK ERVQRC AML QFSEFHEKLV NTLCRKTDDG QITEHAQSLV LDTLCWLAGV HSNGPGSSKE GNENLLSKTR KFLSDIVRVC FFEAGRS IA HKCARFLALC ISNGKCDPCQ PAFGPVLLKA LLDNMSFLPA ATTGGSVYWY FVLLNYVKDE DLAGCSTACA SLLTAVSR Q LQDRLTPMEA LLQTRYGLYS SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTG LLEVEPLHFT CVSTSDGTRI ERDDAMSSFG VTPAVGGLSS GTVGEASTAL SSAAQVALQS LSHAMASAEQ QLQVLQEKQQ QLLKLQQQK AKLEAKLHQT TAAAAAAASA VGPVHNSVPS NPVAAPGFFI HPSDVIPPTP KTTPLFMTPP LTPPNEAVSV V INAELAQL FPGSVIDPPA VNLAAHNKNS NKSRMNPLGS GLALAISHAS HFLQPPPHQS IIIERMHSGA RRFVTLDFGR PI LLTDVLI PTCGDLASLS IDIWTLGEEV DGRRLVVATD ISTHSLILHD LIPPPVCRFM KITVIGRYGS TNARAKIPLG FYY GHTYIL PWESELKLMH DPLKGEGESA NQPEIDQHLA MMVALQEDIQ CRYNLACHRL ETLLQSIDLP PLNSANNAQY FLRK PDKAV EEDSRVFSAY QDCIQLQLQL NLAHNAVQRL KVALGASRKM LSETSNPEDL IQTSSTEQLR TIIRYLLDTL LSLLH ASNG HSVPAVLQST FHAQACEELF KHLCISGTPK IRLHTGLLLV QLCGGERWWG QFLSNVLQEL YNSEQLLIFP QDRVFM LLS CIGQRSLSNS GVLESLLNLL DNLLSPLQPQ LPMHRRTEGV LDIPMISWVV MLVSRLLDYV ATVEDEAAAA KKPLNGN QW SFINNNLHTQ SLNRSSKGSS SLDRLYSRKI RKQLVHHKQQ LNLLKAKQKA LVEQMEKEKI QSNKGSSYKL LVEQAKLK Q ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL SMDFTCHADL LLFVCKVLA RIANATRPTI HLCEIVNEPQ LERLLLLLVG TDFNRGDISW GGAWAQYSLT CMLQDILAGE LLAPVAAEAM EEGTVGDDVG ATAGDSDDS LQQSSVQLLE TIDEPLTHDI TGAPPLSSLE KDKEIDLELL QDLMEVDIDP LDIDLEKDPL AAKVFKPISS T WYDYWGAD YGTYNYNPYI GGLGIPVAKP PANTEKNGSQ TVSVSVSQAL DARLEVGLEQ QAELMLKMMS TLEADSILQA LT NTSPTLS QSPTGTDDSL LGGLQAANQT SQLIIQLSSV PMLNVCFNKL FSMLQVHHVQ LESLLQLWLT LSLNSSSTGN KEN GADIFL YNANRIPVIS LNQASITSFL TVLAWYPNTL LRTWCLVLHS LTLMTNMQLN SGSSSAIGTQ ESTAHLLVSD PNLI HVLVK FLSGTSPHGT NQHSPQVGPT ATQAMQEFLT RLQVHLSSTC PQIFSEFLLK LIHILSTERG AFQTGQGPLD AQVKL LEFT LEQNFEVVSV STISAVIESV TFLVHHYITC SDKVMSRSGS DSSVGARACF GGLFANLIRP GDAKAVCGEM TRDQLM FDL LKLVNILVQL PLSGNREYSA RVSVTTNTTD SVSDEEKVSG GKDGNGSSTS VQGSPAYVAD LVLANQQIMS QILSALG LC NSSAMAMIIG ASGLHLTKHE NFHGGLDAIS VGDGLFTILT TLSKKASTVH MMLQPILTYM ACGYMGRQGS LATCQLSE P LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEG IHNFAPLGTI TSSSPTAQPA EVLLQATPPH RRARSAAWSY IFLPEEAWCD LTIHLPAAVL LKEIHIQPHL ASLATCPSSV SVEVSADGV NMLPLSTPVV TSGLTYIKIQ LVKAEVASAV CLRLHRPRDA STLGLSQIKL LGLTAFGTTS SATVNNPFLP S EDQVSKTS IGWLRLLHHC LTHISDLEGM MASAAAPTAN LLQTCAALLM SPYCGMHSPN IEVVLVKIGL QSTRIGLKLI DI LLRNCAA SGSDPTDLNS PLLFGRLNGL SSDSTIDILY QLGTTQDPGT KDRIQALLKW VSDSARVAAM KRSGRMNYMC PNS STVEYG LLMPSPSHLH CVAAILWHSY ELLVEYDLPA LLDQELFELL FNWSMSLPCN MVLKKAVDSL LCSMCHVHPN YFSL LMGWM GITPPPVQCH HRLSMTDDSK KQDLSSSLTD DSKNAQAPLA LTESHLATLA SSSQSPEAIK QLLDSGLPSL LVRSL ASFC FSHISSSESI AQSIDISQDK LRRHHVPQQC NKMPITADLV APILRFLTEV GNSHIMKDWL GGSEVNPLWT ALLFLL CHS GSTSGSHNLG AQQTSARSAS LSSAATTGLT TQQRTAIENA TVAFFLQCIS CHPNNQKLMA QVLCELFQTS PQRGNLP TS GNISGFIRRL FLQLMLEDEK VTMFLQSPCP LYKGRINATS HVIQHPMYGA GHKFRTLHLP VSTTLSDVLD RVSDTPSI T AKLISEQKDD KEKKNHEEKE KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKI ITVPVFHLFH KLLAGQPLPA EMTLAQLLTL LYDRKLPQGY RSIDLTVKLG SRVITDPSLS KTDSYKRLHP EKDHGDLLAS CPEDEALTP GDECMDGILD ESLLETCPIQ SPLQVFAGMG GLALIAERLP MLYPEVIQQV SAPVVTSTTQ EKPKDSDQFE W VTIEQSGE LVYEAPETVA AEPPPIKSAV QTMSPIPAHS LAAFGLFLRL PGYAEVLLKE RKHAQCLLRL VLGVTDDGEG SH ILQSPSA NVLPTLPFHV LRSLFSTTPL TTDDGVLLRR MALEIGALHL ILVCLSALSH HSPRVPNSSV NQTEPQVSSS HNP TSTEEQ QLYWAKGTGF GTGSTASGWD VEQALTKQRL EEEHVTCLLQ VLASYINPVS SAVNGEAQSS HETRGQNSNA LPSV LLELL SQSCLIPAMS SYLRNDSVLD MARHVPLYRA LLELLRAIAS CAAMVPLLLP LSTENGEEEE EQSECQTSVG TLLAK MKTC VDTYTNRLRS KRENVKTGVK PDASDQEPEG LTLLVPDIQK TAEIVYAATT SLRQANQEKK LGEYSKKAAM KPKPLS VLK SLEEKYVAVM KKLQFDTFEM VSEDEDGKLG FKVNYHYMSQ VKNANDANSA ARARRLAQEA VTLSTSLPLS SSSSVFV RC DEERLDIMKV LITGPADTPY ANGCFEFDVY FPQDYPSSPP LVNLETTGGH SVRFNPNLYN DGKVCLSILN TWHGRPEE K WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM LEQIRNPSPC FKEVIHKHF YLKRVEIMAQ CEEWIADIQQ YSSDKRVGRT MSHHAAALKR HTAQLREELL KLPCPEGLDP DTDDAPEVCR ATTGAEETLM HDQVKPSSS KELPSDFQL

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Macromolecule #2: Serine protease HTRA2, mitochondrial

MacromoleculeName: Serine protease HTRA2, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: HtrA2 peptidase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.961887 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAVPSPPPAS PRSQYNFIAD VVEKTAPAVV YIEILDRHPF LGREVPISNG SGFVVAADGL IVTNAHVVAD RRRVRVRLLS GDTYEAVVT AVDPVADIAT LRIQTKEPLP TLPLGRSADV RQGEFVVAMG SPFALQNTIT SGIVSSAQRP ARDLGLPQTN V EYIQTDAA ...String:
MAVPSPPPAS PRSQYNFIAD VVEKTAPAVV YIEILDRHPF LGREVPISNG SGFVVAADGL IVTNAHVVAD RRRVRVRLLS GDTYEAVVT AVDPVADIAT LRIQTKEPLP TLPLGRSADV RQGEFVVAMG SPFALQNTIT SGIVSSAQRP ARDLGLPQTN V EYIQTDAA IDFGNAGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS SSGISGSQRR YIGVMMLTLS PS ILAELQL REPSFPDVQH GVLIHKVILG SPAHRAGLRP GDVILAIGEQ MVQNAEDVYE AVRTQSQLAV QIRRGRETLT LYV TPEVTE HHHHHH

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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

Concentration1 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
30.0 mMC8H18N2O4SHEPES
150.0 mMNaClSodium chlorideSodium chloride
3.0 mMC9H15O6PTCEP
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 12.0 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.039 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 283.15 K / Instrument: LEICA EM GP
Detailsadded CHAPSO to 0.4 mM

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
DetailsData collection in counting mode, using multi-shot scheme (9 holes per stage position, 3 movies per hole)
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Digitization - Frames/image: 1-50 / Number grids imaged: 1 / Number real images: 15309 / Average exposure time: 2.5 sec. / Average electron dose: 60.659 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2049607
Startup modelType of model: OTHER / Details: ab initio
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 6 / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 73712
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-8e2k:
Cryo-EM structure of BIRC6/HtrA2-S306A

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