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- EMDB-72166: Rad55-Rad57-SHU homologous recombination complex -

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Basic information

Entry
Database: EMDB / ID: EMD-72166
TitleRad55-Rad57-SHU homologous recombination complex
Map dataRad55-Rad57-SHU homologous recombination complex
Sample
  • Complex: Rad55-Rad57-SHU
    • Protein or peptide: x 7 types
    • DNA: x 1 types
  • Ligand: x 4 types
KeywordsHomologous Recombination Complex / Rad51 Paralog Complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


Shu complex / positive regulation of single-strand break repair via homologous recombination / Presynaptic phase of homologous DNA pairing and strand exchange / meiotic joint molecule formation / error-free postreplication DNA repair / heteroduplex formation / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / meiotic DNA recombinase assembly / methylated-DNA-[protein]-cysteine S-methyltransferase ...Shu complex / positive regulation of single-strand break repair via homologous recombination / Presynaptic phase of homologous DNA pairing and strand exchange / meiotic joint molecule formation / error-free postreplication DNA repair / heteroduplex formation / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / meiotic DNA recombinase assembly / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / maintenance of rDNA / meiotic chromosome segregation / mitochondrial chromosome / mitotic recombination-dependent replication fork processing / chromosome organization involved in meiotic cell cycle / mitochondrial DNA repair / DNA recombinase assembly / DNA strand invasion / mitotic recombination / DNA strand exchange activity / telomere maintenance via recombination / reciprocal meiotic recombination / recombinational repair / error-free translesion synthesis / ATP-dependent DNA damage sensor activity / nuclear chromosome / DNA replication origin binding / ATP-dependent activity, acting on DNA / condensed nuclear chromosome / G2/M transition of mitotic cell cycle / replication fork / double-strand break repair via homologous recombination / nucleotide-excision repair / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / double-strand break repair / single-stranded DNA binding / site of double-strand break / DNA recombination / double-stranded DNA binding / mitochondrial matrix / DNA repair / nucleolus / DNA binding / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / Suppressor of hydroxyurea sensitivity protein 2 / : / Suppressor of HU sensitivity involved in recombination protein 1 / Shu complex, component Psy3 / Chromosome segregation in meiosis protein 2 / Shu complex component Csm2, DNA-binding / Shu complex component Psy3, DNA-binding description / : / : ...: / Suppressor of hydroxyurea sensitivity protein 2 / : / Suppressor of HU sensitivity involved in recombination protein 1 / Shu complex, component Psy3 / Chromosome segregation in meiosis protein 2 / Shu complex component Csm2, DNA-binding / Shu complex component Psy3, DNA-binding description / : / : / Methylguanine DNA methyltransferase, ribonuclease-like domain / KaiC-like domain / 6-O-methylguanine DNA methyltransferase, ribonuclease-like domain / KaiC / Methylated DNA-protein cysteine methyltransferase domain superfamily / Methylated-DNA-[protein]-cysteine S-methyltransferase, active site / Methylated-DNA--protein-cysteine methyltransferase active site. / Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding / Methylated DNA-protein cysteine methyltransferase, DNA binding domain / 6-O-methylguanine DNA methyltransferase, DNA binding domain / DNA recombination/repair protein Rad51 / DNA recombination and repair protein, RecA-like / DNA recombination and repair protein Rad51-like, C-terminal / Rad51 / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. / DNA repair Rad51/transcription factor NusA, alpha-helical / : / SAM-like Helix-hairpin-helix tandem / Winged helix-like DNA-binding domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Suppressor of hydroxyurea sensitivity protein 2 / Methylated-DNA--[protein]-cysteine S-methyltransferase / DNA repair protein RAD57 / DNA repair protein RAD51 / Suppressor of HU sensitivity involved in recombination protein 1 / DNA repair protein RAD55 / Chromosome segregation in meiosis protein 2 / Platinum sensitivity protein 3
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsYatskevich S / Koo CW / Ciferri C
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Mol Cell / Year: 2026
Title: Yeast Rad55-Rad57-SHU paralog complex dynamically promotes Rad51 filament formation.
Authors: Christopher W Koo / Steven K Gore / Soo Y Ro / Jie Liu / Christine Yu / Caleigh M Azumaya / Bobby Brillantes / Inna Zilberleyb / Henry Chen / Mariam B Rafiqzada / Lyra Garcia Sanchez / Wolf- ...Authors: Christopher W Koo / Steven K Gore / Soo Y Ro / Jie Liu / Christine Yu / Caleigh M Azumaya / Bobby Brillantes / Inna Zilberleyb / Henry Chen / Mariam B Rafiqzada / Lyra Garcia Sanchez / Wolf-Dietrich Heyer / Claudio Ciferri / Stanislau Yatskevich /
Abstract: Homologous recombination (HR) is an important DNA repair pathway that safeguards genome integrity. During HR, the Rad51 nucleoprotein filaments catalyze strand invasion into a homologous duplex DNA. ...Homologous recombination (HR) is an important DNA repair pathway that safeguards genome integrity. During HR, the Rad51 nucleoprotein filaments catalyze strand invasion into a homologous duplex DNA. Filament formation requires a conserved family of Rad51 paralogs that act as tumor suppressors in humans. By capturing six distinct states using cryo-electron microscopy, we reveal that the Saccharomyces cerevisiae Rad51 paralog complex, composed of the Rad55-Rad57 heterodimer and the SHU (Psy3-Csm2-Shu1-Shu2) complex, selectively brings Rad51 to single-stranded DNA to seed filament formation. Rad51 itself is a transient yet integral component of this machinery which binds along the Rad57 subunit to complete a high-affinity DNA-binding site. We also uncover a dual-nucleotide regulatory mechanism: a structural ADP molecule stabilizes the complex, while a second, catalytic ATPase site at the Rad57-Rad51 interface promotes the release of the paralog complex. These structural and mechanistic features provide a blueprint for understanding the function of Rad51 paralogs across eukaryotes.
History
DepositionAug 15, 2025-
Header (metadata) releaseJul 22, 2026-
Map releaseJul 22, 2026-
UpdateSep 30, 2026-
Current statusSep 30, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_72166.png

Downloads & links

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Map

FileDownload / File: emd_72166.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRad55-Rad57-SHU homologous recombination complex
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.91 Å/pix.
x 400 pix.
= 362.5 Å		0.91 Å/pix.
x 400 pix.
= 362.5 Å		0.91 Å/pix.
x 400 pix.
= 362.5 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.90625 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.05
Minimum - Maximum-0.16663107 - 0.41449824
Average (Standard dev.)-0.00017917642 (±0.009049312)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 362.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Additional Map 1

Fileemd_72166_additional_1.map
AnnotationAdditional Map 1
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Additional map: Additional Map 1

Fileemd_72166_additional_2.map
AnnotationAdditional Map 1
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Additional map: Additional Map 3

Fileemd_72166_additional_3.map
AnnotationAdditional Map 3
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Additional map: Additional Map 4

Fileemd_72166_additional_4.map
AnnotationAdditional Map 4
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Additional map: Additional Map 5

Fileemd_72166_additional_5.map
AnnotationAdditional Map 5
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Half map: Half Map B

Fileemd_72166_half_map_1.map
AnnotationHalf Map B
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Half map: Half Map A

Fileemd_72166_half_map_2.map
AnnotationHalf Map A
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Sample components

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Entire : Rad55-Rad57-SHU

EntireName: Rad55-Rad57-SHU
Components
  • Complex: Rad55-Rad57-SHU
    • Protein or peptide: Methylated-DNA--protein-cysteine methyltransferase,DNA repair protein RAD55
    • Protein or peptide: DNA repair protein RAD57
    • Protein or peptide: Chromosome segregation in meiosis protein 2
    • Protein or peptide: Platinum sensitivity protein 3
    • Protein or peptide: Suppressor of HU sensitivity involved in recombination protein 1
    • Protein or peptide: Suppressor of hydroxyurea sensitivity protein 2
    • Protein or peptide: DNA repair protein RAD51
    • DNA: ssDNA (12-mer)
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ZINC ION

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Supramolecule #1: Rad55-Rad57-SHU

SupramoleculeName: Rad55-Rad57-SHU / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 271.98 KDa

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Macromolecule #1: Methylated-DNA--protein-cysteine methyltransferase,DNA repair pro...

MacromoleculeName: Methylated-DNA--protein-cysteine methyltransferase,DNA repair protein RAD55
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: methylated-DNA-[protein]-cysteine S-methyltransferase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 70.243594 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KGSMDKDCEM KRTTLDSPLG KLELSGCEQG LHRIIFLGKG TSAADAVEVP APAAVLGGP EPLMQATAWL NAYFHQPEAI EEFPVPALHH PVFQQESFTR QVLWKLLKVV KFGEVISYSH LAALAGNPAA T AAVKTALS ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KGSMDKDCEM KRTTLDSPLG KLELSGCEQG LHRIIFLGKG TSAADAVEVP APAAVLGGP EPLMQATAWL NAYFHQPEAI EEFPVPALHH PVFQQESFTR QVLWKLLKVV KFGEVISYSH LAALAGNPAA T AAVKTALS GNPVPILIPC HRVVQGDLDV GGYEGGLAVK EWLLAHEGHR LGKPGLGGSE NLYFQGSMSL GIPLSQLIVE SP KPLSSGI TGLDEILNLG FQARSIYEIF GPPGIGKTNF GIQLVCNSLE GIQQSEINDD KILWIETFQE MPINILRERF QKF KIVEEN VKRVRITKFG QLLYFFQNLF KLSQSVRYKL VIIDGFSQLV CDHLCTLSKR GGGMIDKTIH ELKCRHLILI FTVM TKYTH STGSTIIVLN DCMNTAFQSN EFESLEEYYE ILDDGSNFFV NSNNERRKNN VHILKSALVA NIAMGSKDST WEVFL RDRI GLFRDWNEQV DETVFVKSKR VKASSSQSNE GCTTIKEMRI NKRNFENLRI AIVFNLHGED RKREGRNLKR SRSSDD RNY IVKFDFDKAT GQLRDIIDLK PDTANIASFP TLSTSSSSCS QVFNNIDSND NPLPNAEGKE EIIYDSEG

UniProtKB: Methylated-DNA--[protein]-cysteine S-methyltransferase, DNA repair protein RAD55

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Macromolecule #2: DNA repair protein RAD57

MacromoleculeName: DNA repair protein RAD57 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 52.307316 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MPRALSIKFD NTYMDLYDEL PESKLLYDEE FSYLLDAVRQ NGVCVVDFLT LTPKELARLI QRSINEVFRF QQLLVHEYNE KYLEICEKN SISPDNGPEC FTTADVAMDE LLGGGIFTHG ITEIFGESST GKSQLLMQLA LSVQLSEPAG GLGGKCVYIT T QGDLPTQR ...String:
MPRALSIKFD NTYMDLYDEL PESKLLYDEE FSYLLDAVRQ NGVCVVDFLT LTPKELARLI QRSINEVFRF QQLLVHEYNE KYLEICEKN SISPDNGPEC FTTADVAMDE LLGGGIFTHG ITEIFGESST GKSQLLMQLA LSVQLSEPAG GLGGKCVYIT T QGDLPTQR LESMLSSRPA YEKLGITQSN IFTVSCNDLI NQEHIINVQL PILLERSKGS IKLVIIDSIS HHLRVELQNK SF RESQENK NYLDRMAEKL QILAHDYSLS VVVANQVGDK PLANSPVAHR TYVTDYDYQL GWLVGWKNST ILYRQMNSLL GAS SNNDEI LSDDEDYMLI ERVMSTVNDR NYDFFSKKKP PIIENKTVER NSSSPISRQS KKRKFDYRVP NLGLTWSNHV STRI LLQKS FKASTIIQRG EAHLYKGGDS ASFWQVKRTM KVVYSTFAKP GQIAYQITKR GIETA

UniProtKB: DNA repair protein RAD57

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Macromolecule #3: Chromosome segregation in meiosis protein 2

MacromoleculeName: Chromosome segregation in meiosis protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 24.98368 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEYEDLELIT IWPSPTKNKL CQFIKQNLSK EHVVTQLFFI DATSSFPLSQ FQKLVPPTLP ENVRIYENIR INTCLDLEEL SAITVKLLQ ILSMNKINAQ RGTEDAVTEP LKIILYINGL EVMFRNSQFK SSPQRSHELL RDTLLKLRVM GNDENENASI R TLLEFPKE ...String:
MEYEDLELIT IWPSPTKNKL CQFIKQNLSK EHVVTQLFFI DATSSFPLSQ FQKLVPPTLP ENVRIYENIR INTCLDLEEL SAITVKLLQ ILSMNKINAQ RGTEDAVTEP LKIILYINGL EVMFRNSQFK SSPQRSHELL RDTLLKLRVM GNDENENASI R TLLEFPKE QLLDYYLKKN NNTRTSSVRS KRRRIKNGDS LAEYIWKYYA DSLFE

UniProtKB: Chromosome segregation in meiosis protein 2

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Macromolecule #4: Platinum sensitivity protein 3

MacromoleculeName: Platinum sensitivity protein 3 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 32.385123 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KSGENLYFQM EVLKNIRIYP LSNFITSTKN YINLPNELRN LISEEQESKL GFLHIIESD FKPSVALQKL VNCTTGDEKI LIIDIVSIWS QQKQRQHGAI YMNSLSCINI TGLIVFLELL YDSPMDALRR C QVDNFNFQ ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KSGENLYFQM EVLKNIRIYP LSNFITSTKN YINLPNELRN LISEEQESKL GFLHIIESD FKPSVALQKL VNCTTGDEKI LIIDIVSIWS QQKQRQHGAI YMNSLSCINI TGLIVFLELL YDSPMDALRR C QVDNFNFQ LRGIVIDNLS FLNFESDKNY DVINLSKFEK LFKILRKLRE FLGCWIITKS FPTDFYNGIE NTLVDKWSIK RK SGVTLYP TKLPDSYMKG MDLIIYREVV DGRPQYRRIA ALEE

UniProtKB: Platinum sensitivity protein 3

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Macromolecule #5: Suppressor of HU sensitivity involved in recombination protein 1

MacromoleculeName: Suppressor of HU sensitivity involved in recombination protein 1
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 17.138637 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MQFEERLQQL VESDWSLDQS SPNVLVIVLG DTARKYVELG GLKEHVTTNT VAGHVASRER VSVVFLGRVK YLYMYLTRMQ AQANGPQYS NVLVYGLWDL TATQDGPQQL RLLSLVLRQC LSLPSKVEFY PEPPSSSVPA RLLRFWDHII R

UniProtKB: Suppressor of HU sensitivity involved in recombination protein 1

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Macromolecule #6: Suppressor of hydroxyurea sensitivity protein 2

MacromoleculeName: Suppressor of hydroxyurea sensitivity protein 2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 30.179885 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KSGENLYFQG SKDVIEYSKL FAKLVNTNDD TKLDDTIASF LYYMFPRELF IRAISLLES SDMFIYILDR VHNKEGNEHT SLIDVLVDEF YKGSSNSLLE YRLIVKDTND GAPPILVDIA HWFCSCEEFC K YFHEALEK ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KSGENLYFQG SKDVIEYSKL FAKLVNTNDD TKLDDTIASF LYYMFPRELF IRAISLLES SDMFIYILDR VHNKEGNEHT SLIDVLVDEF YKGSSNSLLE YRLIVKDTND GAPPILVDIA HWFCSCEEFC K YFHEALEK TDEKEELHDV LINEVDDHLQ FSDDRFAQLD PHSLSKQWYF KFDKVCCSHL LAFSILLRSS INVLKFFTVN SN KVFVIAI DNIDEWLNLH INIVE

UniProtKB: Suppressor of hydroxyurea sensitivity protein 2

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Macromolecule #7: DNA repair protein RAD51

MacromoleculeName: DNA repair protein RAD51 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 45.239727 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHHHHHHHHG ENLYFQGSMS QVQEQHISES QLQYGNGSLM STVPADLSQS VVDGNGNGSS EDIEATNGSG DGGGLQEQAE AQGEMEDEA YDEAALGSFV PIEKLQVNGI TMADVKKLRE SGLHTAEAVA YAPRKDLLEI KGISEAKADK LLNEAARLVP M GFVTAADF ...String:
MHHHHHHHHG ENLYFQGSMS QVQEQHISES QLQYGNGSLM STVPADLSQS VVDGNGNGSS EDIEATNGSG DGGGLQEQAE AQGEMEDEA YDEAALGSFV PIEKLQVNGI TMADVKKLRE SGLHTAEAVA YAPRKDLLEI KGISEAKADK LLNEAARLVP M GFVTAADF HMRRSELICL TTGSKNLDTL LGGGVETGSI TELFGEFRTG KSQLCHTLAV TCQIPLDIGG GEGKCLYIDT EG TFRPVRL VSIAQRFGLD PDDALNNVAY ARAYNADHQL RLLDAAAQMM SESRFSLIVV DSVMALYRTD FSGRGELSAR QMH LAKFMR ALQRLADQFG VAVVVTNQVV AQVDGGMAFN PDPKKPIGGN IMAHSSTTRL GFKKGKGCQR LCKVVDSPCL PEAE CVFAI YEDGVGDPRE EDE

UniProtKB: DNA repair protein RAD51

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Macromolecule #8: ssDNA (12-mer)

MacromoleculeName: ssDNA (12-mer) / type: dna / ID: 8 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 3.605356 KDa
SequenceString:
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 4 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #11: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 2 / 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 #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / 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

BufferpH: 7.2
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 56.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 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: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 155157
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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