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- EMDB-50201: Human condensin II - M18BP1 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-50201
TitleHuman condensin II - M18BP1 complex
Map data
Sample
  • Complex: Human condensin II holocomplex bound to M18BP1 fragment
    • Protein or peptide: Structural maintenance of chromosomes protein 2
    • Protein or peptide: Structural maintenance of chromosomes protein 4
    • Protein or peptide: Condensin-2 complex subunit D3
    • Protein or peptide: Condensin-2 complex subunit H2
    • Protein or peptide: Maltose/maltodextrin-binding periplasmic protein,Mis18-binding protein 1
    • Protein or peptide: Condensin-2 complex subunit G2
KeywordsChromosome organisation complex / DNA BINDING PROTEIN
Function / homology
Function and homology information


histone H4K20me1 reader activity / female meiosis chromosome separation / positive regulation of chromosome condensation / positive regulation of chromosome separation / meiotic chromosome condensation / positive regulation of chromosome segregation / condensin complex / kinetochore organization / bHLH transcription factor binding / meiotic chromosome segregation ...histone H4K20me1 reader activity / female meiosis chromosome separation / positive regulation of chromosome condensation / positive regulation of chromosome separation / meiotic chromosome condensation / positive regulation of chromosome segregation / condensin complex / kinetochore organization / bHLH transcription factor binding / meiotic chromosome segregation / mitotic sister chromatid separation / condensed chromosome, centromeric region / mitotic chromosome condensation / Condensation of Prometaphase Chromosomes / chromosome condensation / inner cell mass cell proliferation / nuclear chromosome / detection of maltose stimulus / maltose transport complex / carbohydrate transport / mitotic sister chromatid segregation / chromosome, centromeric region / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / pericentric heterochromatin / intercellular bridge / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / condensed chromosome / Deposition of new CENPA-containing nucleosomes at the centromere / ATP-binding cassette (ABC) transporter complex / erythrocyte differentiation / Condensation of Prophase Chromosomes / condensed nuclear chromosome / cell chemotaxis / cell junction / single-stranded DNA binding / T cell differentiation in thymus / outer membrane-bounded periplasmic space / histone binding / transcription by RNA polymerase II / periplasmic space / nuclear speck / cell division / DNA damage response / chromatin binding / chromatin / nucleolus / ATP hydrolysis activity / DNA binding / extracellular exosome / nucleoplasm / ATP binding / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
Condensin II complex subunit H2, N-terminal / Condensin-2 complex subunit D3 / Condensin-2 complex subunit G2 / Condensin II complex subunit H2, middle domain / Condensin-2 complex subunit H2, C-terminal / Condensin-2 complex subunit H2 / Condensin II complex subunit CAP-H2 or CNDH2, N-terminal / Condensin II non structural maintenance of chromosomes subunit / Condensin II complex subunit CAP-H2 or CNDH2, C-terminal wHTH domain / Condensin II complex subunit CAP-H2 or CNDH2, mid domain ...Condensin II complex subunit H2, N-terminal / Condensin-2 complex subunit D3 / Condensin-2 complex subunit G2 / Condensin II complex subunit H2, middle domain / Condensin-2 complex subunit H2, C-terminal / Condensin-2 complex subunit H2 / Condensin II complex subunit CAP-H2 or CNDH2, N-terminal / Condensin II non structural maintenance of chromosomes subunit / Condensin II complex subunit CAP-H2 or CNDH2, C-terminal wHTH domain / Condensin II complex subunit CAP-H2 or CNDH2, mid domain / SANT associated / KNL2-like / SANTA (SANT Associated) / Condensin subunit 1/Condensin-2 complex subunit D3 / Condensin complex subunit 1, C-terminal / non-SMC mitotic condensation complex subunit 1 / Smc2, ATP-binding cassette domain / Structural maintenance of chromosomes protein / SMCs flexible hinge / SMCs flexible hinge superfamily / SMC proteins Flexible Hinge Domain / SMC proteins Flexible Hinge Domain / RecF/RecN/SMC, N-terminal / RecF/RecN/SMC N terminal domain / SANT domain profile. / SANT domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / SANT/Myb domain / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Homeobox-like domain superfamily / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Structural maintenance of chromosomes protein 2 / Maltose/maltodextrin-binding periplasmic protein / Condensin-2 complex subunit D3 / Condensin-2 complex subunit H2 / Mis18-binding protein 1 / Condensin-2 complex subunit G2 / Structural maintenance of chromosomes protein 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.5 Å
AuthorsBorsellini A / Vannini A
Funding supportEuropean Union, 1 items
OrganizationGrant numberCountry
European Molecular Biology Organization (EMBO)European Union
CitationJournal: To Be Published
Title: Condensin II activation by M18BP1
Authors: Borsellini A / Conti D / Cutts E / Harris RJ / Walstein K / Graziadei A / Cecatiello V / Aarts TF / Xie R / Mazouzi A / Sen S / Hoencamp C / Pleuger R / Ghetti S / Oberste-Lehn L / Pan D / ...Authors: Borsellini A / Conti D / Cutts E / Harris RJ / Walstein K / Graziadei A / Cecatiello V / Aarts TF / Xie R / Mazouzi A / Sen S / Hoencamp C / Pleuger R / Ghetti S / Oberste-Lehn L / Pan D / Bange T / Haarhuis JHI / Perrakis A / Brummelkamp TR / Rowland BD / Musacchio A / Vannini A
History
DepositionApr 30, 2024-
Header (metadata) releaseJul 2, 2025-
Map releaseJul 2, 2025-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50201.png

Downloads & links

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Map

FileDownload / File: emd_50201.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.4 Å/pix.
x 160 pix.
= 384. Å		2.4 Å/pix.
x 160 pix.
= 384. Å		2.4 Å/pix.
x 160 pix.
= 384. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.4 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0248
Minimum - Maximum-0.032785103 - 0.124920234
Average (Standard dev.)0.0007828406 (±0.004783455)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions160160160
Spacing160160160
CellA=B=C: 384.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_50201_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_50201_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human condensin II holocomplex bound to M18BP1 fragment

EntireName: Human condensin II holocomplex bound to M18BP1 fragment
Components
  • Complex: Human condensin II holocomplex bound to M18BP1 fragment
    • Protein or peptide: Structural maintenance of chromosomes protein 2
    • Protein or peptide: Structural maintenance of chromosomes protein 4
    • Protein or peptide: Condensin-2 complex subunit D3
    • Protein or peptide: Condensin-2 complex subunit H2
    • Protein or peptide: Maltose/maltodextrin-binding periplasmic protein,Mis18-binding protein 1
    • Protein or peptide: Condensin-2 complex subunit G2

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Supramolecule #1: Human condensin II holocomplex bound to M18BP1 fragment

SupramoleculeName: Human condensin II holocomplex bound to M18BP1 fragment
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Structural maintenance of chromosomes protein 2

MacromoleculeName: Structural maintenance of chromosomes protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 135.872141 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKK QSPLGFEVHD EITVTRQVVI GGRNKYLING VNANNTRVQD LFCSVGLNVN NPHFLIMQGR ITKVLNMKPP E ILSMIEEA ...String:
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKK QSPLGFEVHD EITVTRQVVI GGRNKYLING VNANNTRVQD LFCSVGLNVN NPHFLIMQGR ITKVLNMKPP E ILSMIEEA AGTRMYEYKK IAAQKTIEKK EAKLKEIKTI LEEEITPTIQ KLKEERSSYL EYQKVMREIE HLSRLYIAYQ FL LAEDTKV RSAEELKEMQ DKVIKLQEEL SENDKKIKAL NHEIEELEKR KDKETGGILR SLEDALAEAQ RVNTKSQSAF DLK KKNLAC EESKRKELEK NMVEDSKTLA AKEKEVKKIT DGLHALQEAS NKDAEALAAA QQHFNAVSAG LSSNEDGAEA TLAG QMMAC KNDISKAQTE AKQAQMKLKH AQQELKNKQA EVKKMDSGYR KDQEALEAVK RLKEKLEAEM KKLNYEENKE ESLLE KRRQ LSRDIGRLKE TYEALLARFP NLRFAYKDPE KNWNRNCVKG LVASLISVKD TSATTALELV AGERLYNVVV DTEVTG KKL LERGELKRRY TIIPLNKISA RCIAPETLRV AQNLVGPDNV HVALSLVEYK PELQKAMEFV FGTTFVCDNM DNAKKVA FD KRIMTRTVTL GGDVFDPHGT LSGGARSQAA SILTKFQELK DVQDELRIKE NELRALEEEL AGLKNTAEKY RQLKQQWE M KTEEADLLQT KLQQSSYHKQ QEELDALKKT IEESEETLKN TKEIQRKAEE KYEVLENKMK NAEAEREREL KDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVI KAKYAEVAKH KEQNNDSQLK IKELDHNISK HKREAEDGAA KVSKMLKDYD WINAERHLFG QPNSAYDFKT N NPKEAGQR LQKLQEMKEK LGRNVNMRAM NVLTEAEERY NDLMKKKRIV ENDKSKILTT IEDLDQKKNQ ALNIAWQKVN KD FGSIFST LLPGANAMLA PPEGQTVLDG LEFKVALGNT WKENLTELSG GQRSLVALSL ILSMLLFKPA PIYILDEVDA ALD LSHTQN IGQMLRTHFT HSQFIVVSLK EGMFNNANVL FKTKFVDGVS TVARFTQCQN GKISKEAKSK AKPPKGAHVE V

UniProtKB: Structural maintenance of chromosomes protein 2

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Macromolecule #2: Structural maintenance of chromosomes protein 4

MacromoleculeName: Structural maintenance of chromosomes protein 4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 149.551078 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: HHHHHHHHHH LEVLFQGPPR KGTQPSTARR REEGPPPPSP DGASSDAEPE PPSGRTESPA TAAETASEEL DNRSLEEILN SIPPPPPPA MTNEAGAPRL MITHIVNQNF KSYAGEKILG PFHKRFSCII GPNGSGKSNV IDSMLFVFGY RAQKIRSKKL S VLIHNSDE ...String:
HHHHHHHHHH LEVLFQGPPR KGTQPSTARR REEGPPPPSP DGASSDAEPE PPSGRTESPA TAAETASEEL DNRSLEEILN SIPPPPPPA MTNEAGAPRL MITHIVNQNF KSYAGEKILG PFHKRFSCII GPNGSGKSNV IDSMLFVFGY RAQKIRSKKL S VLIHNSDE HKDIQSCTVE VHFQKIIDKE GDDYEVIPNS NFYVSRTACR DNTSVYHISG KKKTFKDVGN LLRSHGIDLD HN RFLILQG EVEQIAMMKP KGQTEHDEGM LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG EKN IAIEFL TLENEIFRKK NHVCQYYIYE LQKRIAEMET QKEKIHEDTK EINEKSNILS NEMKAKNKDV KDTEKKLNKI TKFI EENKE KFTQLDLEDV QVREKLKHAT SKAKKLEKQL QKDKEKVEEF KSIPAKSNNI INETTTRNNA LEKEKEKEEK KLKEV MDSL KQETQGLQKE KESREKELMG FSKSVNEARS KMDVAQSELD IYLSRHNTAV SQLTKAKEAL IAASETLKER KAAIRD IEG KLPQTEQELK EKEKELQKLT QEETNFKSLV HDLFQKVEEA KSSLAMNRSR GKVLDAIIQE KKSGRIPGIY GRLGDLG AI DEKYDVAISS CCHALDYIVV DSIDIAQECV NFLKRQNIGV ATFIGLDKMA VWAKKMTEIQ TPENTPRLFD LVKVKDEK I RQAFYFALRD TLVADNLDQA TRVAYQKDRR WRVVTLQGQI IEQSGTMTGG GSKVMKGRMG SSLVIEISEE EVNKMESQL QNDSKKAMQI QEQKVQLEER VVKLRHSERE MRNTLEKFTA SIQRLIEQEE YLNVQVKELE ANVLATAPDK KKQKLLEENV SAFKTEYDA VAEKAGKVEA EVKRLHNTIV EINNHKLKAQ QDKLDKINKQ LDECASAITK AQVAIKTADR NLQKAQDSVL R TEKEIKDT EKEVDDLTAE LKSLEDKAAE VVKNTNAAEE SLPEIQKEHR NLLQELKVIQ ENEHALQKDA LSIKLKLEQI DG HIAEHNS KIKYWHKEIS KISLHPIEDN PIEEISVLSP EDLEAIKNPD SITNQIALLE ARCHEMKPNL GAIAEYKKKE ELY LQRVAE LDKITYERDS FRQAYEDLRK QRLNEFMAGF YIITNKLKEN YQMLTLGGDA ELELVDSLDP FSEGIMFSVR PPKK SWKKI FNLSGGEKTL SSLALVFALH HYKPTPLYFM DEIDAALDFK NVSIVAFYIY EQTKNAQFII ISLRNNMFEI SDRLI GIYK TYNITKSVAV NPKEIASKGL C

UniProtKB: Structural maintenance of chromosomes protein 4

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Macromolecule #3: Condensin-2 complex subunit D3

MacromoleculeName: Condensin-2 complex subunit D3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 169.109938 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MVALRGLGSG LQPWCPLDLR LEWVDTVWEL DFTETEPLDP SIEAEIIETG LAAFTKLYES LLPFATGEHG SMESIWTFFI ENNVSHSTL VALFYHFVQI VHKKNVSVQY REYGLHAAGL YFLLLEVPGS VANQVFHPVM FDKCIQTLKK SWPQESNLNR K RKKEQPKS ...String:
MVALRGLGSG LQPWCPLDLR LEWVDTVWEL DFTETEPLDP SIEAEIIETG LAAFTKLYES LLPFATGEHG SMESIWTFFI ENNVSHSTL VALFYHFVQI VHKKNVSVQY REYGLHAAGL YFLLLEVPGS VANQVFHPVM FDKCIQTLKK SWPQESNLNR K RKKEQPKS SQANPGRHRK RGKPPRREDI EMDEIIEEQE DENICFSARD LSQIRNAIFH LLKNFLRLLP KFSLKEKPQC VQ NCIEVFV SLTNFEPVLH ECHVTQARAL NQAKYIPELA YYGLYLLCSP IHGEGDKVIS CVFHQMLSVI LMLEVGEGSH RAP LAVTSQ VINCRNQAVQ FISALVDELK ESIFPVVRIL LQHICAKVVD KSEYRTFAAQ SLVQLLSKLP CGEYAMFIAW LYKY SRSSK IPHRVFTLDV VLALLELPER EVDNTLSLEH QKFLKHKFLV QEIMFDRCLD KAPTVRSKAL SSFAHCLELT VTSAS ESIL ELLINSPTFS VIESHPGTLL RNSSAFSYQR QTSNRSEPSG EINIDSSGET VGSGERCVMA MLRRRIRDEK TNVRKS ALQ VLVSILKHCD VSGMKEDLWI LQDQCRDPAV SVRKQALQSL TELLMAQPRC VQIQKAWLRG VVPVVMDCES TVQEKAL EF LDQLLLQNIR HHSHFHSGDD SQVLAWALLT LLTTESQELS RYLNKAFHIW SKKEKFSPTF INNVISHTGT EHSAPAWM L LSKIAGSSPR LDYSRIIQSW EKISSQQNPN SNTLGHILCV IGHIAKHLPK STRDKVTDAV KCKLNGFQWS LEVISSAVD ALQRLCRASA ETPAEEQELL TQVCGDVLST CEHRLSNIVL KENGTGNMDE DLLVKYIFTL GDIAQLCPAR VEKRIFLLIQ SVLASSADA DHSPSSQGSS EAPASQPPPQ VRGSVMPSVI RAHAIITLGK LCLQHEDLAK KSIPALVREL EVCEDVAVRN N VIIVMCDL CIRYTIMVDK YIPNISMCLK DSDPFIRKQT LILLTNLLQE EFVKWKGSLF FRFVSTLIDS HPDIASFGEF CL AHLLLKR NPVMFFQHFI ECIFHFNNYE KHEKYNKFPQ SEREKRLFSL KGKSNKERRM KIYKFLLEHF TDEQRFNITS KIC LSILAC FADGILPLDL DASELLSDTF EVLSSKEIKL LAMRSKPDKD LLMEEDDMAL ANVVMQEAQK KLISQVQKRN FIEN IIPII ISLKTVLEKN KIPALRELMH YLREVMQDYR DELKDFFAVD KQLASELEYD MKKYQEQLVQ EQELAKHADV AGTAG GAEV APVAQVALCL ETVPVPAGQE NPAMSPAVSQ PCTPRASAGH VAVSSPTPET GPLQRLLPKA RPMSLSTIAI LNSVKK AVE SKSRHRSRSL GVLPFTLNSG SPEKTCSQVS SYSLEQESNG EIEHVTKRAI STPEKSISDV TFGAGVSYIG TPRTPSS AK EKIEGRSQGN DILCLSLPDK PPPQPQQWNV RSPARNKDTP ACSRRSLRKT PLKTAN

UniProtKB: Condensin-2 complex subunit D3

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Macromolecule #4: Condensin-2 complex subunit H2

MacromoleculeName: Condensin-2 complex subunit H2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.040391 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKR RAKQLSSVQE DRANGVASSG VPQEAENEFL SLDDFPDSRT NVDLKNDQTP SEVLIIPLLP MALVAPDEME K NNNPLYSR ...String:
MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKR RAKQLSSVQE DRANGVASSG VPQEAENEFL SLDDFPDSRT NVDLKNDQTP SEVLIIPLLP MALVAPDEME K NNNPLYSR QGEVLASRKD FRMNTCVPHP RGAFMLEPEG MSPMEPAGVS PMPGTQKDTG RTEEQPMEVS VCRSPVPALG FS QEPGPSP EGPMPLGGGE DEDAEEAVEL PEASAPKAAL EPKESRSPQQ SAALPRRYML REREGAPEPA SCVKETPDPW QSL DPFDSL ESKPFKKGRP YSVPPCVEEA LGQKRKRKGA AKLQDFHQWY LAAYADHADS RRLRRKGPSF ADMEVLYWTH VKEQ LETLR KLQRREVAEQ WLRPAEEDHL EDSLEDLGAA DDFLEPEEYM EPEGADPREA ADLDAVPMSL SYEELVRRNV ELFIA TSQK FVQETELSQR IRDWEDTVQP LLQEQEQHVP FDIHTYGDQL VSRFPQLNEW CPFAELVAGQ PAFEVCRSML ASLQLA NDY TVEITQQPGL EMAVDTMSLR LLTHQRAHKR FQTYAAPSMA QPENLYFQSW SHPQFEKGGG SGGGSGGGSW SHPQFEK

UniProtKB: Condensin-2 complex subunit H2

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Macromolecule #5: Maltose/maltodextrin-binding periplasmic protein,Mis18-binding pr...

MacromoleculeName: Maltose/maltodextrin-binding periplasmic protein,Mis18-binding protein 1
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.917172 KDa
Recombinant expressionOrganism: Rosetta (plant)
SequenceString: MAKIEEGKLV IWINGDKGYN GLAEVGKKFE KDTGIKVTVE HPDKLEEKFP QVAATGDGPD IIFWAHDRFG GYAQSGLLAE ITPDKAFQD KLYPFTWDAV RYNGKLIAYP IAVEALSLIY NKDLLPNPPK TWEEIPALDK ELKAKGKSAL MFNLQEPYFT W PLIAADGG ...String:
MAKIEEGKLV IWINGDKGYN GLAEVGKKFE KDTGIKVTVE HPDKLEEKFP QVAATGDGPD IIFWAHDRFG GYAQSGLLAE ITPDKAFQD KLYPFTWDAV RYNGKLIAYP IAVEALSLIY NKDLLPNPPK TWEEIPALDK ELKAKGKSAL MFNLQEPYFT W PLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TS KVNYGVT VLPTFKGQPS KPFVGVLSAG INAASPNKEL AKEFLENYLL TDEGLEAVNK DKPLGAVALK SYEEELAKDP RIA ATMENA QKGEIMPNIP QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITKGSEN LYFQGSGLIQ DKEWNEKELQ KLHC AFASL PKHKPGFWSE VAAAVGSRSP EECQRKYMEN PRGKGSQKHV TKKKPANSKG QNGKRGDADQ KQTIKITAKV GTLKR KQQM REFLEQLPKD DHDDFFSTTP LQHQRILLPS FQDSEDDDDI LPNMDKNPTT PSSVIFPLVK TPQCQHVSPG MLGSIN RND CDKYVFRMQK YHKSNGGIVW GNIKKKLVET DFSTPTPRRK TPFNTDLGEN SGIGKLFTNA VESLDEEEKD YYFSNSD SA LEHHHHHHHH

UniProtKB: Maltose/maltodextrin-binding periplasmic protein, Mis18-binding protein 1

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Macromolecule #6: Condensin-2 complex subunit G2

MacromoleculeName: Condensin-2 complex subunit G2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 131.135969 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEKRETFVQA VSKELVGEFL QFVQLDKEAS DPFSLNELLD ELSRKQKEEL WQRLKNLLTD VLLESPVDGW QVVEAQGEDN METEHGSKM RKSIEIIYAI TSVILASVSV INESENYEAL LECVIILNGI LYALPESERK LQSSIQDLCV TWWEKGLPAK E DTGKTAFV ...String:
MEKRETFVQA VSKELVGEFL QFVQLDKEAS DPFSLNELLD ELSRKQKEEL WQRLKNLLTD VLLESPVDGW QVVEAQGEDN METEHGSKM RKSIEIIYAI TSVILASVSV INESENYEAL LECVIILNGI LYALPESERK LQSSIQDLCV TWWEKGLPAK E DTGKTAFV MLLRRSLETK TGADVCRLWR IHQALYCFDY DLEESGEIKD MLLECFININ YIKKEEGRRF LSCLFNWNIN FI KMIHGTI KNQLQGLQKS LMVYIAEIYF RAWKKASGKI LEAIENDCIQ DFMFHGIHLP RRSPVHSKVR EVLSYFHHQK KVR QGVEEM LYRLYKPILW RGLKARNSEV RSNAALLFVE AFPIRDPNLH AIEMDSEIQK QFEELYSLLE DPYPMVRSTG ILGV CKITS KYWEMMPPTI LIDLLKKVTG ELAFDTSSAD VRCSVFKCLP MILDNKLSHP LLEQLLPALR YSLHDNSEKV RVAFV DMLL KIKAVRAAKF WKICPMEHIL VRLETDSRPV SRRLVSLIFN SFLPVNQPEE VWCERCVTLV QMNHAAARRF YQYAHE HTA CTNIAKLIHV IRHCLNACIQ RAVREPPEDE EEEDGREKEN VTVLDKTLSV NDVACMAGLL EIIVILWKSI DRSMENN KE AKLYTINKFA SVLPEYLKVF KDDRCKIPLF MLMSFMPASA VPPFSCGVIS TLRSREEGAV DKSYCTLLDC LCSWGQVG H ILELVDNWLP TEHAQAKSNT ASKGRVQIHD TRPVKPELAL VYIEYLLTHP KNRECLLSAP RKKLNHLLKA LETSKADLE SLLQTPGGKP RGFSEAAAPR AFGLHCRLSI HLQHKFCSEG KVYLSMLEDT GFWLESKILS FIQDQEEDYL KLHRVIYQQI IQTYLTVCK DVVMVGLGDH QFQMQLLQRS LGIMQTVKGF FYVSLLLDIL KEITGSSLIQ KTDSDEEVAM LLDTVQKVFQ K MLECIARS FRKQPEEGLR LLYSVQRPLH EFITAVQSRH TDTPVHRGVL STLIAGPVVE ISHQLRKVSD VEELTPPEHL SD LPPFSRC LIGIIIKSSN VVRSFLDELK ACVASNDIEG IVCLTAAVHI ILVINAGKHK SSKVREVAAT VHRKLKTFME ITL EEDSIE RFLYESSSRT LGELLNS

UniProtKB: Condensin-2 complex subunit G2

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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: 8.5
Component:
ConcentrationName
20.0 mMTRIS
150.0 mMNaCl
5.0 mMMgCl2
1.0 mMDTT
0.03 %Octyl beta-D-glucopyranoside
GridModel: Quantifoil / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK II

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: INSILICO MODEL / In silico model: 3D initial model generated in RELION
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 7.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0) / Number images used: 24490
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9f5w:
Human condensin II - M18BP1 complex

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