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- EMDB-45387: Cryo-EM structure of the TRRAP lobe of the native human TIP60 com... -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-45387
TitleCryo-EM structure of the TRRAP lobe of the native human TIP60 complex (composite structure)
Map data
Sample
  • Complex: TIP60 complex
    • Complex: TRRAP lobe of the TIP60 complex
      • Protein or peptide: E1A-binding protein p400
      • Protein or peptide: Isoform 2 of Transformation/transcription domain-associated protein
  • Ligand: INOSITOL HEXAKISPHOSPHATE
Keywordshistone acetyltransferase / chromatin regulator / transcription regulation / GENE REGULATION
Function / homology
Function and homology information


transcription factor TFTC complex / Swr1 complex / protein antigen binding / regulation of double-strand break repair / SAGA complex / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / NuA4 histone acetyltransferase complex / regulation of RNA splicing / positive regulation of double-strand break repair via homologous recombination ...transcription factor TFTC complex / Swr1 complex / protein antigen binding / regulation of double-strand break repair / SAGA complex / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / NuA4 histone acetyltransferase complex / regulation of RNA splicing / positive regulation of double-strand break repair via homologous recombination / regulation of DNA repair / transcription coregulator activity / Formation of the beta-catenin:TCF transactivating complex / helicase activity / DNA Damage/Telomere Stress Induced Senescence / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / nucleosome / HATs acetylate histones / chromatin organization / regulation of apoptotic process / hydrolase activity / Ub-specific processing proteases / regulation of cell cycle / nuclear speck / DNA repair / chromatin binding / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / Golgi apparatus / DNA binding / nucleoplasm / ATP binding / nucleus
Similarity search - Function
E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains / HSA domain / Helicase/SANT-associated domain ...E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / : / PIK-related kinase, FAT / FAT domain / FATC / FATC domain / PIK-related kinase / FAT domain profile. / FATC domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / SANT/Myb domain / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Helicase conserved C-terminal domain / Armadillo-like helical / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Armadillo-type fold / Protein kinase-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
E1A-binding protein p400 / Transformation/transcription domain-associated protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.05 Å
AuthorsLouder RK / Park G / Patel AB
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: To Be Published
Title: Structural divergence of H2A.Z-associated human chromatin remodelers SRCAP and TIP60
Authors: Park G / Patel AB / Wu C / Louder RK
History
DepositionJun 17, 2024-
Header (metadata) releaseJun 18, 2025-
Map releaseJun 18, 2025-
UpdateJun 18, 2025-
Current statusJun 18, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45387.png

Downloads & links

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Map

FileDownload / File: emd_45387.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.93 Å/pix.
x 384 pix.
= 355.2 Å		0.93 Å/pix.
x 384 pix.
= 355.2 Å		0.93 Å/pix.
x 384 pix.
= 355.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.925 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.07970362 - 2.3098075
Average (Standard dev.)0.0013697153 (±0.026499)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 355.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : TIP60 complex

EntireName: TIP60 complex
Components
  • Complex: TIP60 complex
    • Complex: TRRAP lobe of the TIP60 complex
      • Protein or peptide: E1A-binding protein p400
      • Protein or peptide: Isoform 2 of Transformation/transcription domain-associated protein
  • Ligand: INOSITOL HEXAKISPHOSPHATE

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Supramolecule #1: TIP60 complex

SupramoleculeName: TIP60 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human) / Strain: K-562 / Organ: BLOOD / Tissue: BONE MARROW / Organelle: NUCLEUS / Location in cell: NUCLEOPLASM
Molecular weightTheoretical: 1.8 MDa

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Supramolecule #2: TRRAP lobe of the TIP60 complex

SupramoleculeName: TRRAP lobe of the TIP60 complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human) / Strain: K-562 / Organ: BLOOD / Tissue: BONE MARROW / Organelle: NUCLEUS / Location in cell: NUCLEOPLASM

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Macromolecule #1: E1A-binding protein p400

MacromoleculeName: E1A-binding protein p400 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human) / Organ: BLOOD / Tissue: BONE MARROW
Molecular weightTheoretical: 343.867312 KDa
SequenceString: MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS YIQVTSPLSQ QVQTQSPTQP SPGPGQALQN VRAGAPGPGL G LCSSSPTG ...String:
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS YIQVTSPLSQ QVQTQSPTQP SPGPGQALQN VRAGAPGPGL G LCSSSPTG GFVDASVLVR QISLSPSSGG HFVFQDGSGL TQIAQGAQVQ LQHPGTPITV RERRPSQPHT QSGGTIHHLG PQ SPAAAGG AGLQPLASPS HITTANLPPQ ISSIIQGQLV QQQQVLQGPP LPRPLGFERT PGVLLPGAGG AAGFGMTSPP PPT SPSRTA VPPGLSSLPL TSVGNTGMKK VPKKLEEIPP ASPEMAQMRK QCLDYHYQEM QALKEVFKEY LIELFFLQHF QGNM MDFLA FKKKHYAPLQ AYLRQNDLDI EEEEEEEEEE EEKSEVINDE VKVVTGKDGQ TGTPVAIATQ LPPKVSAAFS SQQQP FQQA LAGSLVAGAG STVETDLFKR QQAMPSTGMA EQSKRPRLEV GHQGVVFQHP GADAGVPLQQ LMPTAQGGMP PTPQAA QLA GQRQSQQQYD PSTGPPVQNA ASLHTPLPQL PGRLPPAGVP TAALSSALQF AQQPQVVEAQ TQLQIPVKTQ QPNVPIP AP PSSQLPIPPS QPAQLALHVP TPGKVQVQAS QLSSLPQMVA STRLPVDPAP PCPRPLPTSS TSSLAPVSGS GPGPSPAR S SPVNRPSSAT NKALSPVTSR TPGVVASAPT KPQSPAQNAT SSQDSSQDTL TEQITLENQV HQRIAELRKA GLWSQRRLP KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL VRTVVRHHEE KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVE IKLRVELEEK RKKALNLQKV SRRGKELRPK GFDALQESSL DSGMSGRKRK ASISLTDDEV DDEEETIEEE E ANEGVVDH QTELSNLAKE AELPLLDLMK LYEGAFLPSS QWPRPKPDGE DTSGEEDADD CPGDRESRKD LVLIDSLFIM DQ FKAAERM NIGKPNAKDI ADVTAVAEAI LPKGSARVTT SVKFNAPSLL YGALRDYQKI GLDWLAKLYR KNLNGILADE AGL GKTVQI IAFFAHLACN EGNWGPHLVV VRSCNILKWE LELKRWCPGL KILSYIGSHR ELKAKRQEWA EPNSFHVCIT SYTQ FFRGL TAFTRVRWKC LVIDEMQRVK GMTERHWEAV FTLQSQQRLL LIDSPLHNTF LELWTMVHFL VPGISRPYLS SPLRA PSEE SQDYYHKVVI RLHRVTQPFI LRRTKRDVEK QLTKKYEHVL KCRLSNRQKA LYEDVILQPG TQEALKSGHF VNVLSI LVR LQRICNHPGL VEPRHPGSSY VAGPLEYPSA SLILKALERD FWKEADLSMF DLIGLENKIT RHEAELLSKK KIPRKLM EE ISTSAAPAAR PAAAKLKASR LFQPVQYGQK PEGRTVAFPS THPPRTAAPT TASAAPQGPL RGRPPIATFS ANPEAKAA A APFQTSQASA SAPRHQPASA SSTAASPAHP AKLRAQTTAQ ASTPGQPPPQ PQAPSHAAGQ SALPQRLVLP SQAQARLPS GEVVKIAQLA SITGPQSRVA QPETPVTLQF QGSKFTLSHS QLRQLTAGQP LQLQGSVLQI VSAPGQPYLR APGPVVMQTV SQAGAVHGA LGSKPPAGGP SPAPLTPQVG VPGRVAVNAL AVGEPGTASK PASPIGGPTQ EEKTRLLKER LDQIYLVNER R CSQAPVYG RDLLRICALP SHGRVQWRGS LDGRRGKEAG PAHSYTSSSE SPSELMLTLC RCGESLQDVI DRVAFVIPPV VA APPSLRV PRPPPLYSHR MRILRQGLRE HAAPYFQQLR QTTAPRLLQF PELRLVQFDS GKLEALAILL QKLKSEGRRV LIL SQMILM LDILEMFLNF HYLTYVRIDE NASSEQRQEL MRSFNRDRRI FCAILSTHSR TTGINLVEAD TVVFYDNDLN PVMD AKAQE WCDRIGRCKD IHIYRLVSGN SIEEKLLKNG TKDLIREVAA QGNDYSMAFL TQRTIQELFE VYSPMDDAGF PVKAE EFVV LSQEPSVTET IAPKIARPFI EALKSIEYLE EDAQKSAQEG VLGPHTDALS SDSENMPCDE EPSQLEELAD FMEQLT PIE KYALNYLELF HTSIEQEKER NSEDAVMTAV RAWEFWNLKT LQEREARLRL EQEEAELLTY TREDAYSMEY VYEDVDG QT EVMPLWTPPT PPQDDSDIYL DSVMCLMYEA TPIPEAKLPP VYVRKERKRH KTDPSAAGRK KKQRHGEAVV PPRSLFDR A TPGLLKIRRE GKEQKKNILL KQQVPFAKPL PTFAKPTAEP GQDNPEWLIS EDWALLQAVK QLLELPLNLT IVSPAHTPN WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA QDENATHTQL YTSHFDLMKM TAGKRSPPIK PLLGMNPFQ KNPKHASVLA ESGINYDKPL PPIQVASLRA ERIAKEKKAL ADQQKAQQPA VAQPPPPQPQ PPPPPQQPPP P LPQPQAAG SQPPAGPPAV QPQPQPQPQT QPQPVQAPAK AQPAITTGGS AAVLAGTIKT SVTGTSMPTG AVSGNVIVNT IA GVPAATF QSINKRLASP VAPGALTTPG GSAPAQVVHT QPPPRAVGSP ATATPDLVSM ATTQGVRAVT SVTASAVVTT NLT PVQTPA RSLVPQVSQA TGVQLPGKTI TPAHFQLLRQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQTT TTSQVQVPQI QGQA QSPAQ IKAVGKLTPE HLIKMQKQKL QMPPQPPPPQ AQSAPPQPTA QVQVQTSQPP QQQSPQLTTV TAPRPGALLT GTTVA NLQV ARLTRVPTSQ LQAQGQMQTQ APQPAQVALA KPPVVSVPAA VVSSPGVTTL PMNVAGISVA IGQPQKAAGQ TVVAQP VHM QQLLKLKQQA VQQQKAIQPQ AAQGPAAVQQ KITAQQITTP GAQQKVAYAA QPALKTQFLT TPISQAQKLA GAQQVQT QI QVAKLPQVVQ QQTPVASIQQ VASASQQASP QTVALTQATA AGQQVQMIPA VTATAQVVQQ KLIQQQVVTT ASAPLQTP G APNPAQVPAS SDSPSQQPKL QMRVPAVRLK TPTKPPCQ

UniProtKB: E1A-binding protein p400

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Macromolecule #2: Isoform 2 of Transformation/transcription domain-associated protein

MacromoleculeName: Isoform 2 of Transformation/transcription domain-associated protein
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: BLOOD / Tissue: BONE MARROW
Molecular weightTheoretical: 434.949906 KDa
SequenceString: MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST FLEHIIPRFL TFLQDGEVQF LQEKPAQQL RKLVLEIIHR IPTNEHLRPH TKNVLSVMFR FLETENEENV LICLRIIIEL HKQFRPPITQ EIHHFLDFVK Q IYKELPKV ...String:
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST FLEHIIPRFL TFLQDGEVQF LQEKPAQQL RKLVLEIIHR IPTNEHLRPH TKNVLSVMFR FLETENEENV LICLRIIIEL HKQFRPPITQ EIHHFLDFVK Q IYKELPKV VNRYFENPQV IPENTVPPPE MVGMITTIAV KVNPEREDSE TRTHSIIPRG SLSLKVLAEL PIIVVLMYQL YK LNIHNVV AEFVPLIMNT IAIQVSAQAR QHKLYNKELY ADFIAAQIKT LSFLAYIIRI YQELVTKYSQ QMVKGMLQLL SNC PAETAH LRKELLIAAK HILTTELRNQ FIPCMDKLFD ESILIGSGYT ARETLRPLAY STLADLVHHV RQHLPLSDLS LAVQ LFAKN IDDESLPSSI QTMSCKLLLN LVDCIRSKSE QESGNGRDVL MRMLEVFVLK FHTIARYQLS AIFKKCKPQS ELGAV EAAL PGVPTAPAAP GPAPSPAPVP APPPPPPPPP PATPVTPAPV PPFEKQGEKD KEDKQTFQVT DCRSLVKTLV CGVKTI TWG ITSCKAPGEA QFIPNKQLQP KETQIYIKLV KYAMQALDIY QVQIAGNGQT YIRVANCQTV RMKEEKEVLE HFAGVFT MM NPLTFKEIFQ TTVPYMVERI SKNYALQIVA NSFLANPTTS ALFATILVEY LLDRLPEMGS NVELSNLYLK LFKLVFGS V SLFAAENEQM LKPHLHKIVN SSMELAQTAK EPYNYFLLLR ALFRSIGGGS HDLLYQEFLP LLPNLLQGLN MLQSGLHKQ HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT LVSQGLRTLE LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISH VAYRVLGKFG GSNRKMLKES QKLHYVVTEV QGPSITVEFS DCKASLQLPM EKAIETALDC LKSANTEPYY R RQAWEVIK CFLVAMMSLE DNKHALYQLL AHPNFTEKTI PNVIISHRYK AQDTPARKTF EQALTGAFMS AVIKDLRPSA LP FVASLIR HYTMVAVAQQ CGPFLLPCYQ VGSQPSTAMF HSEENGSKGM DPLVLIDAIA ICMAYEEKEL CKIGEVALAV IFD VASIIL GSKERACQLP LFSYIVERLC ACCYEQAWYA KLGGVVSIKF LMERLPLTWV LQNQQTFLKA LLFVMMDLTG EVSN GAVAM AKTTLEQLLM RCATPLKDEE RAEEIVAAQE KSFHHVTHDL VREVTSPNST VRKQAMHSLQ VLAQVTGKSV TVIME PHKE VLQDMVPPKK HLLRHQPANA QIGLMEGNTF CTTLQPRLFT MDLNVVEHKV FYTELLNLCE AEDSALTKLP CYKSLP SLV PLRIAALNAL AACNYLPQSR EKIIAALFKA LNSTNSELQE AGEACMRKFL EGATIEVDQI HTHMRPLLMM LGDYRSL TL NVVNRLTSVT RLFPNSFNDK FCDQMMQHLR KWMEVVVITH KGGQRSDGNE MKICSAIINL FHLIPAAPQT LVKPLLEV V MKTERAMLIE AGSPFREPLI KFLTRHPSQT VELFMMEATL NDPQWSRMFM SFLKHKDARP LRDVLAANPN RFITLLLPG GAQTAVRPGS PSTSTMRLDL QFQAIKIISI IVKNDDSWLA SQHSLVSQLR RVWVSENFQE RHRKENMAAT NWKEPKLLAY CLLNYCKRN YGDIELLFQL LRAFTGRFLC NMTFLKEYME EEIPKNYSIA QKRALFFRFV DFNDPNFGDE LKAKVLQHIL N PAFLYSFE KGEGEQLLGP PNPEGDNPES ITSVFITKVL DPEKQADMLD SLRIYLLQYA TLLVEHAPHH IHDNNKNRNS KL RRLMTFA WPCLLSKACV DPACKYSGHL LLAHIIAKFA IHKKIVLQVF HSLLKAHAME ARAIVRQAMA ILTPAVPARM EDG HQMLTH WTRKIIVEEG HTVPQLVHIL HLIVQHFKVY YPVRHHLVQH MVSAMQRLGF TPSVTIEQRR LAVDLSEVVI KWEL QRIKD QQPDSDMDPN SSGEGVNSVS SSIKRGLSVD SAQEVKRFRT ATGAISAVFG RSQSLPGADS LLAKPIDKQH TDTVV NFLI RVACQVNDNT NTAGSPGEVL SRRCVNLLKT ALRPDMWPKS ELKLQWFDKL LMTVEQPNQV NYGNICTGLE VLSFLL TVL QSPAILSSFK PLQRGIAACM TCGNTKVLRA VHSLLSRLMS IFPTEPSTSS VASKYEELEC LYAAVGKVIY EGLTNYE KA TNANPSQLFG TLMILKSACS NNPSYIDRLI SVFMRSLQKM VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVM S MEMRKNFIQA ILTSLIEKSP DAKILRAVVK IVEEWVKNNS PMAANQTPTL REKSILLVKM MTYIEKRFPE DLELNAQFL DLVNYVYRDE TLSGSELTAK LEPAFLSGLR CAQPLIRAKF FEVFDNSMKR RVYERLLYVT CSQNWEAMGN HFWIKQCIEL LLAVCEKST PIGTSCQGAM LPSITNVINL ADSHDRAAFA MVTHVKQEPR ERENSESKEE DVEIDIELAP GDQTSTPKTK E LSEKDIGN QLHMLTNRHD KFLDTLREVK TGALLSAFVQ LCHISTTLAE KTWVQLFPRL WKILSDRQQH ALAGEISPFL CS GSHQVQR DCQPSALNCF VEAMSQCVPP IPIRPCVLKY LGKTHNLWFR STLMLEHQAF EKGLSLQIKP KQTTEFYEQE SIT PPQQEI LDSLAELYSL LQEEDMWAGL WQKRCKYSET ATAIAYEQHG FFEQAQESYE KAMDKAKKEH ERSNASPAIF PEYQ LWEDH WIRCSKELNQ WEALTEYGQS KGHINPYLVL ECAWRVSNWT AMKEALVQVE VSCPKEMAWK VNMYRGYLAI CHPEE QQLS FIERLVEMAS SLAIREWRRL PHVVSHVHTP LLQAAQQIIE LQEAAQINAG LQPTNLGRNN SLHDMKTVVK TWRNRL PIV SDDLSHWSSI FMWRQHHYQA IVTAYENSSQ HDPSSNNAML GVHASASAII QYGKIARKQG LVNVALDILS RIHTIPT VP IVDCFQKIRQ QVKCYLQLAG VMGKNECMQG LEVIESTNLK YFTKEMTAEF YALKGMFLAQ INKSEEANKA FSAAVQMH D VLVKAWAMWG DYLENIFVKE RQLHLGVSAI TCYLHACRHQ NESKSRKYLA KVLWLLSFDD DKNTLADAVD KYCIGVPPI QWLAWIPQLL TCLVGSEGKL LLNLISQVGR VYPQAVYFPI RTLYLTLKIE QRERYKSDPG PIRATAPMWR CSRIMHMQRE LHPTLLSSL EGIVDQMVWF RENWHEEVLR QLQQGLAKCY SVAFEKSGAV SDAKITPHTL NFVKKLVSTF GVGLENVSNV S TMFSSAAS ESLARRAQAT AQDPVFQKLK GQFTTDFDFS VPGSMKLHNL ISKLKKWIKI LEAKTKQLPK FFLIEEKCRF LS NFSAQTA EVEIPGEFLM PKPTHYYIKI ARFMPRVEIV QKHNTAARRL YIRGHNGKIY PYLVMNDACL TESRREERVL QLL RLLNPC LEKRKETTKR HLFFTVPRVV AVSPQMRLVE DNPSSLSLVE IYKQRCAKKG IEHDNPISRY YDRLATVQAR GTQA SHQVL RDILKEVQSN MVPRSMLKEW ALHTFPNATD YWTFRKMFTI QLALIGFAEF VLHLNRLNPE MLQIAQDTGK LNVAY FRFD INDATGDLDA NRPVPFRLTP NISEFLTTIG VSGPLTASMI AVARCFAQPN FKVDGILKTV LRDEIIAWHK KTQEDT SSP LSAAGQPENM DSQQLVSLVQ KAVTAIMTRL HNLAQFEGGE SKVNTLVAAA NSLDNLCRMD PAWHPWL

UniProtKB: Transformation/transcription domain-associated protein

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Macromolecule #3: INOSITOL HEXAKISPHOSPHATE

MacromoleculeName: INOSITOL HEXAKISPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: IHP
Molecular weightTheoretical: 660.035 Da
Chemical component information

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

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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: 7.6
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: 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: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.05 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 106666
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION

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