[English] 日本語
Yorodumi
- EMDB-11693: Human pre-Bact-2 spliceosome core structure -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-11693
TitleHuman pre-Bact-2 spliceosome core structure
Map dataMasked/sharpened map of the pre-Bact-2 spliceosome core structure.
Sample
  • Complex: pre-Bact-2 spliceosomal core structure
    • Complex: pre-Bact-2 spliceosomal core structure
      • Protein or peptide: x 13 types
      • RNA: x 3 types
    • Complex: MINX M3 pre-mRNA
      • RNA: x 1 types
  • Ligand: x 3 types
Function / homology
Function and homology information


microfibril / regulation of retinoic acid receptor signaling pathway / regulation of vitamin D receptor signaling pathway / embryonic brain development / nuclear retinoic acid receptor binding / U2-type catalytic step 1 spliceosome / Prp19 complex / RNA splicing, via transesterification reactions / positive regulation of androgen receptor activity / mRNA 3'-end processing ...microfibril / regulation of retinoic acid receptor signaling pathway / regulation of vitamin D receptor signaling pathway / embryonic brain development / nuclear retinoic acid receptor binding / U2-type catalytic step 1 spliceosome / Prp19 complex / RNA splicing, via transesterification reactions / positive regulation of androgen receptor activity / mRNA 3'-end processing / pre-mRNA binding / mRNA cis splicing, via spliceosome / U2-type spliceosomal complex / U2-type precatalytic spliceosome / positive regulation of mRNA splicing, via spliceosome / U2-type catalytic step 2 spliceosome / positive regulation by host of viral transcription / positive regulation of vitamin D receptor signaling pathway / Transport of Mature mRNA derived from an Intron-Containing Transcript / Notch binding / nuclear vitamin D receptor binding / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RNA Polymerase II Transcription Termination / RUNX3 regulates NOTCH signaling / NOTCH4 Intracellular Domain Regulates Transcription / K63-linked polyubiquitin modification-dependent protein binding / positive regulation of protein targeting to mitochondrion / WD40-repeat domain binding / NOTCH3 Intracellular Domain Regulates Transcription / positive regulation of neurogenesis / precatalytic spliceosome / nuclear androgen receptor binding / Notch-HLH transcription pathway / mRNA Splicing - Minor Pathway / Formation of paraxial mesoderm / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / protein localization to nucleus / spliceosomal tri-snRNP complex assembly / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of G1/S transition of mitotic cell cycle / U5 snRNA binding / U5 snRNP / retinoic acid receptor signaling pathway / Cajal body / U2 snRNA binding / U6 snRNA binding / pre-mRNA intronic binding / U1 snRNA binding / cellular response to retinoic acid / U4/U6 x U5 tri-snRNP complex / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / positive regulation of RNA splicing / RNA splicing / positive regulation of protein export from nucleus / response to cocaine / nuclear receptor coactivator activity / DNA damage checkpoint signaling / nuclear receptor binding / Downregulation of SMAD2/3:SMAD4 transcriptional activity / RNA polymerase II transcription regulatory region sequence-specific DNA binding / spliceosomal complex / protein modification process / NOTCH1 Intracellular Domain Regulates Transcription / protein tag activity / mRNA processing / fibrillar center / mRNA splicing, via spliceosome / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / Pre-NOTCH Transcription and Translation / nuclear matrix / positive regulation of protein import into nucleus / calcium-dependent protein binding / transcription corepressor activity / cellular response to xenobiotic stimulus / cellular response to tumor necrosis factor / DNA-binding transcription activator activity, RNA polymerase II-specific / nuclear membrane / cellular response to lipopolysaccharide / transcription coactivator activity / nuclear body / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / cell cycle / mRNA binding / intracellular membrane-bounded organelle / DNA repair / GTPase activity / negative regulation of DNA-templated transcription / centrosome / chromatin / GTP binding / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / enzyme binding / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding
Similarity search - Function
Pre-mRNA-splicing factor 38, C-terminal / Pre-mRNA-splicing factor 38-associated hydrophilic C-term / Micro-fibrillar-associated protein 1, C-terminal / Microfibrillar-associated protein 1 / Ubiquitin-like modifier Hub1/Ubl5 / Microfibril-associated/Pre-mRNA processing / U4/U6.U5 small nuclear ribonucleoprotein component Snu23 / Pre-mRNA-splicing factor 38 / PRP38 family / Pre-mRNA-processing factor 17 ...Pre-mRNA-splicing factor 38, C-terminal / Pre-mRNA-splicing factor 38-associated hydrophilic C-term / Micro-fibrillar-associated protein 1, C-terminal / Microfibrillar-associated protein 1 / Ubiquitin-like modifier Hub1/Ubl5 / Microfibril-associated/Pre-mRNA processing / U4/U6.U5 small nuclear ribonucleoprotein component Snu23 / Pre-mRNA-splicing factor 38 / PRP38 family / Pre-mRNA-processing factor 17 / : / STL11, N-terminal / WD repeat Prp46/PLRG1-like / BUD31/G10-related, conserved site / : / : / G10 protein signature 1. / G10 protein signature 2. / SKI-interacting protein SKIP, SNW domain / SKI-interacting protein, SKIP / SKIP/SNW domain / Myb-like DNA-binding domain / Pre-mRNA-splicing factor Cwf15/Cwc15 / Cwf15/Cwc15 cell cycle control protein / Pre-mRNA-splicing factor Cwc2/Slt11 / G10 protein / Pre-mRNA-splicing factor BUD31 / Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminal / pre-mRNA splicing factor component / Zinc-finger double-stranded RNA-binding / Zinc finger, double-stranded RNA binding / Zinc finger, CCCH-type superfamily / Snu114, GTP-binding domain / 116kDa U5 small nuclear ribonucleoprotein component, N-terminal / 116kDa U5 small nuclear ribonucleoprotein component, C-terminal / 116 kDa U5 small nuclear ribonucleoprotein component N-terminus / zinc finger / Matrin/U1-C-like, C2H2-type zinc finger / U1-like zinc finger / Myb-type HTH DNA-binding domain profile. / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / Myb domain / Elongation Factor G, domain II / Elongation Factor G, domain III / JAB1/Mov34/MPN/PAD-1 ubiquitin protease / Translation elongation factor EFG/EF2, domain IV / Elongation factor G, domain IV / Elongation factor G, domain IV / Elongation factor G C-terminus / Elongation factor EFG, domain V-like / Elongation factor G C-terminus / EF-G domain III/V-like / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / PROCT domain / Prp8 RNase domain IV, fingers region / PROCT (NUC072) domain / PRO8NT domain / PROCN domain / Pre-mRNA-processing-splicing factor 8, U6-snRNA-binding / Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding / RNA recognition motif, spliceosomal PrP8 / PRP8 domain IV core / Pre-mRNA-processing-splicing factor 8, U5-snRNA-binding domain superfamily / Prp8 RNase domain IV, palm region / PRO8NT (NUC069), PrP8 N-terminal domain / PROCN (NUC071) domain / U6-snRNA interacting domain of PrP8 / U5-snRNA binding site 2 of PrP8 / RNA recognition motif of the spliceosomal PrP8 / PRP8 domain IV core / Pre-mRNA-processing-splicing factor 8 / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / JAB/MPN domain / JAB1/MPN/MOV34 metalloenzyme domain / MPN domain / MPN domain profile. / Zinc finger C2H2 superfamily / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Homeobox-like domain superfamily / Ubiquitin family / Ubiquitin-like domain / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / G-protein beta WD-40 repeat / Ubiquitin-like domain superfamily / WD40 repeat, conserved site / Ribonuclease H-like superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Ribosomal protein S5 domain 2-type fold
Similarity search - Domain/homology
Pleiotropic regulator 1 / Pre-mRNA-processing factor 17 / Protein BUD31 homolog / Microfibrillar-associated protein 1 / SNW domain-containing protein 1 / 116 kDa U5 small nuclear ribonucleoprotein component / Pre-mRNA-processing-splicing factor 8 / Pre-mRNA-splicing factor 38A / Zinc finger matrin-type protein 2 / Cell division cycle 5-like protein ...Pleiotropic regulator 1 / Pre-mRNA-processing factor 17 / Protein BUD31 homolog / Microfibrillar-associated protein 1 / SNW domain-containing protein 1 / 116 kDa U5 small nuclear ribonucleoprotein component / Pre-mRNA-processing-splicing factor 8 / Pre-mRNA-splicing factor 38A / Zinc finger matrin-type protein 2 / Cell division cycle 5-like protein / Ubiquitin-like protein 5 / Pre-mRNA-splicing factor RBM22 / Spliceosome-associated protein CWC15 homolog
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others) / Human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsTownsend C / Kastner B / Leelaram MN / Bertram K / Stark H / Luehrmann R
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG)860 Germany
CitationJournal: Science / Year: 2020
Title: Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation.
Authors: Cole Townsend / Majety N Leelaram / Dmitry E Agafonov / Olexandr Dybkov / Cindy L Will / Karl Bertram / Henning Urlaub / Berthold Kastner / Holger Stark / Reinhard Lührmann /
Abstract: Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway ...Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway of the latter and the mechanism whereby proteins aid its proper folding. Here, we report the cryo-electron microscopy structures of two human, activated spliceosome precursors (that is, pre-B complexes) at core resolutions of 3.9 and 4.2 angstroms. These structures elucidate the order of the numerous protein exchanges that occur during activation, the mutually exclusive interactions that ensure the correct order of ribonucleoprotein rearrangements needed to form the U2/U6 catalytic RNA, and the stepwise folding pathway of the latter. Structural comparisons with mature B complexes reveal the molecular mechanism whereby a conformational change in the scaffold protein PRP8 facilitates final three-dimensional folding of the U2/U6 catalytic RNA.
History
DepositionSep 4, 2020-
Header (metadata) releaseDec 9, 2020-
Map releaseDec 9, 2020-
UpdateDec 30, 2020-
Current statusDec 30, 2020Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.051
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.051
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7aav
  • Surface level: 0.035
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11693.png

Downloads & links

-
Map

FileDownload / File: emd_11693.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMasked/sharpened map of the pre-Bact-2 spliceosome core structure.
Voxel sizeX=Y=Z: 1.16 Å
Density
Contour LevelBy AUTHOR: 0.051 / Movie #1: 0.051
Minimum - Maximum-0.06758506 - 0.13364817
Average (Standard dev.)0.00027001693 (±0.0034261802)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 445.44 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.161.161.16
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z445.440445.440445.440
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ240240240
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-0.0680.1340.000

-
Supplemental data

-
Sample components

+
Entire : pre-Bact-2 spliceosomal core structure

EntireName: pre-Bact-2 spliceosomal core structure
Components
  • Complex: pre-Bact-2 spliceosomal core structure
    • Complex: pre-Bact-2 spliceosomal core structure
      • Protein or peptide: 116 kDa U5 small nuclear ribonucleoprotein component
      • Protein or peptide: Protein BUD31 homolog
      • Protein or peptide: Cell division cycle 5-like protein
      • Protein or peptide: Spliceosome-associated protein CWC15 homolog
      • Protein or peptide: Microfibrillar-associated protein 1
      • Protein or peptide: Pleiotropic regulator 1
      • Protein or peptide: Pre-mRNA-processing factor 17
      • Protein or peptide: Pre-mRNA-splicing factor 38A
      • Protein or peptide: Pre-mRNA-processing-splicing factor 8
      • Protein or peptide: Pre-mRNA-splicing factor RBM22
      • Protein or peptide: SNW domain-containing protein 1
      • Protein or peptide: Zinc finger matrin-type protein 2
      • RNA: U2 snRNAU2 spliceosomal RNA
      • RNA: U5 snRNAU5 spliceosomal RNA
      • RNA: U6 snRNAU6 spliceosomal RNA
      • Protein or peptide: Ubiquitin-like protein 5
    • Complex: MINX M3 pre-mRNA
      • RNA: MINX M3 pre-mRNA
  • Ligand: GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate
  • Ligand: MAGNESIUM ION
  • Ligand: D-chiro inositol hexakisphosphate

+
Supramolecule #1: pre-Bact-2 spliceosomal core structure

SupramoleculeName: pre-Bact-2 spliceosomal core structure / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17

+
Supramolecule #2: pre-Bact-2 spliceosomal core structure

SupramoleculeName: pre-Bact-2 spliceosomal core structure / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#6, #8-#17
Source (natural)Organism: Homo sapiens (human)

+
Supramolecule #3: MINX M3 pre-mRNA

SupramoleculeName: MINX M3 pre-mRNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #7
Source (natural)Organism: synthetic construct (others)

+
Macromolecule #1: 116 kDa U5 small nuclear ribonucleoprotein component

MacromoleculeName: 116 kDa U5 small nuclear ribonucleoprotein component / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 109.560625 KDa
SequenceString: MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPL TEPIIKPVKT KKFTLMEQTL PVTVYEMDFL ADLMDNSELI RNVTLCGHLH HGKTCFVDCL IEQTHPEIRK R YDQDLCYT ...String:
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDVGDHDD DHPGMEVVLH EDKKYYPTAE EVYGPEVETI VQEEDTQPL TEPIIKPVKT KKFTLMEQTL PVTVYEMDFL ADLMDNSELI RNVTLCGHLH HGKTCFVDCL IEQTHPEIRK R YDQDLCYT DILFTEQERG VGIKSTPVTV VLPDTKGKSY LFNIMDTPGH VNFSDEVTAG LRISDGVVLF IDAAEGVMLN TE RLIKHAV QERLAVTVCI NKIDRLILEL KLPPTDAYYK LRHIVDEVNG LISMYSTDEN LILSPLLGNV CFSSSQYSIC FTL GSFAKI YADTFGDINY QEFAKRLWGD IYFNPKTRKF TKKAPTSSSQ RSFVEFILEP LYKILAQVVG DVDTSLPRTL DELG IHLTK EELKLNIRPL LRLVCKKFFG EFTGFVDMCV QHIPSPKVGA KPKIEHTYTG GVDSDLGEAM SDCDPDGPLM CHTTK MYST DDGVQFHAFG RVLSGTIHAG QPVKVLGENY TLEDEEDSQI CTVGRLWISV ARYHIEVNRV PAGNWVLIEG VDQPIV KTA TITEPRGNEE AQIFRPLKFN TTSVIKIAVE PVNPSELPKM LDGLRKVNKS YPSLTTKVEE SGEHVILGTG ELYLDCV MH DLRKMYSEID IKVADPVVTF CETVVETSSL KCFAETPNKK NKITMIAEPL EKGLAEDIEN EVVQITWNRK KLGEFFQT K YDWDLLAARS IWAFGPDATG PNILVDDTLP SEVDKALLGS VKDSIVQGFQ WGTREGPLCD ELIRNVKFKI LDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRT HTQGQAFSLS VFHHWQIVPG DPLDKSIVIR PLEPQPAPHL AREFMIKTRR RKGLSEDVSI SKFFDDPMLL E LAKQDVVL NYPM

+
Macromolecule #2: Protein BUD31 homolog

MacromoleculeName: Protein BUD31 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 17.03285 KDa
SequenceString:
MPKVKRSRKA PPDGWELIEP TLDELDQKMR EAETEPHEGK RKVESLWPIF RIHHQKTRYI FDLFYKRKAI SRELYEYCIK EGYADKNLI AKWKKQGYEN LCCLRCIQTR DTNFGTNCIC RVPKSKLEVG RIIECTHCGC RGCSG

+
Macromolecule #3: Cell division cycle 5-like protein

MacromoleculeName: Cell division cycle 5-like protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 92.406883 KDa
SequenceString: MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK TEWSREEEEK LLHLAKLMPT QWRTIAPII GRTAAQCLEH YEFLLDKAAQ RDNEEETTDD PRKLKPGEID PNPETKPARP DPIDMDEDEL EMLSEARARL A NTQGKKAK ...String:
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK TEWSREEEEK LLHLAKLMPT QWRTIAPII GRTAAQCLEH YEFLLDKAAQ RDNEEETTDD PRKLKPGEID PNPETKPARP DPIDMDEDEL EMLSEARARL A NTQGKKAK RKAREKQLEE ARRLAALQKR RELRAAGIEI QKKRKRKRGV DYNAEIPFEK KPALGFYDTS EENYQALDAD FR KLRQQDL DGELRSEKEG RDRKKDKQHL KRKKESDLPS AILQTSGVSE FTKKRSKLVL PAPQISDAEL QEVVKVGQAS EIA RQTAEE SGITNSASST LLSEYNVTNN SVALRTPRTP ASQDRILQEA QNLMALTNVD TPLKGGLNTP LHESDFSGVT PQRQ VVQTP NTVLSTPFRT PSNGAEGLTP RSGTTPKPVI NSTPGRTPLR DKLNINPEDG MADYSDPSYV KQMERESREH LRLGL LGLP APKNDFEIVL PENAEKELEE REIDDTYIED AADVDARKQA IRDAERVKEM KRMHKAVQKD LPRPSEVNET ILRPLN VEP PLTDLQKSEE LIKKEMITML HYDLLHHPYE PSGNKKGKTV GFGTNNSEHI TYLEHNPYEK FSKEELKKAQ DVLVQEM EV VKQGMSHGEL SSEAYNQVWE ECYSQVLYLP GQSRYTRANL ASKKDRIESL EKRLEINRGH MTTEAKRAAK MEKKMKIL L GGYQSRAMGL MKQLNDLWDQ IEQAHLELRT FEELKKHEDS AIPRRLECLK EDVQRQQERE KELQHRYADL LLEKETLKS KF

+
Macromolecule #4: Spliceosome-associated protein CWC15 homolog

MacromoleculeName: Spliceosome-associated protein CWC15 homolog / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 26.674447 KDa
SequenceString: MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA PEEVRNRDFR RELEERERAA AREKNRDRPT REHTTSSSV SKKPRLDQIP AANLDADDPL TDEEDEDFEE ESDDDDTAAL LAELEKIKKE RAEEQARKEQ EQKAEEERIR M ENILSGNP ...String:
MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA PEEVRNRDFR RELEERERAA AREKNRDRPT REHTTSSSV SKKPRLDQIP AANLDADDPL TDEEDEDFEE ESDDDDTAAL LAELEKIKKE RAEEQARKEQ EQKAEEERIR M ENILSGNP LLNLTGPSQP QANFKVKRRW DDDVVFKNCA KGVDDQKKDK RFVNDTLRSE FHKKFMEKYI K

+
Macromolecule #5: Microfibrillar-associated protein 1

MacromoleculeName: Microfibrillar-associated protein 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 52.050527 KDa
SequenceString: MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF QFIKKAKEQE AEPEEQEEDS SSDPRLRRL QNRISEDVEE RLARHRKIVE PEVVGESDSE VEGDAWRMER EDSSEEEEEE IDDEEIERRR GMMRQRAQER K NEEMEVME ...String:
MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF QFIKKAKEQE AEPEEQEEDS SSDPRLRRL QNRISEDVEE RLARHRKIVE PEVVGESDSE VEGDAWRMER EDSSEEEEEE IDDEEIERRR GMMRQRAQER K NEEMEVME VEDEGRSGEE SESESEYEEY TDSEDEMEPR LKPVFIRKKD RVTVQEREAE ALKQKELEQE AKRMAEERRK YT LKIVEEE TKKELEENKR SLAALDALNT DDENDEEEYE AWKVRELKRI KRDREDREAL EKEKAEIERM RNLTEEERRA ELR ANGKVI TNKAVKGKYK FLQKYYHRGA FFMDEDEEVY KRDFSAPTLE DHFNKTILPK VMQVKNFGRS GRTKYTHLVD QDTT SFDSA WGQESAQNTK FFKQKAAGVR DVFERPSAKK RKTT

+
Macromolecule #6: Pleiotropic regulator 1

MacromoleculeName: Pleiotropic regulator 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 57.280758 KDa
SequenceString: MVEEVQKHSV HTLVFRSLKR THDMFVADNG KPVPLDEESH KRKMAIKLRN EYGPVLHMPT SKENLKEKGP QNATDSYVHK QYPANQGQE VEYFVAGTHP YPPGPGVALT ADTKIQRMPS ESAAQSLAVA LPLQTKADAN RTAPSGSEYR HPGASDRPQP T AMNSIVME ...String:
MVEEVQKHSV HTLVFRSLKR THDMFVADNG KPVPLDEESH KRKMAIKLRN EYGPVLHMPT SKENLKEKGP QNATDSYVHK QYPANQGQE VEYFVAGTHP YPPGPGVALT ADTKIQRMPS ESAAQSLAVA LPLQTKADAN RTAPSGSEYR HPGASDRPQP T AMNSIVME TGNTKNSALM AKKAPTMPKP QWHPPWKLYR VISGHLGWVR CIAVEPGNQW FVTGSADRTI KIWDLASGKL KL SLTGHIS TVRGVIVSTR SPYLFSCGED KQVKCWDLEY NKVIRHYHGH LSAVYGLDLH PTIDVLVTCS RDSTARIWDV RTK ASVHTL SGHTNAVATV RCQAAEPQII TGSHDTTIRL WDLVAGKTRV TLTNHKKSVR AVVLHPRHYT FASGSPDNIK QWKF PDGSF IQNLSGHNAI INTLTVNSDG VLVSGADNGT MHLWDWRTGY NFQRVHAAVQ PGSLDSESGI FACAFDQSES RLLTA EADK TIKVYREDDT ATEETHPVSW KPEIIKRKRF

+
Macromolecule #8: Pre-mRNA-processing factor 17

MacromoleculeName: Pre-mRNA-processing factor 17 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 65.61218 KDa
SequenceString: MSAAIAALAA SYGSGSGSES DSDSESSRCP LPAADSLMHL TKSPSSKPSL AVAVDSAPEV AVKEDLETGV HLDPAVKEVQ YNPTYETMF APEFGPENPF RTQQMAAPRN MLSGYAEPAH INDFMFEQQR RTFATYGYAL DPSLDNHQVS AKYIGSVEEA E KNQGLTVF ...String:
MSAAIAALAA SYGSGSGSES DSDSESSRCP LPAADSLMHL TKSPSSKPSL AVAVDSAPEV AVKEDLETGV HLDPAVKEVQ YNPTYETMF APEFGPENPF RTQQMAAPRN MLSGYAEPAH INDFMFEQQR RTFATYGYAL DPSLDNHQVS AKYIGSVEEA E KNQGLTVF ETGQKKTEKR KKFKENDASN IDGFLGPWAK YVDEKDVAKP SEEEQKELDE ITAKRQKKGK QEEEKPGEEK TI LHVKEMY DYQGRSYLHI PQDVGVNLRS TMPPEKCYLP KKQIHVWSGH TKGVSAVRLF PLSGHLLLSC SMDCKIKLWE VYG ERRCLR TFIGHSKAVR DICFNTAGTQ FLSAAYDRYL KLWDTETGQC ISRFTNRKVP YCVKFNPDED KQNLFVAGMS DKKI VQWDI RSGEIVQEYD RHLGAVNTIV FVDENRRFVS TSDDKSLRVW EWDIPVDFKY IAEPSMHSMP AVTLSPNGKW LACQS MDNQ ILIFGAQNRF RLNKKKIFKG HMVAGYACQV DFSPDMSYVI SGDGNGKLNI WDWKTTKLYS RFKAHDKVCI GAVWHP HET SKVITCGWDG LIKLWD

+
Macromolecule #9: Pre-mRNA-splicing factor 38A

MacromoleculeName: Pre-mRNA-splicing factor 38A / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 37.563863 KDa
SequenceString: MANRTVKDAH SIHGTNPQYL VEKIIRTRIY ESKYWKEECF GLTAELVVDK AMELRFVGGV YGGNIKPTPF LCLTLKMLQI QPEKDIIVE FIKNEDFKYV RMLGALYMRL TGTAIDCYKY LEPLYNDYRK IKSQNRNGEF ELMHVDEFID ELLHSERVCD I ILPRLQKR ...String:
MANRTVKDAH SIHGTNPQYL VEKIIRTRIY ESKYWKEECF GLTAELVVDK AMELRFVGGV YGGNIKPTPF LCLTLKMLQI QPEKDIIVE FIKNEDFKYV RMLGALYMRL TGTAIDCYKY LEPLYNDYRK IKSQNRNGEF ELMHVDEFID ELLHSERVCD I ILPRLQKR YVLEEAEQLE PRVSALEEDM DDVESSEEEE EEDEKLERVP SPDHRRRSYR DLDKPRRSPT LRYRRSRSRS PR RRSRSPK RRSPSPRRER HRSKSPRRHR SRSRDRRHRS RSKSPGHHRS HRHRSHSKSP ERSKKSHKKS RRGNE

+
Macromolecule #10: Pre-mRNA-processing-splicing factor 8

MacromoleculeName: Pre-mRNA-processing-splicing factor 8 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 273.97425 KDa
SequenceString: MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYL GALKYMPHAV LKLLENMPMP WEQIRDVPVL YHITGAISFV NEIPWVIEPV YISQWGSMWI MMRREKRDRR H FKRMRFPP ...String:
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED MPPEHVRKII RDHGDMTNRK FRHDKRVYL GALKYMPHAV LKLLENMPMP WEQIRDVPVL YHITGAISFV NEIPWVIEPV YISQWGSMWI MMRREKRDRR H FKRMRFPP FDDEEPPLDY ADNILDVEPL EAIQLELDPE EDAPVLDWFY DHQPLRDSRK YVNGSTYQRW QFTLPMMSTL YR LANQLLT DLVDDNYFYL FDLKAFFTSK ALNMAIPGGP KFEPLVRDIN LQDEDWNEFN DINKIIIRQP IRTEYKIAFP YLY NNLPHH VHLTWYHTPN VVFIKTEDPD LPAFYFDPLI NPISHRHSVK SQEPLPDDDE EFELPEFVEP FLKDTPLYTD NTAN GIALL WAPRPFNLRS GRTRRALDIP LVKNWYREHC PAGQPVKVRV SYQKLLKYYV LNALKHRPPK AQKKRYLFRS FKATK FFQS TKLDWVEVGL QVCRQGYNML NLLIHRKNLN YLHLDYNFNL KPVKTLTTKE RKKSRFGNAF HLCREVLRLT KLVVDS HVQ YRLGNVDAFQ LADGLQYIFA HVGQLTGMYR YKYKLMRQIR MCKDLKHLIY YRFNTGPVGK GPGCGFWAAG WRVWLFF MR GITPLLERWL GNLLARQFEG RHSKGVAKTV TKQRVESHFD LELRAAVMHD ILDMMPEGIK QNKARTILQH LSEAWRCW K ANIPWKVPGL PTPIENMILR YVKAKADWWT NTAHYNRERI RRGATVDKTV CKKNLGRLTR LYLKAEQERQ HNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQR AFKEVGIEFM DLYSHLVPVY DVEPLEKITD AYLDQYLWYE ADKRRLFPPW IKPADTEPPP LLVYKWCQGI N NLQDVWET SEGECNVMLE SRFEKMYEKI DLTLLNRLLR LIVDHNIADY MTAKNNVVIN YKDMNHTNSY GIIRGLQFAS FI VQYYGLV MDLLVLGLHR ASEMAGPPQM PNDFLSFQDI ATEAAHPIRL FCRYIDRIHI FFRFTADEAR DLIQRYLTEH PDP NNENIV GYNNKKCWPR DARMRLMKHD VNLGRAVFWD IKNRLPRSVT TVQWENSFVS VYSKDNPNLL FNMCGFECRI LPKC RTSYE EFTHKDGVWN LQNEVTKERT AQCFLRVDDE SMQRFHNRVR QILMASGSTT FTKIVNKWNT ALIGLMTYFR EAVVN TQEL LDLLVKCENK IQTRIKIGLN SKMPSRFPPV VFYTPKELGG LGMLSMGHVL IPQSDLRWSK QTDVGITHFR SGMSHE EDQ LIPNLYRYIQ PWESEFIDSQ RVWAEYALKR QEAIAQNRRL TLEDLEDSWD RGIPRINTLF QKDRHTLAYD KGWRVRT DF KQYQVLKQNP FWWTHQRHDG KLWNLNNYRT DMIQALGGVE GILEHTLFKG TYFPTWEGLF WEKASGFEES MKWKKLTN A QRSGLNQIPN RRFTLWWSPT INRANVYVGF QVQLDLTGIF MHGKIPTLKI SLIQIFRAHL WQKIHESIVM DLCQVFDQE LDALEIETVQ KETIHPRKSY KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA RAKFLDYTT DNMSIYPSPT GVLIAIDLAY NLHSAYGNWF PGSKPLIQQA MAKIMKANPA LYVLRERIRK GLQLYSSEPT E PYLSSQNY GELFSNQIIW FVDDTNVYRV TIHKTFEGNL TTKPINGAIF IFNPRTGQLF LKIIHTSVWA GQKRLGQLAK WK TAEEVAA LIRSLPVEEQ PKQIIVTRKG MLDPLEVHLL DFPNIVIKGS ELQLPFQACL KVEKFGDLIL KATEPQMVLF NLY DDWLKT ISSYTAFSRL ILILRALHVN NDRAKVILKP DKTTITEPHH IWPTLTDEEW IKVEVQLKDL ILADYGKKNN VNVA SLTQS EIRDIILGME ISAPSQQRQQ IAEIEKQTKE QSQLTATQTR TVNKHGDEII TSTTSNYETQ TFSSKTEWRV RAISA ANLH LRTNHIYVSS DDIKETGYTY ILPKNVLKKF ICISDLRAQI AGYLYGVSPP DNPQVKEIRC IVMVPQWGTH QTVHLP GQL PQHEYLKEME PLGWIHTQPN ESPQLSPQDV TTHAKIMADN PSWDGEKTII ITCSFTPGSC TLTAYKLTPS GYEWGRQ NT DKGNNPKGYL PSHYERVQML LSDRFLGFFM VPAQSSWNYN FMGVRHDPNM KYELQLANPK EFYHEVHRPS HFLNFALL Q EGEVYSADRE DLYA

+
Macromolecule #11: Pre-mRNA-splicing factor RBM22

MacromoleculeName: Pre-mRNA-splicing factor RBM22 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 46.959555 KDa
SequenceString: MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLE YGLPIQVRDA GLSFKDDMPK SDVNKEYYTQ NMEREISNSD GTRPVGMLGK ATSTSDMLLK LARTTPYYKR N RPHICSFW ...String:
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG VRMRFKKTEV CQTCSKLKNV CQTCLLDLE YGLPIQVRDA GLSFKDDMPK SDVNKEYYTQ NMEREISNSD GTRPVGMLGK ATSTSDMLLK LARTTPYYKR N RPHICSFW VKGECKRGEE CPYRHEKPTD PDDPLADQNI KDRYYGINDP VADKLLKRAS TMPRLDPPED KTITTLYVGG LG DTITETD LRNHFYQFGE IRTITVVQRQ QCAFIQFATR QAAEVAAEKS FNKLIVNGRR LNVKWGRSQA ARGKEKEKDG TTD SGIKLE PVPGLPGALP PPPAAEEEAS ANYFNLPPSG PPAVVNIALP PPPGIAPPPP PGFGPHMFHP MGPPPPFMRA PGPI HYPSQ DPQRMGAHAG KHSSP

+
Macromolecule #12: SNW domain-containing protein 1

MacromoleculeName: SNW domain-containing protein 1 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 61.610703 KDa
SequenceString: MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQ VDSEGKIKYD AIARQGQSKD KVIYSKYTDL VPKEVMNADD PDLQRPDEEA IKEITEKTRV ALEKSVSQKV A AAMPVRAA ...String:
MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQ VDSEGKIKYD AIARQGQSKD KVIYSKYTDL VPKEVMNADD PDLQRPDEEA IKEITEKTRV ALEKSVSQKV A AAMPVRAA DKLAPAQYIR YTPSQQGVAF NSGAKQRVIR MVEMQKDPME PPRFKINKKI PRGPPSPPAP VMHSPSRKMT VK EQQEWKI PPCISNWKNA KGYTIPLDKR LAADGRGLQT VHINENFAKL AEALYIADRK AREAVEMRAQ VERKMAQKEK EKH EEKLRE MAQKARERRA GIKTHVEKED GEARERDEIR HDRRKERQHD RNLSRAAPDK RSKLQRNENR DISEVIALGV PNPR TSNEV QYDQRLFNQS KGMDSGFAGG EDEIYNVYDQ AWRGGKDMAQ SIYRPSKNLD KDMYGDDLEA RIKTNRFVPD KEFSG SDRR QRGREGPVQF EEDPFGLDKF LEEAKQHGGS KRPSDSSRPK EHEHEGKKRR KE

+
Macromolecule #13: Zinc finger matrin-type protein 2

MacromoleculeName: Zinc finger matrin-type protein 2 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 23.664047 KDa
SequenceString: MASGSGTKNL DFRRKWDKDE YEKLAEKRLT EEREKKDGKP VQPVKRELLR HRDYKVDLES KLGKTIVITK TTPQSEMGGY YCNVCDCVV KDSINFLDHI NGKKHQRNLG MSMRVERSTL DQVKKRFEVN KKKMEEKQKD YDFEERMKEL REEEEKAKAY K KEKQKEKK ...String:
MASGSGTKNL DFRRKWDKDE YEKLAEKRLT EEREKKDGKP VQPVKRELLR HRDYKVDLES KLGKTIVITK TTPQSEMGGY YCNVCDCVV KDSINFLDHI NGKKHQRNLG MSMRVERSTL DQVKKRFEVN KKKMEEKQKD YDFEERMKEL REEEEKAKAY K KEKQKEKK RRAEEDLTFE EDDEMAAVMG FSGFGSTKKS Y

+
Macromolecule #17: Ubiquitin-like protein 5

MacromoleculeName: Ubiquitin-like protein 5 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 8.560945 KDa
SequenceString:
MIEVVCNDRL GKKVRVKCNT DDTIGDLKKL IAAQTGTRWN KIVLKKWYTI FKDHVSLGDY EIHDGMNLEL YYQ

+
Macromolecule #7: MINX M3 pre-mRNA

MacromoleculeName: MINX M3 pre-mRNA / type: rna / ID: 7 / Number of copies: 1
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 73.712359 KDa
SequenceString: GGGAGACGGA AUUCGAGCUC GCCCACUCUU GGAUCGGAAA CCCGUCGGCC UCCGAACGGU AAGAGCCUAG CAUGUAGAAC UGGUUACCU GCAGCCCAAG CUUGCUGCAC GUCUAGGGCG CAGUAGUCCA GGGUUUCCUU GAUGAUGUCA UACUUAUCCU G UCCCUUUU ...String:
GGGAGACGGA AUUCGAGCUC GCCCACUCUU GGAUCGGAAA CCCGUCGGCC UCCGAACGGU AAGAGCCUAG CAUGUAGAAC UGGUUACCU GCAGCCCAAG CUUGCUGCAC GUCUAGGGCG CAGUAGUCCA GGGUUUCCUU GAUGAUGUCA UACUUAUCCU G UCCCUUUU UUUUCCACAG CUCGCGGUUG AGGACAAACU CUUCGCGGUC UUUCCAGUGG GGAUCCAAUA UC

+
Macromolecule #14: U2 snRNA

MacromoleculeName: U2 snRNA / type: rna / ID: 14 / Number of copies: 1
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 60.186445 KDa
SequenceString:
AUCGCUUCUC GGCCUUUUGG CUAAGAUCAA GUGUAGUAUC UGUUCUUAUC AGUUUAAUAU CUGAUACGUC CUCUAUCCGA GGACAAUAU AUUAAAUGGA UUUUUGGAGC AGGGAGAUGG AAUAGGAGCU UGCUCCGUCC ACUCCACGCA UCGACCUGGU A UUGCAGUA CCUCCAGGAA CGGUGCACCC

+
Macromolecule #15: U5 snRNA

MacromoleculeName: U5 snRNA / type: rna / ID: 15 / Number of copies: 1
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 36.908668 KDa
SequenceString:
AUACUCUGGU UUCUCUUCAG AUCGCAUAAA UCUUUCGCCU UUUACUAAAG AUUUCCGUGG AGAGGAACAA CUCUGAGUCU UAACCCAAU UUUUUGAGCC UUGCCUUGGC AAGGCUA

+
Macromolecule #16: U6 snRNA

MacromoleculeName: U6 snRNA / type: rna / ID: 16 / Number of copies: 1
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 34.09827 KDa
SequenceString:
GUGCUCGCUU CGGCAGCACA UAUACUAAAA UUGGAACGAU ACAGAGAAGA UUAGCAUGGC CCCUGCGCAA GGAUGACACG CAAAUUCGU GAAGCGUUCC AUAUUUU

+
Macromolecule #18: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 18 / Number of copies: 1 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

+
Macromolecule #19: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 19 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #20: D-chiro inositol hexakisphosphate

MacromoleculeName: D-chiro inositol hexakisphosphate / type: ligand / ID: 20 / Number of copies: 1 / Formula: KGN
Molecular weightTheoretical: 660.035 Da
Chemical component information

ChemComp-KGN:
D-chiro inositol hexakisphosphate

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.9
GridModel: Quantifoil R3.5/1 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Average exposure time: 1.0 sec. / Average electron dose: 2.25 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: OTHER / Details: cryoSPARC ab initio reconstruction
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 39336

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7aav:
Human pre-Bact-2 spliceosome core structure

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more