[English] 日本語
Yorodumi
- PDB-5an9: Mechanism of eIF6 release from the nascent 60S ribosomal subunit -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5an9
TitleMechanism of eIF6 release from the nascent 60S ribosomal subunit
Components
  • (60S RIBOSOMAL PROTEIN ...) x 6
  • 26S RIBOSOMAL RNA
  • 60S ACIDIC RIBOSOMAL PROTEIN P0
  • EUKARYOTIC TRANSLATION INITIATION FACTOR 6
  • RIBOSOME MATURATION PROTEIN SBDS
  • UBIQUITIN-60S RIBOSOMAL PROTEIN L40
KeywordsTRANSLATION / RIBOSOMOPATHY / EFL1 / GTPASE / RIBOSOME BIOGENESIS
Function / homology
Function and homology information


L13a-mediated translational silencing of Ceruloplasmin expression / APC/C:Cdc20 mediated degradation of Cyclin B / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / APC-Cdc20 mediated degradation of Nek2A / SRP-dependent cotranslational protein targeting to membrane / Separation of Sister Chromatids / Senescence-Associated Secretory Phenotype (SASP) ...L13a-mediated translational silencing of Ceruloplasmin expression / APC/C:Cdc20 mediated degradation of Cyclin B / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / APC-Cdc20 mediated degradation of Nek2A / SRP-dependent cotranslational protein targeting to membrane / Separation of Sister Chromatids / Senescence-Associated Secretory Phenotype (SASP) / Autodegradation of the E3 ubiquitin ligase COP1 / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Hedgehog ligand biogenesis / Negative regulation of MAPK pathway / Regulation of necroptotic cell death / MAPK6/MAPK4 signaling / UCH proteinases / Josephin domain DUBs / Ub-specific processing proteases / Metalloprotease DUBs / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Major pathway of rRNA processing in the nucleolus and cytosol / CDK-mediated phosphorylation and removal of Cdc6 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Formation of a pool of free 40S subunits / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / GTP hydrolysis and joining of the 60S ribosomal subunit / : / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E3 ubiquitin ligases ubiquitinate target proteins / Regulation of PTEN localization / Regulation of PTEN stability and activity / ER Quality Control Compartment (ERQC) / Interleukin-1 signaling / Peroxisomal protein import / Endosomal Sorting Complex Required For Transport (ESCRT) / Negative regulators of DDX58/IFIH1 signaling / : / : / Aggrephagy / Pexophagy / : / KEAP1-NFE2L2 pathway / Regulation of NF-kappa B signaling / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / : / Orc1 removal from chromatin / Cyclin D associated events in G1 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Neddylation / Iron uptake and transport / Antigen processing: Ubiquitination & Proteasome degradation / leukocyte chemotaxis / bone marrow development / inner cell mass cell proliferation / maturation of 5.8S rRNA / ribosomal subunit export from nucleus / bone mineralization / ribosomal large subunit binding / preribosome, large subunit precursor / hematopoietic progenitor cell differentiation / phagocytic vesicle / maturation of LSU-rRNA / ribosomal large subunit biogenesis / extracellular matrix / translation initiation factor activity / lipid droplet / assembly of large subunit precursor of preribosome / mitotic spindle organization / cytosolic ribosome assembly / modification-dependent protein catabolic process / protein tag activity / rRNA processing / spindle pole / large ribosomal subunit rRNA binding / ribosome binding / ribosome biogenesis / large ribosomal subunit / cytoplasmic translation / cytosolic large ribosomal subunit / microtubule binding / protein ubiquitination / rRNA binding / structural constituent of ribosome / translation / mRNA binding / ubiquitin protein ligase binding / nucleolus / RNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
Wheat Germ Agglutinin (Isolectin 2); domain 1 - #300 / ZNF265 like - #50 / ZNF265 like / Ribosome maturation protein SDO1/SBDS, C-terminal domain / SBDS protein, C-terminal domain / Ribosome maturation protein Sdo1/SBDS / Ribosome maturation protein SBDS, conserved site / Ribosome maturation protein SDO1/SBDS, central domain / Ribosome maturation protein Sdo1/SBDS, central domain superfamily / SBDS protein, domain II ...Wheat Germ Agglutinin (Isolectin 2); domain 1 - #300 / ZNF265 like - #50 / ZNF265 like / Ribosome maturation protein SDO1/SBDS, C-terminal domain / SBDS protein, C-terminal domain / Ribosome maturation protein Sdo1/SBDS / Ribosome maturation protein SBDS, conserved site / Ribosome maturation protein SDO1/SBDS, central domain / Ribosome maturation protein Sdo1/SBDS, central domain superfamily / SBDS protein, domain II / Uncharacterized protein family UPF0023 signature. / Ribosome maturation protein SDO1/SBDS, N-terminal / Ribosome maturation protein SBDS, N-terminal domain superfamily / Ribosome maturation protein Sdo1/SBDS-like / Shwachman-Bodian-Diamond syndrome (SBDS) protein / Ribosomal protein L24 / Ribosomal protein L3; domain 3 / Ribosomal protein L3, domain 3 / Ribosomal Protein L3; Chain: B; domain 2, / Ribosomal Protein L3; Chain: B; domain 2, - #10 / Ribosomal Protein L24e; Chain: T; / Ribosomal protein L6 / L-arginine/glycine Amidinotransferase; Chain A / 5-stranded Propeller / L-arginine/glycine Amidinotransferase; Chain A / Ribosomal protein L16/L10 / Ribosomal Protein L14 / Ribosomal protein L14/L23 / Outer Surface Protein A; domain 3 / 60s Acidic ribosomal protein / 60S acidic ribosomal protein P0 / Aldehyde Oxidoreductase; domain 3 / Wheat Germ Agglutinin (Isolectin 2); domain 1 / Translation initiation factor IF6 / eIF-6 family / translation initiation factor 6 / 50S ribosomal protein L10, insertion domain superfamily / Translation factors / 60S ribosomal protein L10P, insertion domain / Insertion domain in 60S ribosomal protein L10P / Ribosomal protein L10e, conserved site / Ribosomal protein L10e / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Ribosomal protein L10e signature. / Ribosomal protein L24e, conserved site / Ribosomal protein L24e signature. / Ribosomal protein L3, domain 3, archaeal type superfamily / Ribosomal protein L3, archaeal/eukaryotic type / Ribosomal protein L6, conserved site-2 / Ribosomal protein L6 signature 2. / Ribosomal protein L24e-related / Ribosomal protein L24e/L24 superfamily / Ribosomal protein L24e / Elongation Factor Tu (Ef-tu); domain 3 / Ribosomal protein L10-like domain superfamily / Ribosomal protein L10P / Ribosomal protein L10 / Ribosomal protein L11, N-terminal / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11/L12 / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11, RNA binding domain / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / : / Few Secondary Structures / Irregular / Ubiquitin family / Ribosomal protein L10e/L16 / Ribosomal protein L10e/L16 superfamily / Ubiquitin homologues / Ribosomal protein L16p/L10e / Ribosomal protein L6, alpha-beta domain / Ribosomal protein L6 / Ribosomal protein L6, alpha-beta domain superfamily / Ribosomal protein L6 / Ubiquitin-like domain / Ubiquitin domain profile. / Ribosomal protein L14p/L23e / Ribosomal protein L14P / Ribosomal protein L14 superfamily / Ribosomal protein L3, conserved site / Ribosomal protein L14p/L23e / Ribosomal protein L3 / Ribosomal protein L3 / Ribosomal protein L3 signature. / Zinc-binding ribosomal protein / Translation protein, beta-barrel domain superfamily / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Beta Barrel / 2-Layer Sandwich
Similarity search - Domain/homology
: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Ubiquitin-ribosomal protein eL40 fusion protein / Large ribosomal subunit protein uL10 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL11 ...: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Ubiquitin-ribosomal protein eL40 fusion protein / Large ribosomal subunit protein uL10 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL11 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein eL24 / Large ribosomal subunit protein uL6 / Eukaryotic translation initiation factor 6 / Ribosome maturation protein SBDS
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
DICTYOSTELIUM DISCOIDEUM (eukaryote)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsWeis, F. / Giudice, E. / Churcher, M. / Jin, L. / Hilcenko, C. / Wong, C.C. / Traynor, D. / Kay, R.R. / Warren, A.J.
CitationJournal: Nat Struct Mol Biol / Year: 2015
Title: Mechanism of eIF6 release from the nascent 60S ribosomal subunit.
Authors: Félix Weis / Emmanuel Giudice / Mark Churcher / Li Jin / Christine Hilcenko / Chi C Wong / David Traynor / Robert R Kay / Alan J Warren /
Abstract: SBDS protein (deficient in the inherited leukemia-predisposition disorder Shwachman-Diamond syndrome) and the GTPase EFL1 (an EF-G homolog) activate nascent 60S ribosomal subunits for translation by ...SBDS protein (deficient in the inherited leukemia-predisposition disorder Shwachman-Diamond syndrome) and the GTPase EFL1 (an EF-G homolog) activate nascent 60S ribosomal subunits for translation by catalyzing eviction of the antiassociation factor eIF6 from nascent 60S ribosomal subunits. However, the mechanism is completely unknown. Here, we present cryo-EM structures of human SBDS and SBDS-EFL1 bound to Dictyostelium discoideum 60S ribosomal subunits with and without endogenous eIF6. SBDS assesses the integrity of the peptidyl (P) site, bridging uL16 (mutated in T-cell acute lymphoblastic leukemia) with uL11 at the P-stalk base and the sarcin-ricin loop. Upon EFL1 binding, SBDS is repositioned around helix 69, thus facilitating a conformational switch in EFL1 that displaces eIF6 by competing for an overlapping binding site on the 60S ribosomal subunit. Our data reveal the conserved mechanism of eIF6 release, which is corrupted in both inherited and sporadic leukemias.
History
DepositionSep 6, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 21, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 28, 2015Group: Database references
Revision 1.2Dec 2, 2015Group: Database references
Revision 1.3Apr 19, 2017Group: Other
Revision 2.0Aug 2, 2017Group: Atomic model / Data collection / Derived calculations
Category: atom_site / em_image_scans ...atom_site / em_image_scans / em_software / struct_conn
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _em_software.fitting_id / _em_software.image_processing_id / _em_software.name
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

-
Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
  • Download
  • Simplified surface model + fitted atomic model
  • EMDB-3145
  • Imaged by Jmol
  • Download
  • Superimposition on EM map
  • EMDB-3145
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 60S RIBOSOMAL PROTEIN L3
B: 60S RIBOSOMAL PROTEIN L9
C: 60S ACIDIC RIBOSOMAL PROTEIN P0
D: 60S RIBOSOMAL PROTEIN L12
E: 60S RIBOSOMAL PROTEIN L23
F: 60S RIBOSOMAL PROTEIN L10
G: 60S RIBOSOMAL PROTEIN L24
H: UBIQUITIN-60S RIBOSOMAL PROTEIN L40
I: EUKARYOTIC TRANSLATION INITIATION FACTOR 6
J: RIBOSOME MATURATION PROTEIN SBDS
N: 26S RIBOSOMAL RNA


Theoretical massNumber of molelcules
Total (without water)1,419,23811
Polymers1,419,23811
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA

-
Components

-
60S RIBOSOMAL PROTEIN ... , 6 types, 6 molecules ABDEFG

#1: Protein 60S RIBOSOMAL PROTEIN L3 /


Mass: 45158.758 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: P34113
#2: Protein 60S RIBOSOMAL PROTEIN L9 /


Mass: 21250.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q54XI5
#4: Protein 60S RIBOSOMAL PROTEIN L12 /


Mass: 17811.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q54J50
#5: Protein 60S RIBOSOMAL PROTEIN L23 /


Mass: 14567.147 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q54G86
#6: Protein 60S RIBOSOMAL PROTEIN L10 /


Mass: 24591.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q54J69
#7: Protein 60S RIBOSOMAL PROTEIN L24 /


Mass: 8334.771 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-69 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q54VN6

-
Protein , 4 types, 4 molecules CHIJ

#3: Protein 60S ACIDIC RIBOSOMAL PROTEIN P0


Mass: 22434.189 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-205 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: P22685
#8: Protein UBIQUITIN-60S RIBOSOMAL PROTEIN L40 / UBIQUITIN A-52 RESIDUE RIBOSOMAL PROTEIN FUSION PRODUCT 1 / CEP52


Mass: 6170.682 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 77-128 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: P14794
#9: Protein EUKARYOTIC TRANSLATION INITIATION FACTOR 6 / EIF-6 / EIF6


Mass: 24107.266 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-224 / Source method: isolated from a natural source / Details: ENDOGENOUS PROTEIN / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: UniProt: Q551M2
#10: Protein RIBOSOME MATURATION PROTEIN SBDS / SHWACHMAN-BODIAN-DIAMOND SYNDROME PROTEIN / SBDS


Mass: 28813.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41 / References: UniProt: Q9Y3A5

-
RNA chain , 1 types, 1 molecules N

#11: RNA chain 26S RIBOSOMAL RNA /


Mass: 1205997.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) DICTYOSTELIUM DISCOIDEUM (eukaryote) / Strain: HM2917 / References: GenBank: FR733594.1

-
Details

Sequence detailsRESIDUES 1-205 IN MODEL RESIDUES 1-69 IN THE MODEL NO UBIQUITIN IN MODEL RESIDUES 1-224 IN THE ...RESIDUES 1-205 IN MODEL RESIDUES 1-69 IN THE MODEL NO UBIQUITIN IN MODEL RESIDUES 1-224 IN THE MODEL FRAGMENTS A1221-A1270, C1356-C1602, A2392-U2700 AND A2925- C3480 IN THE MODEL

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: DICTYOSTELIUM 60S CARRYING ENDOGENOUS EIF6 WITH RECOMBINANT HUMAN SBDS
Type: RIBOSOME
Buffer solutionName: 50 MM HEPES-KOH, 100 MM K(CH3COO), 10 MM MG(CH3COO)2, 6 MM BETA-MERCAPTOETHANOL
pH: 7.5
Details: 50 MM HEPES-KOH, 100 MM K(CH3COO), 10 MM MG(CH3COO)2, 6 MM BETA-MERCAPTOETHANOL
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: HOLEY CARBON
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE
Details: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 120, INSTRUMENT- FEI VITROBOT MARK III, METHOD- 6.5S BLOT,

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS / Date: Sep 3, 2013
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 59000 X / Calibrated magnification: 105263 X / Nominal defocus max: 2800 nm / Nominal defocus min: 2200 nm / Cs: 2.2 mm
Image recordingElectron dose: 30 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k)

-
Processing

EM software
IDNameCategory
1REFMACmodel fitting
2RELION3D reconstruction
CTF correctionDetails: EACH PARTICLE
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.3 Å / Num. of particles: 43063 / Nominal pixel size: 1.33 Å / Actual pixel size: 1.33 Å
Details: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3145. (DEPOSITION ID: 13748).
Symmetry type: POINT
Atomic model buildingB value: 94.2 / Protocol: OTHER / Space: RECIPROCAL / Target criteria: FSCAVERAGE / Details: REFINEMENT PROTOCOL--CRYO-EM
RefinementHighest resolution: 3.3 Å
Refinement stepCycle: LAST / Highest resolution: 3.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14935 24758 0 0 39693

+
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