[English] 日本語
Yorodumi
- EMDB-40208: Backbone model of de novo-designed chlorophyll-binding nanocage O32-15 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-40208
TitleBackbone model of de novo-designed chlorophyll-binding nanocage O32-15
Map dataBackbone model of de novo-designed chlorophyll-binding nanocage O32-15
Sample
  • Complex: Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM
    • Protein or peptide: C3-comp_O32-15, polyalanine model
    • Protein or peptide: C2-chlorophyll-comp_O32-15_ctermHis, polyalanine model
Keywordsnanocage / helical repeats / chlorophyll-binding / octahedral symmetry / DE NOVO PROTEIN
Biological speciessynthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.5 Å
AuthorsRedler RL / Ennist NM / Wang S / Baker D / Ekiert DC / Bhabha G
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)5U19AG065156-02 United States
Other private
CitationJournal: To Be Published
Title: De novo design of energy transfer proteins housing excitonically coupled chlorophyll special pairs
Authors: Ennist NM / Wang S / Kennedy MA / Curti M / Sutherland GA / Vasilev C / Redler RL / Maffeis V / Shareef S / Sica AV / Hua AS / Deshmukh AP / Moyer AP / Hicks DR / Swartz AZ / Cacho RA / Novy ...Authors: Ennist NM / Wang S / Kennedy MA / Curti M / Sutherland GA / Vasilev C / Redler RL / Maffeis V / Shareef S / Sica AV / Hua AS / Deshmukh AP / Moyer AP / Hicks DR / Swartz AZ / Cacho RA / Novy N / Bera AK / Kang A / Sankaran B / Johnson MP / Reppert M / Ekiert DC / Bhabha G / Stewart L / Caram JR / Stoddard BL / Romero E / Hunter CN / Baker D
History
DepositionMar 23, 2023-
Header (metadata) releaseMar 27, 2024-
Map releaseMar 27, 2024-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_40208.map.gz / Format: CCP4 / Size: 184 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationBackbone model of de novo-designed chlorophyll-binding nanocage O32-15
Voxel sizeX=Y=Z: 1.076 Å
Density
Contour LevelBy AUTHOR: 0.17
Minimum - Maximum-0.042963542 - 0.44251803
Average (Standard dev.)0.0041361395 (±0.038141657)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions364364364
Spacing364364364
CellA=B=C: 391.664 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: Half Map 1

Fileemd_40208_half_map_1.map
AnnotationHalf Map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half Map 2

Fileemd_40208_half_map_2.map
AnnotationHalf Map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM

EntireName: Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM
Components
  • Complex: Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM
    • Protein or peptide: C3-comp_O32-15, polyalanine model
    • Protein or peptide: C2-chlorophyll-comp_O32-15_ctermHis, polyalanine model

-
Supramolecule #1: Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM

SupramoleculeName: Chlorophyll-binding nanocage O32-15 loaded with ZnPPaM
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: synthetic construct (others)

-
Macromolecule #1: C3-comp_O32-15, polyalanine model

MacromoleculeName: C3-comp_O32-15, polyalanine model / type: protein_or_peptide / ID: 1 / Number of copies: 24 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 35.889559 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSTKEKARQL AEEAKETAEK VGDPELIKLA EQASQEGDSE KAKAILLAAE AARVAKEVGA PDLIRLARIA ARVGASEAAK AILLAAEAA RVAKEVGDPE LERLALLAAV LGDSEKAKAI LLAAEAARVA KEVGDPELIK LALEAAERGD SEKAKAILLA A EAARVAKE ...String:
MSTKEKARQL AEEAKETAEK VGDPELIKLA EQASQEGDSE KAKAILLAAE AARVAKEVGA PDLIRLARIA ARVGASEAAK AILLAAEAA RVAKEVGDPE LERLALLAAV LGDSEKAKAI LLAAEAARVA KEVGDPELIK LALEAAERGD SEKAKAILLA A EAARVAKE VGDPELIKLA LEAARRGDSE KAKAILLAAE AARVAKEVGD PELIKLALEA ARRGDSRKAE AILLAAEAAR IA KEAGDPE ARKKALEAAR RGDRELATRI LIEALLRLLK KSTAELKRAT ASLRAITEEL KKNPSEDALV EHNRAIVEHN AII VENNRI IAMVLEAIVR AI

-
Macromolecule #2: C2-chlorophyll-comp_O32-15_ctermHis, polyalanine model

MacromoleculeName: C2-chlorophyll-comp_O32-15_ctermHis, polyalanine model
type: protein_or_peptide / ID: 2 / Number of copies: 24 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 27.799957 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MDEEFKFLAT EAKMLITAAE RLAGTDPRLQ EMVALIKKEL EQAERTFRNG DKSEAQRQLE FVLTAARAVM NVAAAANAAG TDPLLKAMV DAILWRLKEA IRTFQNGDQE EAETQLRFVL RAAIAVAVVA AALVLAGTDP ELQEMVEQIK DLLISAFMAG A RGDKEKAL ...String:
MDEEFKFLAT EAKMLITAAE RLAGTDPRLQ EMVALIKKEL EQAERTFRNG DKSEAQRQLE FVLTAARAVM NVAAAANAAG TDPLLKAMV DAILWRLKEA IRTFQNGDQE EAETQLRFVL RAAIAVAVVA AALVLAGTDP ELQEMVEQIK DLLISAFMAG A RGDKEKAL TQLLFVAWAA HAVAMIAAAA NLAGTDPRLQ QQVKEILEKL KEAIETFQKG DEEQAFRQLA EVLAEAALVA LR AALTNLE HHHHHH

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.7 mg/mL
BufferpH: 8
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 5 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.3 µm / Nominal magnification: 64000
Specialist opticsEnergy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 2 / Average exposure time: 2.0 sec. / Average electron dose: 49.99 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 359331
Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.0)
Final reconstructionApplied symmetry - Point group: O (octahedral) / Resolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.0) / Number images used: 205014

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-8glt:
Backbone model of de novo-designed chlorophyll-binding nanocage O32-15

+
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