[English] 日本語
Yorodumi
- EMDB-47896: Focused map of the PH domain in the structure of the CARMIL dimer... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-47896
TitleFocused map of the PH domain in the structure of the CARMIL dimer bound to Capping Protein
Map data
Sample
  • Complex: Complex of the CARMIL dimer bound to Capping Protein
    • Protein or peptide: CARMIL
    • Protein or peptide: CapZ alpha
    • Protein or peptide: CapZ beta
Keywordscytoskeleton / membrane / cell motility / STRUCTURAL PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsBarrie KR / Dominguez R
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM073791 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM152412 United States
CitationJournal: To Be Published
Title: Structural basis for regulation of Capping Protein by the CARMIL dimer
Authors: Barrie KR / Dominguez R
History
DepositionNov 13, 2024-
Header (metadata) releaseJan 21, 2026-
Map releaseJan 21, 2026-
UpdateJan 21, 2026-
Current statusJan 21, 2026Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_47896.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.)
0.83 Å/pix.
x 384 pix.
= 317.184 Å
0.83 Å/pix.
x 384 pix.
= 317.184 Å
0.83 Å/pix.
x 384 pix.
= 317.184 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.826 Å
Density
Contour LevelBy AUTHOR: 0.004
Minimum - Maximum-0.004968855 - 0.013431722
Average (Standard dev.)0.00001386929 (±0.0003694658)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 317.184 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_47896_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_47896_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_47896_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Complex of the CARMIL dimer bound to Capping Protein

EntireName: Complex of the CARMIL dimer bound to Capping Protein
Components
  • Complex: Complex of the CARMIL dimer bound to Capping Protein
    • Protein or peptide: CARMIL
    • Protein or peptide: CapZ alpha
    • Protein or peptide: CapZ beta

-
Supramolecule #1: Complex of the CARMIL dimer bound to Capping Protein

SupramoleculeName: Complex of the CARMIL dimer bound to Capping Protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Molecular weightTheoretical: 370 KDa

-
Macromolecule #1: CARMIL

MacromoleculeName: CARMIL / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MHHHHHHGMT EESSDVPREL IESIKDVIGR KIKISVKKKV KLEVKGDKVE NKVLVLTSCR AFLVTARIPT KLELTFSYLE IHGVVCSKSA QMIVETEKCS ISMKMASPED VSEVLAHIGT CLRKIFPGLS PVRIMKKVSM EPSERLASLQ ALWDSQTVAE QGPCGGFSQM ...String:
MHHHHHHGMT EESSDVPREL IESIKDVIGR KIKISVKKKV KLEVKGDKVE NKVLVLTSCR AFLVTARIPT KLELTFSYLE IHGVVCSKSA QMIVETEKCS ISMKMASPED VSEVLAHIGT CLRKIFPGLS PVRIMKKVSM EPSERLASLQ ALWDSQTVAE QGPCGGFSQM YACVCDWLGF SYREEVQWDV DTIYLTQDTR ELNLQDFSHL DHRDLIPIIA ALEYNQWFTK LSSKDLKLST DVCEQILRVV SRSNRLEELV LENAGLRTDF AQKLASALAH NPNSGLHTIN LAGNPLEDRG VSSLSIQFAK LPKGLKHLNL SKTSLSPKGV NSLSQSLSAN PLTASTLVHL DLSGNVLRGD DLSHMYNFLA QPNAIVHLDL SNTECSLDMV CGALLRGCLQ YLAVLNLSRT VFSHRKGKEV PPSFKQFFSS SLALMHINLS GTKLSPEPLK ALLLGLACNH NLKGVSLDLS NCELRSGGAQ VLEGCIAEIH NITSLDISDN GLESDLSTLI VWLSKNRSIQ HLALGKNFNN MKSKNLTPVL DNLVQMIQDE ESPLQSLSLA DSKLKTEVTI IINALGSNTS LTKVDISGNG MGDMGAKMLA KALQINTKLR TVIWDKNNIT AQGFQDIAVA MEKNYTLRFM PIPMYDASQA LKTNPEKTED ALQKIENYLL RNHETRKYLQ EQAYRLQQGI VTSTTQQMID RICVKVQDHL NSLRNCGGDA IQEDLKSAER LMRDAKNSKT LLPNLYHVGG ASWAGASGLL SSPIQETLES MAGEVTRVVD EQLKALLESM VDAAENLCPN VMKKAHIRQD LIHASTEKIS IPRTFVKNVL LEQSGIDILN KISEVKLTVA SFLSDRIVDE ILDALSHCHH KLADHFSRRG KTLPQQESLE IELAEEKPVK RSIITVEELT EIERLEDLDT CMMTPKSKRK SIHSRMLRPV SRAFEMEFDL DKALEEVPIH IEDPPFPSLR QEKRSSGFIS ELPSEEGKKL EHFTKLRPKR NKKQQPTQAA VCAANIVSQD GEQNGLMGRV DEGVDEFFTK KVTKMDSKKW STRGWSHPQF EK

-
Macromolecule #2: CapZ alpha

MacromoleculeName: CapZ alpha / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN ...String:
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA

-
Macromolecule #3: CapZ beta

MacromoleculeName: CapZ beta / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: SDQQLDCALD LMRRLPPQQI EKNLSDLIDL VPSLCEDLLS SVDQPLKIAR DKVVGKDYLL CDYNRDGDSY RSPWSNKYDP PLEDGAMPSA RLRKLEVEAN NAFDQYRDLY FEGGVSSVYL WDLDHGFAGV ILIKKAGDGS KKIKGCWDSI HVVEVQEKSS GRTAHYKLTS ...String:
SDQQLDCALD LMRRLPPQQI EKNLSDLIDL VPSLCEDLLS SVDQPLKIAR DKVVGKDYLL CDYNRDGDSY RSPWSNKYDP PLEDGAMPSA RLRKLEVEAN NAFDQYRDLY FEGGVSSVYL WDLDHGFAGV ILIKKAGDGS KKIKGCWDSI HVVEVQEKSS GRTAHYKLTS TVMLWLQTNK SGSGTMNLGG SLTRQMEKDE TVSDCSPHIA NIGRLVEDME NKIRSTLNEI YFGKTKDIVN GLRSIDAIPD NQKFKQLQRE LSQVLTQRQI YIQPDN

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 47.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL / Details: ab-initio model generated in cryoSPARC
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 135195
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

+
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