[English] 日本語
Yorodumi
- PDB-7uln: Turnip yellows virus N-terminal readthrough domain -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7uln
TitleTurnip yellows virus N-terminal readthrough domain
ComponentsMinor capsid protein P3-RTD
KeywordsVIRAL PROTEIN / Viral transmission / dimer / vector interaction
Function / homologyPotato leaf roll virus readthrough protein / Potato leaf roll virus readthrough protein / Luteovirus group 1 coat protein / Luteovirus coat protein / host cell plasmodesma / host cell periplasmic space / viral capsid / structural molecule activity / Readthrough protein P3-RTD
Function and homology information
Biological speciesTurnip yellows virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.53 Å
AuthorsSchiltz, C.J. / Chappie, J.S.
Funding support United States, 1items
OrganizationGrant numberCountry
United States Department of Agriculture (USDA)2019-05200 United States
CitationJournal: Nat Commun / Year: 2022
Title: Polerovirus N-terminal readthrough domain structures reveal molecular strategies for mitigating virus transmission by aphids
Authors: Schiltz, C.J. / Wilson, J.R. / Hosford, C.J. / Adams, M.C. / Preising, S.E. / DeBlasio, S.L. / MacLeod, H.J. / Van Eck, J. / Heck, M.L. / Chappie, J.S.
History
DepositionApr 5, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 2, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Minor capsid protein P3-RTD
B: Minor capsid protein P3-RTD


Theoretical massNumber of molelcules
Total (without water)53,8902
Polymers53,8902
Non-polymers00
Water10,575587
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3870 Å2
ΔGint-23 kcal/mol
Surface area19240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.434, 74.859, 130.779
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Minor capsid protein P3-RTD / P74 / Readthrough protein / RT protein


Mass: 26945.105 Da / Num. of mol.: 2
Fragment: N-terminal readthrough domain (UNP residues 224-461)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Turnip yellows virus / Gene: ORF3/ORF5 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P09514
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 587 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.67 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.7
Details: 0.1 M HEPES, pH 7.7, 1.4 M ammonium sulfate, 0.1 M sodium chloride

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9791 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 21, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 1.53→130.78 Å / Num. obs: 69780 / % possible obs: 99.5 % / Redundancy: 6.7 % / Biso Wilson estimate: 19.33 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.07 / Rpim(I) all: 0.029 / Rrim(I) all: 0.076 / Net I/σ(I): 20.5
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.53-1.556.30.7292025732060.7320.310.7942.293.1
8.36-130.7860.04130625140.9990.0170.04562.399.1

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassificationNB
XDSdata reduction
Aimless0.5.32data scaling
PHASERphasing
PHENIX1.13_2998refinement
PDB_EXTRACT3.27data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 7ULO
Resolution: 1.53→65.389 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 18.85 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1964 3428 4.92 %
Rwork0.174 66276 -
obs0.1751 69704 99.48 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 87.99 Å2 / Biso mean: 24.9293 Å2 / Biso min: 9.98 Å2
Refinement stepCycle: final / Resolution: 1.53→65.389 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3740 0 0 587 4327
Biso mean---33.58 -
Num. residues----472
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.53-1.54880.26021250.2207252492
1.5488-1.5720.23121510.20452708100
1.572-1.59650.23681300.2032768100
1.5965-1.62270.24931320.20152717100
1.6227-1.65070.25581270.19252764100
1.6507-1.68070.23331360.19522727100
1.6807-1.7130.24651510.20632759100
1.713-1.7480.25241380.20642724100
1.748-1.7860.26921380.20172798100
1.786-1.82760.25811240.19482717100
1.8276-1.87330.26231560.18692768100
1.8733-1.92390.21121530.18342741100
1.9239-1.98050.21231600.17942701100
1.9805-2.04450.17351490.16952757100
2.0445-2.11750.22111390.17322762100
2.1175-2.20230.17031480.17292778100
2.2023-2.30260.20641180.17172776100
2.3026-2.4240.21811380.17592798100
2.424-2.57580.21971660.18322769100
2.5758-2.77470.20111650.18152776100
2.7747-3.05390.17331360.18132795100
3.0539-3.49580.19071190.16332842100
3.4958-4.40420.14631420.1447285399
4.4042-65.3890.18121870.1681295499

+
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