[English] 日本語
Yorodumi
- PDB-9f36: Crystal estructure of AimR from ATCC13952 phage -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9f36
TitleCrystal estructure of AimR from ATCC13952 phage
ComponentsArbitrium receptor from ATCC13952 phage
KeywordsDNA BINDING PROTEIN / Arbitrium system / antiterminator
Function / homologyPHOSPHATE ION / :
Function and homology information
Biological speciesBacillus subtilis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsGallego del Sol, F. / Marina, A.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
European Research Council (ERC)European Union
CitationJournal: To Be Published
Title: Crystal estructure of AimR from ATCC13952 phage
Authors: Gallego del Sol, F. / Marina, A.
History
DepositionApr 25, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 14, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Arbitrium receptor from ATCC13952 phage
B: Arbitrium receptor from ATCC13952 phage
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,6993
Polymers90,6042
Non-polymers951
Water1,18966
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering, Dimer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3400 Å2
ΔGint-19 kcal/mol
Surface area31610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.989, 150.767, 67.335
Angle α, β, γ (deg.)90, 90, 90
Int Tables number18
Space group name H-MP21212

-
Components

#1: Protein Arbitrium receptor from ATCC13952 phage


Mass: 45301.863 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: KS08_10720 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A7U4KS82
#2: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 66 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.47 Å3/Da / Density % sol: 50.12 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop
Details: 1M Ammonium dihydrogen phosphate 0.1M NaCitrate pH 5.6

-
Data collection

DiffractionMean temperature: 290 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.97926 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 17, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97926 Å / Relative weight: 1
ReflectionResolution: 2.058→75.38 Å / Num. obs: 52043 / % possible obs: 99.3 % / Redundancy: 11.2 % / CC1/2: 0.999 / Net I/σ(I): 12.7
Reflection shellResolution: 2.3→2.38 Å / Num. unique obs: 3679 / CC1/2: 0.826

-
Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
autoPROCdata reduction
autoPROCdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→75.38 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.953 / Cross valid method: THROUGHOUT
RfactorNum. reflection% reflectionSelection details
Rfree0.24707 1906 -RANDOM
Rwork0.19266 ---
obs0.19529 36403 99.97 %-
Displacement parametersBiso mean: 73.572 Å2
Baniso -1Baniso -2Baniso -3
1-7.51 Å20 Å20 Å2
2---3.01 Å20 Å2
3----4.5 Å2
Refinement stepCycle: LAST / Resolution: 2.3→75.38 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5665 0 5 66 5736
LS refinement shellResolution: 2.3→2.36 Å /
Rfactor% reflection
Rfree0.462 -
Rwork0.369 -
obs-99.93 %
Refinement TLS params.

Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.06680.05480.43530.04680.38213.573-0.0413-0.0123-0.0362-0.01230.02290.3049-0.03620.30490.01840.20850.01080.03990.0310.03080.1775-23.38729.5431-23.6606
20.4666-0.28780.6680.9709-1.32642.5518-0.0380.0927-0.00690.0927-0.11530.2021-0.00690.20210.15330.27520.00910.08920.0210.01320.2991-22.302-27.0382-21.6695
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A45 - 386
2X-RAY DIFFRACTION2B46 - 386

+
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