[English] 日本語
Yorodumi
- PDB-3hfo: Crystal Structure of an Hfq protein from Synechocystis sp. -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3hfo
TitleCrystal Structure of an Hfq protein from Synechocystis sp.
ComponentsSsr3341 protein
KeywordsRNA BINDING PROTEIN / HFQ / SM / RNA-BINDING PROTEIN / SRNA / TRANSLATIONAL REGULATION
Function / homologySH3 type barrels. - #100 / LSM domain superfamily / SH3 type barrels. / Roll / Mainly Beta / Ssr3341 protein
Function and homology information
Biological speciesSynechocystis sp. PCC 6803 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.3 Å
AuthorsBoggild, A. / Overgaard, M. / Valentin-Hansen, P. / Brodersen, D.E.
CitationJournal: Febs J. / Year: 2009
Title: Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties.
Authors: Boggild, A. / Overgaard, M. / Valentin-Hansen, P. / Brodersen, D.E.
History
DepositionMay 12, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 14, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 16, 2011Group: Atomic model
Revision 1.3Mar 21, 2012Group: Database references
Revision 1.4Mar 7, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.5Sep 6, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ssr3341 protein
B: Ssr3341 protein
C: Ssr3341 protein


Theoretical massNumber of molelcules
Total (without water)23,5203
Polymers23,5203
Non-polymers00
Water4,900272
1
A: Ssr3341 protein
B: Ssr3341 protein
C: Ssr3341 protein

A: Ssr3341 protein
B: Ssr3341 protein
C: Ssr3341 protein


Theoretical massNumber of molelcules
Total (without water)47,0406
Polymers47,0406
Non-polymers00
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
Buried area8200 Å2
ΔGint-58 kcal/mol
Surface area19720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.470, 86.160, 103.180
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number22
Space group name H-MF222
Components on special symmetry positions
IDModelComponents
11B-89-

HOH

21B-95-

HOH

31B-252-

HOH

-
Components

#1: Protein Ssr3341 protein


Mass: 7839.961 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: codons optimised for E. coli expression / Source: (gene. exp.) Synechocystis sp. PCC 6803 (bacteria) / Strain: PCC6803 / Gene: ssr3341 / Plasmid: pTYP11 / Production host: Escherichia coli (E. coli) / Strain (production host): ER2566 / References: UniProt: P74112
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 272 / 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: 1.92 Å3/Da / Density % sol: 36.09 %
Crystal growTemperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 60% Tacsimate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 0.9 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 19, 2008
RadiationMonochromator: Double crystal monochromator, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.21→26.2 Å / Num. obs: 52709 / % possible obs: 96.5 % / Redundancy: 4.8 % / Biso Wilson estimate: 16.864 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 24.23
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
1.21-1.250.9021.411448318079.2
1.25-1.280.8011.916912375696.5
1.28-1.320.6642.518324371197.2
1.32-1.360.5812.817555355897.4
1.36-1.40.4353.617421351697.8
1.4-1.450.3444.716745338097.8
1.45-1.510.2496.416350329898.3
1.51-1.570.1977.915711317598.3
1.57-1.640.15310.115132304298.5
1.64-1.720.11213.314405290798.7
1.72-1.810.07918.313893279398.8
1.81-1.920.05326.513171265099
1.92-2.050.0434.312350250199.4
2.05-2.220.0345.111436230898.9
2.22-2.430.02651.710516212898.7
2.43-2.720.02554.49649196098.7
2.72-3.140.0265.78368169497.8
3.14-3.840.01677.77109143797.2
3.84-5.430.01481.65477112595.9
5.430.01577.2273359087.5

-
Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 51.73
Highest resolutionLowest resolution
Rotation2.5 Å26.2 Å
Translation2.5 Å26.2 Å

-
Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASER2.1.3phasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
XDSdata scaling
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1HK9
Resolution: 1.3→26.199 Å / Occupancy max: 1 / Occupancy min: 0.16 / FOM work R set: 0.891 / SU ML: 0.04 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2 1652 3.78 %
Rwork0.152 --
obs0.154 43747 98.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.911 Å2 / ksol: 0.389 e/Å3
Displacement parametersBiso max: 64.74 Å2 / Biso mean: 17.734 Å2 / Biso min: 5.63 Å2
Baniso -1Baniso -2Baniso -3
1--0.009 Å20 Å2-0 Å2
2--1.237 Å2-0 Å2
3----1.229 Å2
Refinement stepCycle: LAST / Resolution: 1.3→26.199 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1531 0 0 272 1803
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0171667
X-RAY DIFFRACTIONf_angle_d1.7982294
X-RAY DIFFRACTIONf_chiral_restr0.113284
X-RAY DIFFRACTIONf_plane_restr0.008297
X-RAY DIFFRACTIONf_dihedral_angle_d15.115663
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.3-1.3380.2531290.1893480360997
1.338-1.3810.2351320.1713441357398
1.381-1.4310.2291510.1593461361298
1.431-1.4880.2251310.1423491362298
1.488-1.5560.2231370.1323473361098
1.556-1.6380.1911460.1223508365499
1.638-1.740.1691370.1193498363599
1.74-1.8750.1791380.1153547368599
1.875-2.0630.1811430.1263518366199
2.063-2.3620.1551330.1273570370399
2.362-2.9750.2051370.1543563370099
2.975-26.2040.21380.1713545368395

+
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://pdbjlvh1.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