[English] 日本語
Yorodumi
- PDB-5elk: Crystal structure of mouse Unkempt zinc fingers 4-6 (ZnF4-6), bou... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5elk
TitleCrystal structure of mouse Unkempt zinc fingers 4-6 (ZnF4-6), bound to RNA
Components
  • RING finger protein unkempt homolog
  • RNA
KeywordsRNA BINDING PROTEIN/RNA / Unkempt / RNA-binding protein / CCCH zinc fingers / RNA BINDING PROTEIN-RNA complex
Function / homology
Function and homology information


mRNA CDS binding / : / : / cell morphogenesis involved in neuron differentiation / negative regulation of cytoplasmic translation / neuron migration / in utero embryonic development / metal ion binding / cytoplasm
Similarity search - Function
Unkempt, zinc finger domain 1 / RING finger protein Unkempt-like / Unkempt Zinc finger domain 1 (Znf1) / Zinc finger C-x8-C-x5-C-x3-H type (and similar) / Zinc finger, CCCH-type superfamily / zinc finger / Zinc finger, CCCH-type / Zinc finger C3H1-type profile.
Similarity search - Domain/homology
RNA / RING finger protein unkempt homolog
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å
AuthorsTeplova, M. / Murn, J. / Zarnack, K. / Shi, Y. / Patel, D.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM104962 United States
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2016
Title: Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt.
Authors: Murn, J. / Teplova, M. / Zarnack, K. / Shi, Y. / Patel, D.J.
History
DepositionNov 4, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 9, 2015Provider: repository / Type: Initial release
Revision 1.1Dec 23, 2015Group: Database references
Revision 1.2Jan 20, 2016Group: Database references
Revision 1.3Apr 6, 2016Group: Source and taxonomy
Revision 1.4Sep 27, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Mar 6, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: RING finger protein unkempt homolog
R: RNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,3035
Polymers17,1072
Non-polymers1963
Water34219
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)70.192, 51.203, 37.460
Angle α, β, γ (deg.)90.00, 97.18, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein RING finger protein unkempt homolog / Zinc finger CCCH domain-containing protein 5


Mass: 15231.030 Da / Num. of mol.: 1 / Fragment: UNP residues 204-335
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Unk, Kiaa1753, Zc3h5, Zc3hdc5 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8BL48
#2: RNA chain RNA


Mass: 1876.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse)
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 19 / 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: 2.1 Å3/Da / Density % sol: 37 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Hepes pH 7.0, 17 % PEG 3350

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1.2828 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 21, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2828 Å / Relative weight: 1
ReflectionResolution: 2.29→41.25 Å / Num. obs: 5787 / % possible obs: 96.7 % / Redundancy: 3.7 % / Net I/σ(I): 16

-
Processing

Software
NameVersionClassification
PHENIXrefinement
PDB_EXTRACT3.15data extraction
XDSdata reduction
SCALAdata scaling
AutoSolphasing
RefinementResolution: 2.3→19.348 Å / FOM work R set: 0.7947 / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.41 / Phase error: 26.73 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2235 263 4.6 %
Rwork0.1805 5458 -
obs0.1824 5721 96.33 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 168.94 Å2 / Biso mean: 52.74 Å2 / Biso min: 22.77 Å2
Refinement stepCycle: final / Resolution: 2.3→19.348 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms983 90 3 19 1095
Biso mean--60.89 42.22 -
Num. residues----127
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0081129
X-RAY DIFFRACTIONf_angle_d1.1641549
X-RAY DIFFRACTIONf_chiral_restr0.061146
X-RAY DIFFRACTIONf_plane_restr0.006191
X-RAY DIFFRACTIONf_dihedral_angle_d16.366447
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 2

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3-2.89630.29681320.22462665279794
2.8963-19.34890.20631310.1712793292498
Refinement TLS params.

Method: refined / 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)
16.98650.89650.54151.4856-0.68172.2561-0.125-0.7992-0.41590.390.01180.13040.0625-0.05630.10820.3760.08920.05710.32360.02640.354815.60034.459627.4412
23.00062.29761.81776.533-2.4726.7488-0.3718-0.1071.254-0.57720.29630.40.0676-1.60860.66780.63430.045-0.12820.3659-0.03450.535515.323113.660623.3703
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 204 through 324)A0
2X-RAY DIFFRACTION2chain 'R' and (resid 2 through 7 )R0

+
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