[English] 日本語
Yorodumi
- PDB-5ed8: Crystal structure of CC2-SUN of mouse SUN2 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5ed8
TitleCrystal structure of CC2-SUN of mouse SUN2
ComponentsMKIAA0668 protein
KeywordsTRANSPORT PROTEIN / SUN domain / nuclear membrane
Function / homology
Function and homology information


: / nuclear migration along microfilament / nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration / nuclear matrix anchoring at nuclear membrane / cytoskeleton-nuclear membrane anchor activity / meiotic nuclear membrane microtubule tethering complex / nuclear envelope organization / lamin binding / nuclear inner membrane / centrosome localization ...: / nuclear migration along microfilament / nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration / nuclear matrix anchoring at nuclear membrane / cytoskeleton-nuclear membrane anchor activity / meiotic nuclear membrane microtubule tethering complex / nuclear envelope organization / lamin binding / nuclear inner membrane / centrosome localization / protein-membrane adaptor activity / meiotic cell cycle / condensed nuclear chromosome / nuclear envelope / nuclear membrane / chromosome, telomeric region / endosome membrane / positive regulation of cell migration / identical protein binding
Similarity search - Function
SUN domain-containing protein 2 / SUN domain-containing protein 1-5 / SUN coiled coil domain 2 / SUN2 helix-turn-helix domain / SUN domain profile. / SUN domain / Sad1 / UNC-like C-terminal / Galactose-binding-like domain superfamily
Similarity search - Domain/homology
MKIAA0668 protein / SUN domain-containing protein 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.5 Å
AuthorsNie, S. / Ke, H.M. / Gao, F. / Ren, J.Q. / Wang, M.Z. / Huo, L. / Gong, W.M. / Feng, W.
CitationJournal: Structure / Year: 2016
Title: Coiled-Coil Domains of SUN Proteins as Intrinsic Dynamic Regulators
Authors: Nie, S. / Ke, H. / Gao, F. / Ren, J. / Wang, M. / Huo, L. / Gong, W. / Feng, W.
History
DepositionOct 21, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jan 13, 2016Provider: repository / Type: Initial release
Revision 1.1Jan 20, 2016Group: Database references
Revision 1.2Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: MKIAA0668 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,0752
Polymers30,0511
Non-polymers241
Water1,36976
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area12800 Å2
Unit cell
Length a, b, c (Å)63.374, 63.374, 192.786
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212

-
Components

#1: Protein MKIAA0668 protein


Mass: 30050.902 Da / Num. of mol.: 1 / Fragment: UNP residues 433-694
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: mKIAA0668 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6A022, UniProt: Q8BJS4*PLUS
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 76 / 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: 3.53 Å3/Da / Density % sol: 65.13 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6.9 / Details: 1.4M Na2HPO4/ KH2PO4 / PH range: 6.4-7.3

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 11, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. obs: 14373 / % possible obs: 99.5 % / Redundancy: 4.3 % / Rsym value: 0.077 / Net I/σ(I): 21.6
Reflection shellResolution: 2.5→2.59 Å / Redundancy: 4 % / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
PDB_EXTRACT3.15data extraction
HKL-2000data collection
SHELXCDphasing
PHASERphasing
HKL-2000data scaling
HKL-2000data reduction
RefinementMethod to determine structure: SAD / Resolution: 2.5→32.94 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 28.12 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2545 670 4.92 %
Rwork0.2136 12940 -
obs0.2157 13610 94.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 164.72 Å2 / Biso min: 37.99 Å2
Refinement stepCycle: final / Resolution: 2.5→32.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1870 0 1 76 1947
Biso mean--42.95 71.24 -
Num. residues----245
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0031931
X-RAY DIFFRACTIONf_angle_d0.7292628
X-RAY DIFFRACTIONf_chiral_restr0.032290
X-RAY DIFFRACTIONf_plane_restr0.003345
X-RAY DIFFRACTIONf_dihedral_angle_d14.632692
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Highest resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5002-2.69320.35361320.2988226486
2.6932-2.9640.34471500.2686249794
2.964-3.39250.24121300.2177261297
3.3925-4.27280.2191240.1954270498
4.27280.24291340.2032286398
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)DetailsOrigin x (Å)Origin y (Å)Origin z (Å)
17.91392.29163.05224.249-1.10643.7478-0.36490.408-0.5173-0.25210.31691.27421.1361-1.25080.05960.6354-0.13680.01061.2346-0.31980.9949Chain A group 148.046425.029588.0383
24.36770.4177-3.99891.3592-0.18778.13160.38690.246-0.775-0.6031-0.19920.49670.3414-0.0069-0.14420.3677-0.0569-0.03590.5958-0.19560.5326Chain A group 249.177422.926875.0975
36.16860.3028-0.40096.02530.00297.21440.1567-0.0271-0.2379-0.01250.01360.15050.1903-0.0663-0.15520.2283-0.0246-0.0470.4075-0.05120.3166Chain A group 353.774118.165859.0268
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 454 through 499 )A
2X-RAY DIFFRACTION2chain 'A' and (resid 500 through 574 )A
3X-RAY DIFFRACTION3chain 'A' and (resid 575 through 698 )A

+
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