[English] 日本語
Yorodumi
- PDB-6wmf: Human Sun2-KASH5 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6wmf
TitleHuman Sun2-KASH5 complex
Components
  • Protein KASH5
  • SUN domain-containing protein 2
KeywordsSTRUCTURAL PROTEIN / LINC Complex
Function / homology
Function and homology information


telomere localization / : / chromosome localization to nuclear envelope involved in homologous chromosome segregation / 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 / spindle localization / meiotic spindle pole / meiotic nuclear membrane microtubule tethering complex ...telomere localization / : / chromosome localization to nuclear envelope involved in homologous chromosome segregation / 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 / spindle localization / meiotic spindle pole / meiotic nuclear membrane microtubule tethering complex / homologous chromosome pairing at meiosis / lateral element / lamin binding / nuclear outer membrane / nuclear migration / nuclear inner membrane / centrosome localization / dynein complex binding / oogenesis / spindle assembly / protein-membrane adaptor activity / Meiotic synapsis / mitotic spindle organization / meiotic cell cycle / condensed nuclear chromosome / actin filament organization / double-strand break repair via homologous recombination / nuclear envelope / spermatogenesis / microtubule binding / nuclear membrane / chromosome, telomeric region / endosome membrane / positive regulation of cell migration / identical protein binding
Similarity search - Function
KASH5-like coiled-coil domain / Protein KASH5 / Protein KASH5, EF-hand-like domain / EF-hand domain / Coiled-coil region of CCDC155 or KASH / SUN domain-containing protein 1-5 / SUN coiled coil domain 2 / SUN2 helix-turn-helix domain / SUN domain profile. / SUN domain ...KASH5-like coiled-coil domain / Protein KASH5 / Protein KASH5, EF-hand-like domain / EF-hand domain / Coiled-coil region of CCDC155 or KASH / 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 / EF-hand domain pair
Similarity search - Domain/homology
: / Protein KASH5 / SUN domain-containing protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsCruz, V.E. / Schwartz, T.U.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)AR065484 United States
CitationJournal: J.Mol.Biol. / Year: 2020
Title: Structural Analysis of Different LINC Complexes Reveals Distinct Binding Modes.
Authors: Cruz, V.E. / Esra Demircioglu, F. / Schwartz, T.U.
History
DepositionApr 21, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 2, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 9, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Oct 18, 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: SUN domain-containing protein 2
B: Protein KASH5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,1583
Polymers25,1192
Non-polymers391
Water19811
1
A: SUN domain-containing protein 2
B: Protein KASH5
hetero molecules

A: SUN domain-containing protein 2
B: Protein KASH5
hetero molecules

A: SUN domain-containing protein 2
B: Protein KASH5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,4759
Polymers75,3576
Non-polymers1173
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_785-y+2,x-y+3,z1
crystal symmetry operation3_475-x+y-1,-x+2,z1
Buried area12950 Å2
ΔGint-85 kcal/mol
Surface area25460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.435, 78.435, 249.441
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number155
Space group name H-MH32
Space group name HallR32"
Symmetry operation#1: x,y,z
#2: -y,x-y,z
#3: -x+y,-x,z
#4: x-y,-y,-z
#5: -x,-x+y,-z
#6: y,x,-z
#7: x+1/3,y+2/3,z+2/3
#8: -y+1/3,x-y+2/3,z+2/3
#9: -x+y+1/3,-x+2/3,z+2/3
#10: x-y+1/3,-y+2/3,-z+2/3
#11: -x+1/3,-x+y+2/3,-z+2/3
#12: y+1/3,x+2/3,-z+2/3
#13: x+2/3,y+1/3,z+1/3
#14: -y+2/3,x-y+1/3,z+1/3
#15: -x+y+2/3,-x+1/3,z+1/3
#16: x-y+2/3,-y+1/3,-z+1/3
#17: -x+2/3,-x+y+1/3,-z+1/3
#18: y+2/3,x+1/3,-z+1/3

-
Components

#1: Protein SUN domain-containing protein 2 / Protein unc-84 homolog B / Rab5-interacting protein / Rab5IP / Sad1/unc-84 protein-like 2


Mass: 22381.025 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SUN2, FRIGG, KIAA0668, RAB5IP, UNC84B / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UH99
#2: Protein/peptide Protein KASH5 / Coiled-coil domain-containing protein 155 / KASH domain-containing protein 5


Mass: 2738.102 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CCDC155, KASH5 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8N6L0
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.24 Å3/Da / Density % sol: 62.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 14% PEG3000, 0.1M BisTris/HCl

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 31, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.6→83.15 Å / Num. obs: 9383 / % possible obs: 99.2 % / Redundancy: 15.9 % / Biso Wilson estimate: 79.34 Å2 / CC1/2: 0.999 / Rpim(I) all: 0.025 / Net I/σ(I): 37.3
Reflection shellResolution: 2.6→2.74 Å / Redundancy: 6.3 % / Mean I/σ(I) obs: 0.9 / Num. unique obs: 1257 / CC1/2: 0.51 / Rpim(I) all: 0.466 / % possible all: 95

-
Processing

Software
NameVersionClassification
PHENIX1.17_3644refinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4DXT
Resolution: 2.6→83.15 Å / SU ML: 0.5021 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 35.3665
RfactorNum. reflection% reflection
Rfree0.2859 938 10 %
Rwork0.2212 --
obs0.2278 9383 99.22 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 96.72 Å2
Refinement stepCycle: LAST / Resolution: 2.6→83.15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1584 0 1 11 1596
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00971628
X-RAY DIFFRACTIONf_angle_d1.21312222
X-RAY DIFFRACTIONf_chiral_restr0.0696247
X-RAY DIFFRACTIONf_plane_restr0.0076288
X-RAY DIFFRACTIONf_dihedral_angle_d22.2836216
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.740.43531240.33361133X-RAY DIFFRACTION95.44
2.74-2.910.42491340.3251190X-RAY DIFFRACTION99.62
2.91-3.140.35221310.26471192X-RAY DIFFRACTION99.77
3.14-3.450.29571330.22971197X-RAY DIFFRACTION99.92
3.45-3.950.26091350.20551218X-RAY DIFFRACTION99.85
3.95-4.980.231370.18851219X-RAY DIFFRACTION99.85
4.98-83.150.29511440.21931296X-RAY DIFFRACTION99.93
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)
16.119375153144.12432795864-5.910717607792.78405770046-3.867331158655.802982060540.06606353903931.144680857410.7819103150350.07462029654380.3727297242730.71805878563-1.55985765375-3.026794497820.004999465573811.214206332290.0438941102625-0.1025342655231.090483617720.082840784490.697135728329-45.0826671881115.294489164240.964096418
24.865325510571.378125302641.777424271221.90421540570.606290062855.25476215590.563028853805-0.708273561619-0.4176911281810.120788242357-0.0645153628442-0.115595299931.21347724673-0.00204940434838-0.5228551774420.906669535980.0145878340038-0.02690476618570.7484043918120.04214783452650.535894814078-43.89235324100.897684196272.179201863
37.83823119845-1.475164083931.065700406393.47555961758-2.600389304528.92018793886-0.0349046490218-1.108684515490.1364668746830.419842519944-0.022773565392-0.147559158617-0.357835270241-0.09588607611880.01358872962570.754530589012-0.0267121497867-0.1104257071570.6084916965010.01291147319640.425925069135-39.540426067998.7861211805271.997921675
45.27281628925-1.16181996748-1.251439997473.952555005352.321376479882.19847527375-0.4268891431110.385630875735-0.04196075938670.3192296888610.3740498904320.2888760650960.564469568366-0.2602762128850.1972916464610.846631372443-0.0932631759721-0.1153648173870.6786926873590.05375499692640.369747317959-49.241565641897.8467108857263.136271863
52.03206946565-1.12347826282-4.125189310123.763923111251.655497798489.73005384166-0.883497672069-0.475529582817-1.325483157840.07647619522030.323523295099-0.1267538447921.5122936801-0.09140571207960.3414637151661.10464926659-0.00270618107108-0.1853061108280.5061567040380.1070721419940.708565311195-48.776263677290.0125524073265.092401989
67.17243687133-2.41301175099-0.3582240411935.46595086366-1.042766560825.110323603370.2423005729230.420115541232-0.827191917501-0.7530342747160.1222467201310.2674215648641.207628201810.252803757418-0.4087995074340.772791454238-0.0421320278444-0.09517317600440.684568092227-0.007821334861590.562773928582-46.940047341491.1551687725261.345767433
77.801575355643.857716439617.233508768347.569466979210.201142042969.342788220680.837291239757-0.9163245406381.219688668210.385947831036-0.8782685115280.4092278472250.126335713337-1.302722201260.5311075036990.7868553090570.1617845171430.02114278062150.974570736319-0.1241177597170.473422154171-56.4513306422101.720117479260.696397229
82.19589434747-0.7377534963990.7386499180935.314414205265.118445639235.700562223910.05808296422240.177978890789-0.4911884219411.553418105171.72202925513-2.317466217680.4639918752520.918831230179-1.247064088930.9227896429-0.100213269703-0.08654211753440.969690356335-0.08227992550890.703677495577-27.5396128268106.279118404277.62866563
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 522 through 540 )
2X-RAY DIFFRACTION2chain 'A' and (resid 541 through 581 )
3X-RAY DIFFRACTION3chain 'A' and (resid 582 through 608 )
4X-RAY DIFFRACTION4chain 'A' and (resid 609 through 634 )
5X-RAY DIFFRACTION5chain 'A' and (resid 635 through 659 )
6X-RAY DIFFRACTION6chain 'A' and (resid 660 through 707 )
7X-RAY DIFFRACTION7chain 'A' and (resid 708 through 717 )
8X-RAY DIFFRACTION8chain 'B' and (resid 783 through 797 )

+
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