[English] 日本語
Yorodumi
- PDB-5ifn: Human PSPC1 Homodimer -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5ifn
TitleHuman PSPC1 Homodimer
ComponentsParaspeckle component 1
KeywordsRNA BINDING PROTEIN / DBHS protein RNA binding
Function / homology
Function and homology information


non-membrane-bounded organelle assembly / paraspeckles / activation of innate immune response / regulation of circadian rhythm / fibrillar center / nuclear matrix / rhythmic process / nuclear speck / innate immune response / negative regulation of DNA-templated transcription ...non-membrane-bounded organelle assembly / paraspeckles / activation of innate immune response / regulation of circadian rhythm / fibrillar center / nuclear matrix / rhythmic process / nuclear speck / innate immune response / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / RNA binding / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
PSP1, RNA recognition motif 1 / PSP1, RNA recognition motif 2 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1170 / NOPS / NOPS (NUC059) domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / RRM (RNA recognition motif) domain / Helix non-globular / RNA recognition motif / RNA recognition motif ...PSP1, RNA recognition motif 1 / PSP1, RNA recognition motif 2 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1170 / NOPS / NOPS (NUC059) domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / RRM (RNA recognition motif) domain / Helix non-globular / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Special / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Paraspeckle component 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.17 Å
AuthorsKnott, G.J. / Passon, D.M. / Bond, C.S.
CitationJournal: To Be Published
Title: Human PSPC1 Homodimer
Authors: Knott, G.J. / Passon, D.M. / Bond, C.S.
History
DepositionFeb 26, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 9, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 27, 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: Paraspeckle component 1
B: Paraspeckle component 1


Theoretical massNumber of molelcules
Total (without water)59,8862
Polymers59,8862
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10020 Å2
ΔGint-54 kcal/mol
Surface area27310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.536, 63.493, 67.800
Angle α, β, γ (deg.)90.00, 98.06, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein Paraspeckle component 1 / / Paraspeckle protein 1


Mass: 29943.121 Da / Num. of mol.: 2 / Fragment: UNP residues 61-320
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSPC1, PSP1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8WXF1

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.23 Å3/Da / Density % sol: 44.84 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 100 mM (D/L) malic acid pH 7.0 28% PEG 3350 100 mM Tris pH 7.0
Temp details: +/- 0.5 K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 1.542 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 4, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.542 Å / Relative weight: 1
ReflectionResolution: 3.17→19.41 Å / Num. obs: 8738 / % possible obs: 97.7 % / Redundancy: 3.6 % / Biso Wilson estimate: 62.07 Å2 / Net I/σ(I): 5.7

-
Processing

Software
NameVersionClassification
BUSTER2.10.0refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3SDE
Resolution: 3.17→19.41 Å / Cor.coef. Fo:Fc: 0.8233 / Cor.coef. Fo:Fc free: 0.7123 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.608
RfactorNum. reflection% reflectionSelection details
Rfree0.2889 413 4.73 %RANDOM
Rwork0.2368 ---
obs0.2393 8738 98.05 %-
Displacement parametersBiso mean: 59.86 Å2
Baniso -1Baniso -2Baniso -3
1-20.7669 Å20 Å22.9385 Å2
2---24.356 Å20 Å2
3---3.5891 Å2
Refine analyzeLuzzati coordinate error obs: 0.653 Å
Refinement stepCycle: LAST / Resolution: 3.17→19.41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4112 0 0 0 4112
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0094193HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.135641HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1545SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes122HARMONIC2
X-RAY DIFFRACTIONt_gen_planes604HARMONIC5
X-RAY DIFFRACTIONt_it4193HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.83
X-RAY DIFFRACTIONt_other_torsion20.92
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion529SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact4798SEMIHARMONIC4
LS refinement shellResolution: 3.17→3.54 Å / Total num. of bins used: 5
RfactorNum. reflection% reflection
Rfree0.2912 114 4.55 %
Rwork0.2566 2390 -
all0.2583 2504 -
obs--98.05 %

+
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