[English] 日本語
Yorodumi
- PDB-4wyv: Crystal Structure of Human Translin in Open Conformation -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4wyv
TitleCrystal Structure of Human Translin in Open Conformation
ComponentsTranslin
KeywordsRNA BINDING PROTEIN / Translin / Octomer / RNA / Open / Barrel
Function / homology
Function and homology information


endoribonuclease complex / Small interfering RNA (siRNA) biogenesis / regulatory ncRNA-mediated post-transcriptional gene silencing / siRNA processing / male germ cell nucleus / single-stranded DNA binding / endonuclease activity / DNA recombination / sequence-specific DNA binding / Hydrolases; Acting on ester bonds ...endoribonuclease complex / Small interfering RNA (siRNA) biogenesis / regulatory ncRNA-mediated post-transcriptional gene silencing / siRNA processing / male germ cell nucleus / single-stranded DNA binding / endonuclease activity / DNA recombination / sequence-specific DNA binding / Hydrolases; Acting on ester bonds / mRNA binding / endoplasmic reticulum / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Translin; domain 2 / Translin; domain 1 / Translin, N-terminal / Translin, C-terminal / Translin / Translin family / Translin superfamily / Translin family / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsDvir, H. / Eliahoo, E. / Alian, A.
CitationJournal: J.Mol.Biol. / Year: 2015
Title: A novel open-barrel structure of octameric translin reveals a potential RNA entryway.
Authors: Eliahoo, E. / Marx, A. / Manor, H. / Alian, A.
History
DepositionNov 18, 2014Deposition site: RCSB / Processing site: PDBE
SupersessionNov 26, 2014ID: 4jhf
Revision 1.0Nov 26, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 17, 2014Group: Database references
Revision 1.2Feb 18, 2015Group: Database references
Revision 1.3Jan 10, 2024Group: 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: Translin
B: Translin
C: Translin
D: Translin
E: Translin
F: Translin
G: Translin
H: Translin


Theoretical massNumber of molelcules
Total (without water)221,0048
Polymers221,0048
Non-polymers00
Water32418
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21910 Å2
ΔGint-110 kcal/mol
Surface area72930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.308, 82.308, 635.164
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

-
Components

#1: Protein
Translin / / Component 3 of promoter of RISC / C3PO


Mass: 27625.498 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TSN / Production host: Escherichia coli (E. coli)
References: UniProt: Q15631, Hydrolases; Acting on ester bonds
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49.46 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 0.05M MES, 0.2M KCL, 0.01M MGCL2, 5% PEG8000, PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.8726 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 3, 2012
RadiationMonochromator: Si(111) Single Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 3→58.2 Å / Num. obs: 45180 / % possible obs: 98.4 % / Redundancy: 13.2 % / Rsym value: 0.113 / Net I/σ(I): 15.1
Reflection shellResolution: 3→3.16 Å / Redundancy: 9.8 % / Rmerge(I) obs: 0.645 / Mean I/σ(I) obs: 3.3 / % possible all: 90.5

-
Processing

Software
NameVersionClassification
REFMAC5.5.0109refinement
SCALAdata scaling
MOSFLMdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1j1j
Resolution: 3→58 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.895 / SU B: 48.631 / SU ML: 0.393 / Cross valid method: THROUGHOUT / ESU R Free: 0.476 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27212 2272 5 %RANDOM
Rwork0.22551 ---
obs0.22786 42759 98.55 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 81.457 Å2
Baniso -1Baniso -2Baniso -3
1-0.23 Å20 Å20 Å2
2--0.23 Å20 Å2
3----0.46 Å2
Refinement stepCycle: LAST / Resolution: 3→58 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13917 0 0 18 13935
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.02214164
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.4061.96719106
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.20251686
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.96223.177702
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.891152617
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.53415128
X-RAY DIFFRACTIONr_chiral_restr0.0980.22195
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0210509
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7121.58443
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.401213678
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.93335721
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.4784.55428
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3→3.078 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.334 158 -
Rwork0.315 2632 -
obs--84.6 %
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)
12.1776-0.5027-1.99121.48740.19183.9410.12150.15350.10330.0449-0.0755-0.5273-0.19680.3675-0.0460.1693-0.0523-0.14970.16590.02960.310119.424-6.72461.491
21.0933-0.6994-0.94243.6242.34474.4791-0.03730.073-0.15090.0895-0.1772-0.1810.35430.310.21450.240.0301-0.19090.13210.09390.325512.379-40.87560.549
31.03090.0206-0.77941.5366-2.70186.8027-0.06520.1157-0.05520.15230.09580.0359-0.3184-0.7097-0.03060.20030.0922-0.03690.1874-0.0350.0816-13.5585.11458.552
40.65490.68-0.94991.5608-2.55445.1012-0.05570.1123-0.0619-0.393-0.0114-0.030.2739-0.20670.06720.50670.1228-0.03870.1523-0.01110.1028-6.945-47.40119.231
50.1387-0.1111-0.11571.79022.28574.50120.07780.03340.1381-0.3231-0.0355-0.3305-0.56240.3291-0.04230.42430.04920.12680.34130.13780.354117.297-1.27225.125
61.6096-0.2286-1.47210.81760.26333.25080.0608-0.0905-0.0652-0.0643-0.0890.04990.1717-0.35390.02820.26660.0979-0.08920.52470.03940.0974-17.567-5.04523.822
70.56330.16461.1490.75690.42673.83430.07810.07260.0509-0.0562-0.1511-0.55080.240.50430.0730.39960.22410.00010.50120.18310.492225.192-35.50126.068
81.40040.34321.5381.16450.45916.06250.08120.08090.1495-0.2521-0.14190.2594-0.2488-0.51770.06060.18280.0534-0.06440.1885-0.0060.1804-21.26-38.66251.993
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 217
2X-RAY DIFFRACTION2B1 - 217
3X-RAY DIFFRACTION3C0 - 216
4X-RAY DIFFRACTION4D-1 - 217
5X-RAY DIFFRACTION5E0 - 217
6X-RAY DIFFRACTION6F0 - 217
7X-RAY DIFFRACTION7G1 - 217
8X-RAY DIFFRACTION8H1 - 216

+
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