[English] 日本語
Yorodumi
- PDB-5dbo: Crystal structure of the tetrameric eIF2B-beta2-delta2 complex fr... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5dbo
TitleCrystal structure of the tetrameric eIF2B-beta2-delta2 complex from C. thermophilum
Components
  • Translation initiation factor eIF2b-like protein,Translation initiation factor eIF2b-like protein
  • Translation initiation factor eif-2b-like protein
KeywordsTRANSLATION / Translation initiation / translational regulation / eIF2B / exchange factor / eIF2 / complex
Function / homology
Function and homology information


translation initiation factor activity
Similarity search - Function
Translation initiation factor eif-2b; domain 2 / Initiation factor 2B-related / Initiation factor 2B-like, C-terminal / Initiation factor 2 subunit family / NagB/RpiA transferase-like / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Translation initiation factor eif-2b-like protein / Translation initiation factor eIF2b-like protein
Similarity search - Component
Biological speciesChaetomium thermophilum (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å
AuthorsKuhle, B. / Ficner, R.
CitationJournal: Nucleic Acids Res. / Year: 2015
Title: Architecture of the eIF2B regulatory subcomplex and its implications for the regulation of guanine nucleotide exchange on eIF2.
Authors: Kuhle, B. / Eulig, N.K. / Ficner, R.
History
DepositionAug 21, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Oct 7, 2015Provider: repository / Type: Initial release
Revision 1.1Nov 25, 2015Group: Database references
Revision 1.2Jan 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: Translation initiation factor eif-2b-like protein
B: Translation initiation factor eIF2b-like protein,Translation initiation factor eIF2b-like protein
C: Translation initiation factor eif-2b-like protein
D: Translation initiation factor eIF2b-like protein,Translation initiation factor eIF2b-like protein


Theoretical massNumber of molelcules
Total (without water)190,1834
Polymers190,1834
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8510 Å2
ΔGint-40 kcal/mol
Surface area50830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.430, 109.430, 219.060
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

-
Components

#1: Protein Translation initiation factor eif-2b-like protein


Mass: 49742.598 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum (fungus) / Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: CTHT_0028980 / Plasmid: pGEX-6P1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 / References: UniProt: G0S811
#2: Protein Translation initiation factor eIF2b-like protein,Translation initiation factor eIF2b-like protein


Mass: 45348.828 Da / Num. of mol.: 2 / Fragment: UNP residues 1-92,UNP residues 118-388
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum (fungus) / Gene: CTHT_0063470 / Plasmid: pGEX-6P1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 / References: UniProt: G0SEE6

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.99 Å3/Da / Density % sol: 38.22 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6
Details: MES (pH 6.0), pentaerythritol propoxylate (5/4 PO/OH), NaCl

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.85506 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jul 14, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.85506 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 31063 / % possible obs: 99.6 % / Redundancy: 8.21 % / Rsym value: 0.107 / Net I/σ(I): 14.73
Reflection shellResolution: 3→3.18 Å / Mean I/σ(I) obs: 2.8 / Num. unique all: 4881 / CC1/2: 0.841 / Rsym value: 0.69 / % possible all: 98.3

-
Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation7.63 Å48.95 Å
Translation7.63 Å48.95 Å

-
Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
PHASER2.5.7phasing
PDB_EXTRACT3.15data extraction
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4ZEM and 4ZEO
Resolution: 3→48.948 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 26.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2546 1554 5 %
Rwork0.2082 --
obs0.2105 31060 99.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3→48.948 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9377 0 0 0 9377
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0079564
X-RAY DIFFRACTIONf_angle_d1.31612970
X-RAY DIFFRACTIONf_dihedral_angle_d14.2573538
X-RAY DIFFRACTIONf_chiral_restr0.0531506
X-RAY DIFFRACTIONf_plane_restr0.0071688
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0002-3.0970.35211360.31342579X-RAY DIFFRACTION97
3.097-3.20770.32631390.29242644X-RAY DIFFRACTION100
3.2077-3.33610.28421390.25952627X-RAY DIFFRACTION100
3.3361-3.48790.27641400.24912668X-RAY DIFFRACTION100
3.4879-3.67170.28451400.23132657X-RAY DIFFRACTION100
3.6717-3.90160.2791400.22092659X-RAY DIFFRACTION100
3.9016-4.20270.25971410.20282672X-RAY DIFFRACTION100
4.2027-4.62540.22241410.17532682X-RAY DIFFRACTION100
4.6254-5.2940.19951420.17622702X-RAY DIFFRACTION100
5.294-6.66720.27831440.21082736X-RAY DIFFRACTION100
6.6672-48.9540.23811520.18362880X-RAY DIFFRACTION100
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)
12.37622.30590.62075.04952.24130.9058-0.1371-0.1389-0.67590.79030.2249-0.77820.27330.6638-0.08140.6188-0.0607-0.11880.61670.02341.319842.2395-22.9009-14.5994
24.98520.1616-0.07753.7003-0.93013.8513-0.41480.6413-0.4896-0.96130.4292-0.6834-0.19440.1602-0.06160.6593-0.25170.15610.5338-0.10810.714730.273-27.3796-28.7194
34.52421.08510.11636.3136-1.33734.6160.1993-0.4179-0.7391-0.0841-0.0197-0.10850.4691-0.0607-0.20770.5807-0.1627-0.08850.428-0.00260.679221.7839-36.6115-22.1169
41.88522.4183-0.51854.04630.30951.90160.0666-0.04020.0046-0.3680.01770.684-0.0010.0121-0.0440.4737-0.1369-0.04590.52270.01890.514217.3518-6.501-33.9093
52.95910.11980.25133.55220.60732.1674-0.1510.5044-0.2877-0.64370.2568-0.3454-0.17550.3036-0.15830.5226-0.24880.03760.7099-0.01320.494528.05051.7435-33.1546
62.57750.6831.10691.7774-0.26321.73760.11040.0744-0.39140.2281-0.1141-0.18380.1187-0.0514-0.02980.4851-0.0952-0.02530.4543-0.01960.395824.849-8.4738-17.5472
74.46430.07932.12782.95960.9364.6419-0.26071.2844-0.0579-0.6620.4026-0.64460.3470.4867-0.18590.7557-0.21980.09270.99570.03340.752156.160232.2566-26.4899
82.07722.2009-1.30194.9063-3.60652.43730.3020.28760.4830.90280.1756-0.0712-0.485-0.1748-0.14320.7148-0.17670.07110.6576-0.06281.104252.163833.7991-12.9229
93.3178-0.07040.90574.3817-0.71022.29410.05760.2072-0.0595-0.0916-0.1063-0.105-0.10410.17430.08480.4825-0.2195-0.02140.6081-0.02370.467441.8189.7799-12.0953
108.18973.73561.6295.50691.3012.85341.3316-0.2653.27691.6755-0.85420.7172-1.4932-0.3595-0.31320.9935-0.0090.34350.7332-0.01510.955138.43225.9436-5.9999
110.3736-0.9839-0.40132.98480.82160.04970.1811-0.48020.0160.6358-0.2672-0.12740.04640.31340.15930.9588-0.3632-0.2140.80740.05780.701942.286419.5425.8275
125.19015.63622.44327.97743.08321.72420.9321-0.4768-0.05980.6845-0.5518-0.69710.5550.0624-0.29240.9542-0.3782-0.13850.74750.02331.191451.7931.210124.23
135.16821.90950.44871.498-0.57610.92810.2223-0.0111.12850.1756-0.11760.2062-0.41310.1501-0.09871.0481-0.28450.00550.6056-0.06310.617837.07238.257819.259
143.1639-0.6962-1.00952.521.26041.9650.0352-0.0510.0460.21870.1165-0.1393-0.20760.1239-0.18570.718-0.1389-0.06510.40310.01410.353521.389516.890815.9664
150.47020.28050.29670.15660.18890.28210.0077-0.6749-0.64370.63592.1051-0.918-0.2117-0.69880.20681.8244-0.14940.50181.41520.10721.543310.3512-31.528329.2436
161.01251.01551.29043.55831.69591.7456-0.5866-1.3028-0.99470.5398-0.288-0.2762-0.0792-0.73210.48932.1208-0.68141.45011.1628-0.05150.7416.0294-21.175427.4379
172.1785-2.2559-0.36378.59770.84318.2044-0.3201-0.177-0.96711.23490.39971.66280.1424-0.26770.08751.1045-0.33740.1620.79250.01631.0618-1.4529-28.63518.9489
183.89653.87433.7024.85695.05845.61140.19021.23560.07550.83750.17861.4129-0.2358-0.5690.3681.5131-0.33390.27780.65520.00611.7232-0.129-26.52479.9665
191.99960.488-1.56623.3662-0.32362.2518-0.2197-0.0063-0.55920.31950.09290.03790.4175-0.00240.0030.6535-0.1147-0.06580.42950.06960.54123.3378-13.966410.2697
202.55190.4374-0.60363.3569-0.32034.7970.3285-0.5522-0.63090.3553-0.84891.9555-0.1295-0.78480.14510.694-0.19970.24270.651-0.08021.146910.8893-7.50217.8257
213.0992-1.4353-0.6891.1816-0.21296.2123-0.71090.6077-0.3369-2.37991.17293.6430.5808-0.8492-0.45950.903-0.2408-0.24420.77960.07841.328412.5338-14.4197-0.9227
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 127 through 156 )
2X-RAY DIFFRACTION2chain 'A' and (resid 157 through 190 )
3X-RAY DIFFRACTION3chain 'A' and (resid 191 through 264 )
4X-RAY DIFFRACTION4chain 'A' and (resid 265 through 304 )
5X-RAY DIFFRACTION5chain 'A' and (resid 305 through 353 )
6X-RAY DIFFRACTION6chain 'A' and (resid 354 through 443 )
7X-RAY DIFFRACTION7chain 'B' and (resid 10 through 82 )
8X-RAY DIFFRACTION8chain 'B' and (resid 83 through 214 )
9X-RAY DIFFRACTION9chain 'B' and (resid 215 through 382 )
10X-RAY DIFFRACTION10chain 'B' and (resid 383 through 406 )
11X-RAY DIFFRACTION11chain 'C' and (resid 127 through 191 )
12X-RAY DIFFRACTION12chain 'C' and (resid 192 through 223 )
13X-RAY DIFFRACTION13chain 'C' and (resid 224 through 279 )
14X-RAY DIFFRACTION14chain 'C' and (resid 280 through 441 )
15X-RAY DIFFRACTION15chain 'D' and (resid 10 through 23 )
16X-RAY DIFFRACTION16chain 'D' and (resid 24 through 41 )
17X-RAY DIFFRACTION17chain 'D' and (resid 42 through 82 )
18X-RAY DIFFRACTION18chain 'D' and (resid 83 through 181 )
19X-RAY DIFFRACTION19chain 'D' and (resid 182 through 322 )
20X-RAY DIFFRACTION20chain 'D' and (resid 323 through 378 )
21X-RAY DIFFRACTION21chain 'D' and (resid 379 through 406 )

+
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