[English] 日本語
Yorodumi
- PDB-3eik: double stranded DNA binding protein -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3eik
Titledouble stranded DNA binding protein
ComponentsTATA-box-binding protein
KeywordsTRANSCRIPTION / TATA box binding protein / DNA-binding / Initiation factor / Nucleus
Function / homology
Function and homology information


RNA polymerase II general transcription initiation factor activity / DNA-templated transcription initiation / DNA binding / identical protein binding / nucleus
Similarity search - Function
TATA-Binding Protein / TATA-box binding protein, eukaryotic / TATA-Binding Protein / TATA-box binding protein / TATA-box binding protein, conserved site / Transcription factor TFIID (or TATA-binding protein, TBP) / Transcription factor TFIID repeat signature. / TBP domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
TRANSCRIPTION INITIATION FACTOR TFIID (TFIID-1)
Similarity search - Component
Biological speciesEncephalitozoon cuniculi (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsCui, S. / Wollmann, P. / Moldt, M. / Hopfner, K.-P.
CitationJournal: To be Published
Title: structural studies of ecTBP
Authors: Cui, S. / Wollmann, P. / Moldt, M. / Hopfner, K.-P.
History
DepositionSep 16, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 22, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 30, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: TATA-box-binding protein
B: TATA-box-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,3778
Polymers49,0052
Non-polymers3726
Water2,666148
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4510 Å2
ΔGint4.7 kcal/mol
Surface area17740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.400, 104.400, 129.060
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number146
Space group name H-MH3

-
Components

#1: Protein TATA-box-binding protein


Mass: 24502.486 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Encephalitozoon cuniculi (fungus) / Strain: GB-M1 / Plasmid: pET-28a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q8ST28
#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H6O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 148 / 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: 2.76 Å3/Da / Density % sol: 55.47 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.1M MES,2M NaCl,4% Acetone, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jun 18, 2008
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→30 Å / Num. all: 41388 / Num. obs: 37329 / % possible obs: 90.19 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.03 % / Biso Wilson estimate: 25.23 Å2 / Rmerge(I) obs: 0.047 / Rsym value: 0.047
Reflection shellResolution: 1.9→2.01 Å / Redundancy: 2.99 % / Rmerge(I) obs: 0.326 / Mean I/σ(I) obs: 3.44 / Num. unique all: 5640 / Rsym value: 0.326 / % possible all: 84.8

-
Processing

Software
NameVersionClassificationNB
PHENIXrefinement
PDB_EXTRACT3.006data extraction
remdaq.pilatusdata collection
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1YTB
Resolution: 1.9→26.1 Å / Occupancy max: 1 / Occupancy min: 0 / FOM work R set: 0.851 / SU ML: 0.31 / σ(F): 1.98 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.235 1950 5.01 %RANDOM
Rwork0.177 ---
obs0.18 36954 94.04 %-
all-38913 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 54.278 Å2 / ksol: 0.38 e/Å3
Displacement parametersBiso max: 68.87 Å2 / Biso mean: 30.794 Å2 / Biso min: 13.2 Å2
Baniso -1Baniso -2Baniso -3
1-0.204 Å20 Å2-0 Å2
2--0.204 Å2-0 Å2
3----0.407 Å2
Refinement stepCycle: LAST / Resolution: 1.9→26.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2908 0 24 148 3080
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072990
X-RAY DIFFRACTIONf_angle_d1.0294032
X-RAY DIFFRACTIONf_chiral_restr0.071459
X-RAY DIFFRACTIONf_plane_restr0.005510
X-RAY DIFFRACTIONf_dihedral_angle_d16.0411124
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9-1.9460.2841280.1882628275693
1.946-1.9990.2791430.1672697284097
1.999-2.0580.2221520.1512703285596
2.058-2.1240.2611430.1542652279594
2.124-2.20.2691250.162636276195
2.2-2.2880.2611730.1632685285896
2.288-2.3920.2711370.1692709284696
2.392-2.5180.2621470.1742630277795
2.518-2.6760.2541530.1732603275693
2.676-2.8820.2361380.1822661279995
2.882-3.1710.2481380.1882640277893
3.171-3.6290.2061230.1752583270692
3.629-4.5690.1921290.1542599272892
4.569-26.1030.1811210.1632537265890

+
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