[English] 日本語
Yorodumi
- PDB-3k81: Structure of the central interaction protein from the Trypanosoma... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3k81
TitleStructure of the central interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies
Components
  • MP18 RNA editing complex protein
  • Single strand antibody VHH domain
KeywordsImmune System / RNA Binding Protein / KREPA6 / VHH / Single domain antibody
Function / homology
Function and homology information


RNA modification / mitochondrial mRNA editing complex / kinetoplast / single-stranded DNA binding / endonuclease activity / RNA binding / nucleus
Similarity search - Function
RNA editing complex, subunit MP18 / Single-strand binding protein family / Primosome PriB/single-strand DNA-binding / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Nucleic acid-binding, OB-fold / Immunoglobulins / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
MP18 RNA editing complex protein
Similarity search - Component
Biological speciesTrypanosoma brucei (eukaryote)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsPark, Y.-J. / Hol, W.
CitationJournal: J.Struct.Biol. / Year: 2011
Title: Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.
Authors: Wu, M. / Park, Y.J. / Pardon, E. / Turley, S. / Hayhurst, A. / Deng, J. / Steyaert, J. / Hol, W.G.
History
DepositionOct 13, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 17, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 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
Revision 1.3Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
C: MP18 RNA editing complex protein
D: MP18 RNA editing complex protein
A: Single strand antibody VHH domain
B: Single strand antibody VHH domain


Theoretical massNumber of molelcules
Total (without water)64,1624
Polymers64,1624
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)80.030, 68.605, 93.335
Angle α, β, γ (deg.)90.00, 102.23, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein MP18 RNA editing complex protein


Mass: 18113.566 Da / Num. of mol.: 2 / Fragment: KREPA6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei (eukaryote) / Gene: KREPA6, Tb10.70.2090 / Plasmid: pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 / References: UniProt: Q38B90
#2: Antibody Single strand antibody VHH domain


Mass: 13967.477 Da / Num. of mol.: 2 / Fragment: single domain antibody VHH
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Plasmid: pRSF / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.95 Å3/Da / Density % sol: 36.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.2
Details: 15% PEG3350, 0.1M Citrate pH.4.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.9795 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Apr 1, 2009
Details: Flat collimating mirror, double crystal monochromator, toroid focusing mirror
RadiationMonochromator: Double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 3.4→50 Å / Num. obs: 6402 / % possible obs: 92.3 % / Observed criterion σ(I): 3 / Redundancy: 3.3 % / Biso Wilson estimate: 64.9 Å2 / Rmerge(I) obs: 0.112 / Rsym value: 0.112 / Net I/σ(I): 8.6
Reflection shellResolution: 3.4→3.52 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 2 / Num. unique all: 423 / Rsym value: 0.338 / % possible all: 61.2

-
Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3K7U
Resolution: 3.4→33.467 Å / SU ML: 0.73 / σ(F): 1.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3198 301 4.73 %
Rwork0.2668 --
obs0.2693 6363 91.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 114.052 Å2 / ksol: 0.346 e/Å3
Refinement stepCycle: LAST / Resolution: 3.4→33.467 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3250 0 0 0 3250
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0023312
X-RAY DIFFRACTIONf_angle_d0.5444507
X-RAY DIFFRACTIONf_dihedral_angle_d13.0251110
X-RAY DIFFRACTIONf_chiral_restr0.038521
X-RAY DIFFRACTIONf_plane_restr0.002592
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.4001-4.28230.33871360.27472739X-RAY DIFFRACTION84
4.2823-33.46890.31061650.26273323X-RAY DIFFRACTION100
Refinement TLS params.Method: refined / Origin x: 24.3208 Å / Origin y: 11.4461 Å / Origin z: -23.0129 Å
111213212223313233
T0.2762 Å20.0303 Å20.0143 Å2-0.0517 Å2-0.0428 Å2--0.1592 Å2
L1.1267 °2-0.5763 °2-0.0968 °2-0.6707 °2-1.2693 °2--1.9416 °2
S0.0604 Å °-0.143 Å °-0.1315 Å °-0.3351 Å °-0.0853 Å °0.0896 Å °0.0288 Å °0.1355 Å °-0.0547 Å °
Refinement TLS groupSelection details: all

+
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