[English] 日本語
Yorodumi
- PDB-1xdx: Solution Structure of the Tctex1 Light Chain From Chlamydomonas I... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1xdx
TitleSolution Structure of the Tctex1 Light Chain From Chlamydomonas Inner Dynein Arm I1
ComponentsTctex1 Light Chain protein
KeywordsCONTRACTILE PROTEIN / Chlamydomonas flagella / Tctex1 dimer / NMR solution structure
Function / homology
Function and homology information


cytoplasmic dynein complex / dynein intermediate chain binding / microtubule-based movement / identical protein binding / cytoplasm
Similarity search - Function
Tctex-1 / Dynein light chain Tctex-1 like / Tctex-1-like superfamily / Tctex-1 family / Ribosomal protein S3 C-terminal domain / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Dynein light chain Tctex1
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
MethodSOLUTION NMR / torsion angle dynamics simulated annealing
AuthorsWu, H. / Maciejewski, M.W. / Takebe, S. / King, S.M.
CitationJournal: Structure / Year: 2005
Title: Solution Structure of the Tctex1 Dimer Reveals a Mechanism for Dynein-Cargo Interactions
Authors: Wu, H. / Maciejewski, M.W. / Takebe, S. / King, S.M.
History
DepositionSep 8, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 1, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tctex1 Light Chain protein
B: Tctex1 Light Chain protein


Theoretical massNumber of molelcules
Total (without water)25,3612
Polymers25,3612
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 90target function,structures with the least restraint violations
RepresentativeModel #1fewest violations

-
Components

#1: Protein Tctex1 Light Chain protein


Mass: 12680.427 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydomonas reinhardtii (plant) / Description: flagella Inner Dynein Arm I1 / Gene: AF039437 / Plasmid: pET23d / Production host: Escherichia coli (E. coli) / Strain (production host): BL-21 cells / References: UniProt: O64980

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
2223D 13C-separated NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

-
Sample preparation

Details
Solution-IDContentsSolvent system
1~0.7 mM tctex1 protein; U-15N,13C; 20 mM Na phosphate; pH 6.7; 100mM NaCl; 20mM DTT; 90% H2O, 10% D2O90% H2O/10% D2O
2~0.7 mM tctex1 protein; U-15N,13C; 20 mM Na phosphate; pH 6.7; 100mM NaCl; 20mM DTT; >99% D2O>99% D2O
Sample conditionspH: 6.7 / Pressure: ambient / Temperature: 298 K

-
NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA6002

-
Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1Bvariancollection
NMRPipe1.1Delaglio, F.processing
XEASY1.4Bartels, C.data analysis
CYANA1.1Guentert, P.structure solution
X-PLOR3.851Brungerrefinement
RefinementMethod: torsion angle dynamics simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function,structures with the least restraint violations
Conformers calculated total number: 90 / Conformers submitted total number: 15

+
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