[English] 日本語
Yorodumi
- PDB-1e7j: HMG-D complexed to a bulge DNA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1e7j
TitleHMG-D complexed to a bulge DNA
Components
  • DNA (5'-D(*CP*GP*AP*TP*AP*TP*TP*AP*AP*GP*AP*GP*CP*C)-3')
  • DNA (5'-D(*GP*GP*CP*TP*CP*AP*AP*TP*AP*TP*CP*G)-3')
  • HIGH MOBILITY GROUP PROTEIN DHigh-mobility group
KeywordsPROTEIN/DNA / PROTEIN-DNA COMPLEX
Function / homology
Function and homology information


DNA binding, bending / minor groove of adenine-thymine-rich DNA binding / chromatin organization / transcription cis-regulatory region binding / chromatin / DNA binding / nucleus
Similarity search - Function
High mobility group box domain / DNA Binding (I), subunit A / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA / DNA (> 10) / High mobility group protein D
Similarity search - Component
Biological speciesDROSOPHILA MELANOGASTER (fruit fly)
MethodSOLUTION NMR / SIMULATED ANNEALING, MINIMIZATION
AuthorsCerdan, R. / Payet, D. / Yang, J.-C. / Travers, A.A. / Neuhaus, D.
Citation
Journal: Protein Sci. / Year: 2001
Title: Hmg-D Complexed to a Bulge DNA: An NMR Model
Authors: Cerdan, R. / Payet, D. / Yang, J.-C. / Travers, A.A. / Neuhaus, D.
#1: Journal: Structure / Year: 1994
Title: The Solution Structure and Dynamics of the DNA-Binding Domain of Hmg-D from Drosophila Melanogaster
Authors: Jones, D.N.M. / Searles, M.A. / Shaw, G.L. / Churchill, M.E.A. / Ner, S.S. / Keeler, J. / Travers, A.A. / Neuhaus, D.
History
DepositionAug 29, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 5, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HIGH MOBILITY GROUP PROTEIN D
B: DNA (5'-D(*CP*GP*AP*TP*AP*TP*TP*AP*AP*GP*AP*GP*CP*C)-3')
C: DNA (5'-D(*GP*GP*CP*TP*CP*AP*AP*TP*AP*TP*CP*G)-3')


Theoretical massNumber of molelcules
Total (without water)16,4533
Polymers16,4533
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)10 / 50LOW VALUES OF THE NOE ENERGY TERM AND PROTEIN LOCATED WITHIN MINOR GROOVE OF DNA
RepresentativeModel #1

-
Components

#1: Protein HIGH MOBILITY GROUP PROTEIN D / High-mobility group / HMG-D


Mass: 8501.711 Da / Num. of mol.: 1 / Fragment: HMG-D DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Plasmid: PET13A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q05783
#2: DNA chain DNA (5'-D(*CP*GP*AP*TP*AP*TP*TP*AP*AP*GP*AP*GP*CP*C)-3')


Mass: 4288.817 Da / Num. of mol.: 1 / Source method: obtained synthetically
#3: DNA chain DNA (5'-D(*GP*GP*CP*TP*CP*AP*AP*TP*AP*TP*CP*G)-3')


Mass: 3662.404 Da / Num. of mol.: 1 / Source method: obtained synthetically

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131COSY
14115N-HSQC
1513D CBCA(CO)NH
1613D 15N NOESY-HSQC
1713D 13C NOESY-HSQC
1813D (H)CCH-TOCSY

-
Sample preparation

Sample conditionsIonic strength: LOW / pH: 6.0 / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX5001
Bruker DMXBrukerDMX6002
Bruker AvanceBrukerAvance8003

-
Processing

NMR software
NameVersionDeveloperClassification
X-PLOR 3.851, CHARMM24BRUNGER, MACKERELLrefinement
XPLOR3.851structure solution
CHARMM24structure solution
RefinementMethod: SIMULATED ANNEALING, MINIMIZATION / Software ordinal: 1 / Details: REFINEMENT DETAILS WILL BE FOUND IN THE PAPER
NMR ensembleConformer selection criteria: LOW VALUES OF THE NOE ENERGY TERM AND PROTEIN LOCATED WITHIN MINOR GROOVE OF DNA
Conformers calculated total number: 50 / Conformers submitted total number: 10

+
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