[English] 日本語
Yorodumi
- PDB-2v0v: Crystal Structure of Rev-Erb beta -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2v0v
TitleCrystal Structure of Rev-Erb beta
ComponentsORPHAN NUCLEAR RECEPTOR NR1D2
KeywordsTRANSCRIPTION / ZINC / RECEPTOR / REPRESSOR / ZINC-FINGER / DNA-BINDING / CONSTITUTIVE REPRESSION / TRANSCRIPTION REGULATION / ORPHAN RECEPTOR / A-HELICAL SANDWICH / METAL-BINDING / NUCLEAR PROTEIN
Function / homology
Function and homology information


regulation of skeletal muscle cell differentiation / circadian behavior / lipid homeostasis / regulation of lipid metabolic process / energy homeostasis / hormone-mediated signaling pathway / regulation of circadian rhythm / negative regulation of inflammatory response / DNA-binding transcription repressor activity, RNA polymerase II-specific / Nuclear Receptor transcription pathway ...regulation of skeletal muscle cell differentiation / circadian behavior / lipid homeostasis / regulation of lipid metabolic process / energy homeostasis / hormone-mediated signaling pathway / regulation of circadian rhythm / negative regulation of inflammatory response / DNA-binding transcription repressor activity, RNA polymerase II-specific / Nuclear Receptor transcription pathway / nuclear receptor activity / sequence-specific double-stranded DNA binding / regulation of inflammatory response / cell differentiation / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / chromatin / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily ...Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Nuclear receptor subfamily 1 group D member 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.4 Å
AuthorsWoo, E.-J. / Jeong, D.G. / Lim, M.-Y. / Jun Kim, S. / Eon Ryu, S.
CitationJournal: J.Mol.Biol. / Year: 2007
Title: Structural Insight Into the Constitutive Repression Function of the Nuclear Receptor Rev-Erbbeta
Authors: Woo, E.-J. / Jeong, D.G. / Lim, M.-Y. / Jun Kim, S. / Kim, K.-J. / Yoon, S.-M. / Park, B.-C. / Eon Ryu, S.
History
DepositionMay 19, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 23, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 24, 2018Group: Data collection / Refinement description / Source and taxonomy
Category: entity_src_gen / software
Item: _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name ..._entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _software.name
Revision 1.4May 22, 2019Group: Data collection / Refinement description / Category: refine / Item: _refine.pdbx_ls_cross_valid_method

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: ORPHAN NUCLEAR RECEPTOR NR1D2
B: ORPHAN NUCLEAR RECEPTOR NR1D2
C: ORPHAN NUCLEAR RECEPTOR NR1D2
D: ORPHAN NUCLEAR RECEPTOR NR1D2


Theoretical massNumber of molelcules
Total (without water)87,7774
Polymers87,7774
Non-polymers00
Water1,72996
1
A: ORPHAN NUCLEAR RECEPTOR NR1D2


Theoretical massNumber of molelcules
Total (without water)21,9441
Polymers21,9441
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: ORPHAN NUCLEAR RECEPTOR NR1D2


Theoretical massNumber of molelcules
Total (without water)21,9441
Polymers21,9441
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: ORPHAN NUCLEAR RECEPTOR NR1D2


Theoretical massNumber of molelcules
Total (without water)21,9441
Polymers21,9441
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: ORPHAN NUCLEAR RECEPTOR NR1D2


Theoretical massNumber of molelcules
Total (without water)21,9441
Polymers21,9441
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)102.456, 102.456, 143.964
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number80
Space group name H-MI41
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.99868, -0.04858, 0.01665), (-0.04847, 0.9988, 0.00699), (-0.01697, 0.00617, -0.99984)-1.30339, 0.91793, 18.78336
2given(-0.08449, 0.99569, 0.03837), (0.99641, 0.08425, 0.00776), (0.00449, 0.03889, -0.99923)-3.50674, 51.04293, -17.22289
3given(0.06159, 0.9957, 0.0692), (-0.99801, 0.06048, 0.01809), (0.01383, -0.07017, 0.99744)-47.98832, -6.59137, 38.27809

-
Components

#1: Protein
ORPHAN NUCLEAR RECEPTOR NR1D2 / EAR-1R / ORPHAN NUCLEAR HORMONE RECEPTOR BD73 / REV-ERB BETA


Mass: 21944.166 Da / Num. of mol.: 4 / Fragment: LIGAND-BINDING DOMAIN, RESIDUES 386-579
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET28 / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / References: UniProt: Q14995
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 96 / 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 Å3/Da / Density % sol: 39 % / Description: NONE
Crystal growpH: 7.5 / Details: PEG 4000 18%, ISOPROPANOL 10%, 100 MM HEPES PH 7.5

-
Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Date: Apr 25, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→30 Å / Num. obs: 29048 / % possible obs: 99.4 % / Redundancy: 5 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 17.6
Reflection shellResolution: 2.4→2.49 Å / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 4.7 / % possible all: 99.1

-
Processing

Software
NameClassification
SHELXL-97refinement
HKL-2000data reduction
HKL-2000data scaling
SHELXDEphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 2.4→99 Å / Num. parameters: 23276 / Num. restraintsaints: 23794 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
RfactorNum. reflection% reflectionSelection details
Rfree0.2195 1357 5 %RANDOM
all0.1376 27157 --
obs0.1765 -93.6 %-
Refine analyzeNum. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 5818
Refinement stepCycle: LAST / Resolution: 2.4→99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5714 0 0 96 5810
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.005
X-RAY DIFFRACTIONs_angle_d0.021
X-RAY DIFFRACTIONs_similar_dist0
X-RAY DIFFRACTIONs_from_restr_planes0.0229
X-RAY DIFFRACTIONs_zero_chiral_vol0.023
X-RAY DIFFRACTIONs_non_zero_chiral_vol0.031
X-RAY DIFFRACTIONs_anti_bump_dis_restr0.023
X-RAY DIFFRACTIONs_rigid_bond_adp_cmpnt0
X-RAY DIFFRACTIONs_similar_adp_cmpnt0.112
X-RAY DIFFRACTIONs_approx_iso_adps0

+
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