[English] 日本語
Yorodumi
- PDB-2vpk: Crystal structure of the BTB domain of human myoneurin -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2vpk
TitleCrystal structure of the BTB domain of human myoneurin
ComponentsMYONEURIN
KeywordsTRANSCRIPTION / TRANSCRIPTION REGULATION / METAL-BINDING / ALTERNATIVE SPLICING / ZINC / NUCLEUS / BTB DOMAIN / ZINC-FINGER / DNA-BINDING
Function / homology
Function and homology information


cellular response to leukemia inhibitory factor / DNA binding / nucleoplasm / metal ion binding
Similarity search - Function
Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / BTB/POZ domain / BTB domain profile. / Zinc finger, C2H2 type / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily ...Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / BTB/POZ domain / BTB domain profile. / Zinc finger, C2H2 type / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / zinc finger / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / SKP1/BTB/POZ domain superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsCooper, C.D.O. / Murray, J.W. / Bullock, A. / Pike, A.C.W. / von Delft, F. / Filippakopoulos, P. / Salah, E. / Edwards, A. / Arrowsmith, C.H. / Bountra, C. ...Cooper, C.D.O. / Murray, J.W. / Bullock, A. / Pike, A.C.W. / von Delft, F. / Filippakopoulos, P. / Salah, E. / Edwards, A. / Arrowsmith, C.H. / Bountra, C. / Weigelt, J. / Knapp, S.
CitationJournal: To be Published
Title: Crystal Structure of the Btb Domain of Human Myoneurin
Authors: Cooper, C.D.O. / Murray, J.W. / Bullock, A. / Pike, A.C.W. / von Delft, F. / Filippakopoulos, P. / Salah, E. / Edwards, A. / Arrowsmith, C.H. / Bountra, C. / Weigelt, J. / Knapp, S.
History
DepositionFeb 29, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 11, 2008Provider: repository / Type: Initial release
Revision 1.1Dec 5, 2012Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary / Version format compliance
Revision 1.2Jan 24, 2018Group: Database references / Category: citation_author / Item: _citation_author.name
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: MYONEURIN


Theoretical massNumber of molelcules
Total (without water)13,4571
Polymers13,4571
Non-polymers00
Water91951
1
A: MYONEURIN

A: MYONEURIN


Theoretical massNumber of molelcules
Total (without water)26,9142
Polymers26,9142
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z+1/31
Buried area3140 Å2
ΔGint-19 kcal/mol
Surface area14040 Å2
MethodPQS
Unit cell
Length a, b, c (Å)55.688, 55.688, 126.201
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11A-2011-

HOH

-
Components

#1: Protein MYONEURIN / BTB DOMAIN OF MYONEURIN / ZINC FINGER / BTB DOMAIN-CONTAINING PROTEIN 31


Mass: 13457.242 Da / Num. of mol.: 1 / Fragment: BTB DOMAIN, RESIDUES 4-117
Source method: isolated from a genetically manipulated source
Details: INTERMOLECULAR DISULFIDE LINK BETWEEN SYMMETRY RELATED CYS6.
Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: NEUROMUSCULAR SYSTEM / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-RARE2 / References: UniProt: Q9NPC7
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 51 / 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: 1.88 Å3/Da / Density % sol: 41.39 % / Description: NONE
Crystal growpH: 6.5
Details: 0.2 M NA/KPO4, 0.1 M BIS-TRIS PROPANE PH 6.5, 20% PEG 3350.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9828
DetectorType: ADSC CCD / Detector: CCD / Date: Jan 17, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9828 Å / Relative weight: 1
ReflectionResolution: 1.9→48 Å / Num. obs: 9485 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Redundancy: 4.33 % / Biso Wilson estimate: 24.33 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 0
Reflection shellResolution: 1.9→2 Å / Redundancy: 4.06 % / Rmerge(I) obs: 1.1 / Mean I/σ(I) obs: 1.4 / % possible all: 98.6

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2IF5
Resolution: 2→38.317 Å / SU ML: 0.29 / σ(F): 0.05 / Phase error: 24.62 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2584 529 6.8 %
Rwork0.1938 --
obs0.1981 7785 92.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.17 Å2 / ksol: 0.4 e/Å3
Displacement parametersBiso mean: 33.57 Å2
Baniso -1Baniso -2Baniso -3
1-5.4584 Å20 Å20 Å2
2--5.4584 Å20 Å2
3----10.9169 Å2
Refinement stepCycle: LAST / Resolution: 2→38.317 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms928 0 0 51 979
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0081842
X-RAY DIFFRACTIONf_angle_d0.9043306
X-RAY DIFFRACTIONf_dihedral_angle_d16.372449
X-RAY DIFFRACTIONf_chiral_restr0.07140
X-RAY DIFFRACTIONf_plane_restr0.004289
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.20130.31561190.2411696X-RAY DIFFRACTION90
2.2013-2.51970.26821280.19881759X-RAY DIFFRACTION92
2.5197-3.17440.26461450.171822X-RAY DIFFRACTION95
3.1744-38.32450.23811370.19121979X-RAY DIFFRACTION94
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.453-0.1877-0.23120.4960.28341.2535-0.09640.2917-0.3101-0.02020.24350.4044-0.0892-0.63560.02330.1769-0.0157-0.0280.25770.00750.2335.855118.093824.2669
20.4038-0.6805-0.08761.4670.60091.2501-0.04980.01910.108-0.10370.06270.0302-0.02920.13580.05840.0770.0371-0.01150.14240.02490.138916.114229.739212.1646
30.8211-0.1124-0.35351.26550.48761.09590.08550.1357-0.0365-0.2722-0.0449-0.1316-0.1475-0.42410.01970.2070.0448-0.00540.24480.02110.150212.351726.04554.1687
40.70660.22740.05081.0980.0513-0.1835-0.10550.4876-0.2214-0.7340.08810.3194-0.12010.0604-0.04240.22730.0534-0.04020.2299-0.04890.197113.216816.2582-1.0666
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 2:13)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 14:57)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 58:88)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 89:116)

+
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://pdbjlvh1.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