[English] 日本語
Yorodumi
- PDB-6ml4: BTB24 Zinc Fingers 4-8 with 19+1mer DNA Oligonucleotide (Sequence 3) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6ml4
TitleBTB24 Zinc Fingers 4-8 with 19+1mer DNA Oligonucleotide (Sequence 3)
Components
  • DNA (5'-D(*AP*CP*GP*CP*AP*GP*GP*TP*CP*CP*TP*GP*GP*AP*CP*GP*AP*AP*GP*C)-3')
  • DNA (5'-D(*TP*GP*CP*TP*TP*CP*GP*TP*CP*CP*AP*GP*GP*AP*CP*CP*TP*GP*CP*G)-3')
  • Zinc finger and BTB domain-containing protein 24
KeywordsTRANSCRIPTION/DNA / protein-DNA complex / transcription / TRANSCRIPTION-DNA complex
Function / homology
Function and homology information


regulation of immune system process / hematopoietic progenitor cell differentiation / regulation of cytokine production / DNA-binding transcription repressor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / nucleoplasm / metal ion binding
Similarity search - Function
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
Similarity search - Domain/homology
DNA / DNA (> 10) / Zinc finger and BTB domain-containing protein 24
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.482 Å
AuthorsHorton, J.R. / Cheng, X. / Ren, R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM049245-23 United States
CitationJournal: Nucleic Acids Res. / Year: 2019
Title: Structural basis of specific DNA binding by the transcription factor ZBTB24.
Authors: Ren, R. / Hardikar, S. / Horton, J.R. / Lu, Y. / Zeng, Y. / Singh, A.K. / Lin, K. / Coletta, L.D. / Shen, J. / Lin Kong, C.S. / Hashimoto, H. / Zhang, X. / Chen, T. / Cheng, X.
History
DepositionSep 26, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 3, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 11, 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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Zinc finger and BTB domain-containing protein 24
E: DNA (5'-D(*AP*CP*GP*CP*AP*GP*GP*TP*CP*CP*TP*GP*GP*AP*CP*GP*AP*AP*GP*C)-3')
F: DNA (5'-D(*TP*GP*CP*TP*TP*CP*GP*TP*CP*CP*AP*GP*GP*AP*CP*CP*TP*GP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,05811
Polymers29,5453
Non-polymers5138
Water6,359353
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6110 Å2
ΔGint-38 kcal/mol
Surface area14550 Å2
MethodPISA
Unit cell
Length a, b, c (Å)46.277, 68.807, 48.434
Angle α, β, γ (deg.)90.00, 92.40, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

-
Protein , 1 types, 1 molecules A

#1: Protein Zinc finger and BTB domain-containing protein 24 / Bone morphogenetic protein-induced factor 1 / Brain-specific protein 1 / Zinc finger protein 450


Mass: 17274.033 Da / Num. of mol.: 1 / Fragment: zinc fingers 4-8 (UNP residues 375-519)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Zbtb24, Bif1, Bsg1, Znf450 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q80X44

-
DNA chain , 2 types, 2 molecules EF

#2: DNA chain DNA (5'-D(*AP*CP*GP*CP*AP*GP*GP*TP*CP*CP*TP*GP*GP*AP*CP*GP*AP*AP*GP*C)-3')


Mass: 6168.994 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse)
#3: DNA chain DNA (5'-D(*TP*GP*CP*TP*TP*CP*GP*TP*CP*CP*AP*GP*GP*AP*CP*CP*TP*GP*CP*G)-3')


Mass: 6101.928 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse)

-
Non-polymers , 3 types, 361 molecules

#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 353 / 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: 2.61 Å3/Da / Density % sol: 52.83 %
Crystal growTemperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 25% PEG3350, 0.1 M HEPES, pH 7.5, 0.2 M ammonium acetate

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-003 / Wavelength: 1.5418 Å
DetectorType: RIGAKU / Detector: PIXEL / Date: Jul 24, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.48→28.04 Å / Num. obs: 40443 / % possible obs: 80.4 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.04 / Rpim(I) all: 0.019 / Net I/σ(I): 16.7
Reflection shellResolution: 1.48→1.54 Å / Redundancy: 1.1 % / Mean I/σ(I) obs: 1.5 / Num. unique obs: 570 / CC1/2: 0.53 / Rpim(I) all: 0.53 / % possible all: 11.3

-
Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
CrysalisProdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 6ML3
Resolution: 1.482→28.039 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.98
RfactorNum. reflection% reflection
Rfree0.2113 1981 4.91 %
Rwork0.1907 --
obs0.1917 40368 80.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.482→28.039 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1131 814 17 353 2315
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0032106
X-RAY DIFFRACTIONf_angle_d0.5322996
X-RAY DIFFRACTIONf_dihedral_angle_d24.423845
X-RAY DIFFRACTIONf_chiral_restr0.045321
X-RAY DIFFRACTIONf_plane_restr0.003243
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.4824-1.51940.3499150.3781267X-RAY DIFFRACTION8
1.5194-1.56050.4428350.316819X-RAY DIFFRACTION24
1.5605-1.60640.2881800.27211382X-RAY DIFFRACTION41
1.6064-1.65830.27281070.25832078X-RAY DIFFRACTION61
1.6583-1.71750.2391720.24653031X-RAY DIFFRACTION90
1.7175-1.78630.26891670.2433404X-RAY DIFFRACTION100
1.7863-1.86760.25641810.22643420X-RAY DIFFRACTION100
1.8676-1.9660.25441710.21823375X-RAY DIFFRACTION100
1.966-2.08910.23631830.20773424X-RAY DIFFRACTION100
2.0891-2.25040.19421750.20463409X-RAY DIFFRACTION100
2.2504-2.47670.2091800.19533413X-RAY DIFFRACTION100
2.4767-2.83480.19061730.19183430X-RAY DIFFRACTION100
2.8348-3.57040.19911650.17633439X-RAY DIFFRACTION99
3.5704-28.04450.17891770.14333496X-RAY DIFFRACTION100
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)
19.9331-1.01095.52244.2879-3.38397.81070.11230.13270.1656-0.1725-0.3022-0.15160.4215-0.05870.23180.24420.06680.05780.2309-0.07060.218636.197435.812328.8499
28.2635-1.8280.47719.09842.5795.87930.02010.3039-0.0119-0.4801-0.0887-0.60170.59880.4890.07140.3240.09090.09850.20640.0140.2140.691633.174522.3183
34.7326-2.2687-2.87177.32272.15124.83960.11160.14760.4894-0.41350.1254-0.2129-0.65970.0188-0.20290.1373-0.03110.02270.16680.02280.194941.550924.89057.9771
40.5387-1.018-0.87454.78423.80243.03-0.15840.1478-0.2326-0.0350.0991-0.13850.3261-0.12720.00650.1297-0.02320.04970.2077-0.01910.108938.728715.0537.3696
56.7950.5959-0.73864.98990.80722.12320.0147-0.081-0.24590.18350.076-0.03910.05720.0893-0.08510.12390.0241-0.01920.07490.00970.063625.5782.5387.1451
62.8266-0.0659-0.51063.604-3.04582.7604-0.0285-0.1753-0.00030.17560.10780.1425-0.1567-0.0741-0.08790.0956-0.0020.01010.1048-0.02250.0788.774416.53557.9213
75.8289-1.06171.66524.8558-1.7378.5005-0.12490.4045-0.0961-0.56660.12110.1810.29840.07070.05430.1568-0.0534-0.01350.1117-0.01710.139312.978627.1905-11.0536
83.6492-1.47983.96790.6359-1.28757.6243-0.03090.30780.0627-0.38430.10650.1933-0.09610.2745-0.03230.2296-0.0601-0.06240.16480.01470.15496.34318.5954-10.5388
96.8393-5.05066.34126.1435-3.48736.4441-0.0134-0.0377-0.4073-0.1530.18730.3693-0.2067-0.0716-0.20980.15480.0030.0050.085-0.00420.076617.754110.64031.1344
103.57820.08311.75932.131-0.12755.98460.0511-0.5748-0.03360.26590.175-0.1045-0.0123-0.4178-0.16860.136-0.0123-0.00860.1779-0.02430.103633.332217.024519.7061
114.23280.7872.86792.43861.04525.3260.0019-0.3713-0.02990.31270.1202-0.1857-0.12730.0028-0.11030.16210.0114-0.0190.1922-0.02240.097636.200616.46122.8661
124.82910.81473.80296.88941.5833.1186-0.07880.13220.1047-0.49990.2481-0.1313-1.1191-0.346-0.21120.2323-0.00970.00120.15670.03480.114121.312319.41982.8824
135.5308-0.95443.65636.9047-0.14767.296-0.42151.0737-1.8474-0.55390.83840.16860.24710.1431-0.49420.2688-0.0512-0.05160.2351-0.07080.29999.410410.3677-8.8258
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 374 through 388 )
2X-RAY DIFFRACTION2chain 'A' and (resid 389 through 399 )
3X-RAY DIFFRACTION3chain 'A' and (resid 400 through 416 )
4X-RAY DIFFRACTION4chain 'A' and (resid 417 through 428 )
5X-RAY DIFFRACTION5chain 'A' and (resid 429 through 456 )
6X-RAY DIFFRACTION6chain 'A' and (resid 457 through 489 )
7X-RAY DIFFRACTION7chain 'A' and (resid 490 through 514 )
8X-RAY DIFFRACTION8chain 'E' and (resid 1 through 5 )
9X-RAY DIFFRACTION9chain 'E' and (resid 6 through 10 )
10X-RAY DIFFRACTION10chain 'E' and (resid 11 through 20 )
11X-RAY DIFFRACTION11chain 'F' and (resid 1 through 10 )
12X-RAY DIFFRACTION12chain 'F' and (resid 11 through 15 )
13X-RAY DIFFRACTION13chain 'F' and (resid 16 through 20 )

+
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