[English] 日本語
Yorodumi
- PDB-8p2n: Polymeric form of the BTB domain of ZBTB8A from Xenopus laevis -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8p2n
TitlePolymeric form of the BTB domain of ZBTB8A from Xenopus laevis
ComponentsZinc finger and BTB domain-containing protein 8A.1-A
KeywordsTRANSCRIPTION / Transcription regulation / BTB domain / polymerisation
Function / homology
Function and homology information


DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / nucleus / 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
Zinc finger and BTB domain-containing protein 8A.1-A
Similarity search - Component
Biological speciesXenopus laevis (African clawed frog)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsCoste, F. / Mance, L. / Suskiewicz, M.J.
Funding support France, 1items
OrganizationGrant numberCountry
Centre National de la Recherche Scientifique (CNRS) France
CitationJournal: To Be Published
Title: Polymeric form of the BTB domain of ZBTB8A from Xenopus laevis
Authors: Coste, F. / Mance, L. / Suskiewicz, M.J.
History
DepositionMay 16, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 5, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Zinc finger and BTB domain-containing protein 8A.1-A
B: Zinc finger and BTB domain-containing protein 8A.1-A


Theoretical massNumber of molelcules
Total (without water)35,1802
Polymers35,1802
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: homology
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2870 Å2
ΔGint-22 kcal/mol
Surface area11920 Å2
Unit cell
Length a, b, c (Å)153.695, 153.695, 153.695
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number213
Space group name H-MP4132
Space group name HallP4bd2ab3
Symmetry operation#1: x,y,z
#2: x+1/4,-z+1/4,y+3/4
#3: x+3/4,z+1/4,-y+1/4
#4: z+3/4,y+1/4,-x+1/4
#5: -z+1/4,y+3/4,x+1/4
#6: -y+1/4,x+3/4,z+1/4
#7: y+1/4,-x+1/4,z+3/4
#8: z,x,y
#9: y,z,x
#10: -y+1/2,-z,x+1/2
#11: z+1/2,-x+1/2,-y
#12: -y,z+1/2,-x+1/2
#13: -z+1/2,-x,y+1/2
#14: -z,x+1/2,-y+1/2
#15: y+1/2,-z+1/2,-x
#16: x+1/2,-y+1/2,-z
#17: -x,y+1/2,-z+1/2
#18: -x+1/2,-y,z+1/2
#19: y+3/4,x+1/4,-z+1/4
#20: -y+3/4,-x+3/4,-z+3/4
#21: z+1/4,-y+1/4,x+3/4
#22: -z+3/4,-y+3/4,-x+3/4
#23: -x+1/4,z+3/4,y+1/4
#24: -x+3/4,-z+3/4,-y+3/4
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 7 through 73 or (resid 74...
d_2ens_1(chain "B" and (resid 7 through 75 or (resid 76...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg label comp-IDEnd label comp-IDLabel asym-IDLabel seq-ID
d_11ens_1HISGLUA5 - 124
d_21ens_1HISGLUB3 - 122

NCS oper: (Code: givenMatrix: (-0.986145738629, 0.0216188880639, -0.164466427769), (-0.0173813997273, -0.999479951708, -0.0271608740227), (-0.164968085179, -0.0239259234522, 0.986008661757)Vector: ...NCS oper: (Code: given
Matrix: (-0.986145738629, 0.0216188880639, -0.164466427769), (-0.0173813997273, -0.999479951708, -0.0271608740227), (-0.164968085179, -0.0239259234522, 0.986008661757)
Vector: 169.598158941, 113.849004863, 15.4858466565)

-
Components

#1: Protein Zinc finger and BTB domain-containing protein 8A.1-A


Mass: 17589.959 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Xenopus laevis (African clawed frog) / Gene: zbtb8a.1-a, zbtb8, zbtb8.1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q0IH98

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 4.3 Å3/Da / Density % sol: 71.4 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.2 / Details: PEG200, Na/K phosphate, NaCl

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97856 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 15, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 3.1→48.6 Å / Num. obs: 11832 / % possible obs: 100 % / Redundancy: 65.3 % / Biso Wilson estimate: 130.5 Å2 / CC1/2: 0.999 / Rpim(I) all: 0.029 / Net I/σ(I): 16
Reflection shellResolution: 3.1→3.31 Å / Redundancy: 66.3 % / Mean I/σ(I) obs: 1.2 / Num. unique obs: 2074 / CC1/2: 0.63 / Rpim(I) all: 0.751 / % possible all: 100

-
Processing

Software
NameVersionClassification
MxCuBEdata collection
XDSdata reduction
Aimlessdata scaling
PHASERphasing
Cootmodel building
PHENIXv1.20refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.1→48.6 Å / SU ML: 0.5952 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 30.4293
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2635 1125 9.55 %
Rwork0.2378 10655 -
obs0.2401 11780 99.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 122.18 Å2
Refinement stepCycle: LAST / Resolution: 3.1→48.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1815 0 0 0 1815
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00171850
X-RAY DIFFRACTIONf_angle_d0.37432508
X-RAY DIFFRACTIONf_chiral_restr0.036298
X-RAY DIFFRACTIONf_plane_restr0.0025319
X-RAY DIFFRACTIONf_dihedral_angle_d11.6866619
Refine LS restraints NCSType: Torsion NCS / Rms dev position: 0.446202024908 Å
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1-3.240.53041370.47281293X-RAY DIFFRACTION99.31
3.24-3.410.33971420.34771279X-RAY DIFFRACTION99.93
3.41-3.630.32981510.29591296X-RAY DIFFRACTION99.93
3.63-3.910.37411240.30471319X-RAY DIFFRACTION100
3.91-4.30.29381360.23411317X-RAY DIFFRACTION100
4.3-4.920.23071470.2131331X-RAY DIFFRACTION100
4.92-6.190.27911470.23951348X-RAY DIFFRACTION100
6.2-48.60.2031410.20081472X-RAY DIFFRACTION99.63
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)
12.612386486160.5558924188870.9824157397590.2439985823210.5529198207090.945832656443-0.097211085886-0.294025176581-0.8397011518950.531301332027-0.1411335908290.2878452878880.907809579978-0.446432710417-0.0002388911328951.13750275486-0.06141119902270.06380890862930.71312788526-0.008951533929231.3047877122770.691821301152.2226575254101.70718122
22.37512419501-0.356911467476-0.217716705622.43645896863-0.9501693448430.9295824945420.0861298677566-0.753691961570.6546454851480.620742267947-0.3923008564410.5173253696680.106697197128-0.353823453935-0.0004861645327881.004652763190.04857270779880.05730628050280.825106612605-0.07109344166151.2893270129467.875460173862.4610880373106.733116004
31.37360990469-0.8351559034671.097301198030.45529035203-0.5367999846270.8091545939580.4310600877610.1469334052-0.240561149580.241158577131-0.3295428245340.1477746515570.37086974823-0.3788388054162.00863457053E-51.162498560440.189797364412-0.2016375263870.868542543891-0.02192899163741.1953447380960.910002246168.02227309491.2288176736
40.475514256517-0.116931694883-0.1767832479480.2063046908570.1451281301190.0997853023512-0.4551351812230.5857795795481.16310221962-0.150415843763-1.13901101262-0.388198315356-1.332148710690.790822996079-0.005498521788941.30357674777-0.122910492564-0.03793882524181.12158006290.01085407182341.4552642610781.821404263460.360583603598.6955764045
50.297136807621-0.02783746828930.4171574264580.09319966196170.1154436601930.7803462398520.118755949408-1.60507119799-0.8360361978750.0410997498949-0.2774071847561.39439605625-0.2255459698880.0537619868033-0.001836370102061.316587627940.0935985025161-0.06812657463411.08058545688-0.05607667715851.2132098992188.626395192253.9832093408111.65797011
61.43183620595-0.572602279691-0.4399239071610.314406520972-0.1364194377081.328279054740.0664669474309-0.0598988271211-0.15396296698-0.245733221008-0.047108552419-0.3033310353040.396987557510.2401269274244.94431982047E-51.017854303010.00439035347597-0.01591960235550.763349639360.1528564838941.1597103841282.871221803246.5446371271108.127425936
70.126863466417-0.08789141435450.3213832311280.773655377620.5170885857991.69424174824-0.501368820697-0.811079039177-0.2634353807221.35994570468-0.174943736021-0.4959868696590.4657030331660.16565103503-0.0007957894466981.360955914380.115511055062-0.03773937006260.9563774429930.09843409145131.2043294333486.970402620646.5617072616113.361997259
80.253500364403-0.148156351301-0.2218146633960.0694583644970.1299329857660.178926482121-0.6995283382640.2186204637521.046771900220.006156877731440.643500048027-0.781025494565-0.9486290297380.509113022475-0.001774124391821.249941219310.1174516398980.02715306099960.7351610314360.08281944431651.1410713604392.993342146450.9214969797.852295328
9-0.00848199355481-0.0139167875481-0.03140584858260.1231605646640.2012932399940.294061547650.6887765090630.0949799540840.1155250461591.071721708720.3963901773140.884878208214-1.794758332590.7696139976410.007850202140141.01913475541-0.01547396989230.1774762160261.124801716490.2600734482261.1248541905898.070773551441.267940589597.9179054768
100.304664864148-0.2274834710950.3523558079264.293794087121.012295865580.7921126922410.3130768902560.3630371901440.504256527596-0.471524573536-0.407230440604-0.970436518124-0.06078003382150.0547314375488-0.1837570223661.526987741440.4770068759270.2514897267570.7015795550940.1125648182351.1214911618892.195399077340.658387977192.5542964006
111.027254310011.169077031341.727054736331.464472364491.972850883142.91389197476-0.433440688920.03458503917940.103497614256-1.107308416911.05360468345-0.838478154829-1.417772285351.27627127713-0.136264487580.887209819750.3174256290160.4479233639721.620725235720.3302772915611.39130813814107.22441685535.300403708786.2102006055
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 3 through 32 )AA3 - 321 - 30
22chain 'A' and (resid 33 through 83 )AA33 - 8331 - 81
33chain 'A' and (resid 84 through 126 )AA84 - 12682 - 124
44chain 'B' and (resid 5 through 20 )BB5 - 201 - 16
55chain 'B' and (resid 21 through 32 )BB21 - 3217 - 28
66chain 'B' and (resid 33 through 57 )BB33 - 5729 - 53
77chain 'B' and (resid 58 through 72 )BB58 - 7254 - 68
88chain 'B' and (resid 73 through 91 )BB73 - 9169 - 87
99chain 'B' and (resid 92 through 104 )BB92 - 10488 - 100
1010chain 'B' and (resid 105 through 119 )BB105 - 119101 - 115
1111chain 'B' and (resid 120 through 126 )BB120 - 126116 - 122

+
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