[English] 日本語
Yorodumi
- PDB-8wp6: Crystal structure of a TetR family regulator AmvR from Acinetobac... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8wp6
TitleCrystal structure of a TetR family regulator AmvR from Acinetobacter baumannii (APO FORM)
ComponentsTetR family transcriptional regulator
KeywordsTRANSCRIPTION / TetR family regulator / effector-binding domain
Function / homology: / Tetracyclin repressor-like, C-terminal domain superfamily / Bacterial regulatory proteins, tetR family / DNA-binding HTH domain, TetR-type / TetR-type HTH domain profile. / Homeobox-like domain superfamily / transcription cis-regulatory region binding / DNA-binding transcription factor activity / TetR family transcriptional regulator
Function and homology information
Biological speciesAcinetobacter baumannii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.87 Å
AuthorsMa, J.M. / Ge, H.H. / Wang, N.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32071215 China
CitationJournal: To Be Published
Title: Crystal Structure of Acinetobacter baumannii LysR family regulator AceR effector binding domain (apo)
Authors: Ma, J.M. / Ge, H.H.
History
DepositionOct 9, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 16, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: TetR family transcriptional regulator


Theoretical massNumber of molelcules
Total (without water)22,1461
Polymers22,1461
Non-polymers00
Water1,72996
1
A: TetR family transcriptional regulator

A: TetR family transcriptional regulator


Theoretical massNumber of molelcules
Total (without water)44,2932
Polymers44,2932
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-x+1,-y+1,z1
Buried area2470 Å2
ΔGint-16 kcal/mol
Surface area18610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)64.154, 69.596, 50.771
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

-
Components

#1: Protein TetR family transcriptional regulator


Mass: 22146.275 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acinetobacter baumannii (bacteria) / Gene: ABCAM1_2317 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0D5YGI2
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 96 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.56 Å3/Da / Density % sol: 51.93 %
Crystal growTemperature: 289 K / Method: evaporation / Details: 0.2 M Ammonium fluoride, 20% w/v PEG 3350

-
Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.987 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Sep 11, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 1.87→50.77 Å / Num. obs: 18445 / % possible obs: 94.6 % / Redundancy: 9.3 % / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.025 / Rrim(I) all: 0.08 / Net I/σ(I): 16.1
Reflection shellResolution: 1.87→1.97 Å / Rmerge(I) obs: 0.596 / Mean I/σ(I) obs: 2.7 / Num. unique obs: 1921 / Rpim(I) all: 0.237 / Rrim(I) all: 0.645

-
Processing

Software
NameVersionClassification
PHENIX(1.19.2_4158: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.87→50.77 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 25.3 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2285 876 4.76 %
Rwork0.1998 --
obs0.2012 18409 94.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.87→50.77 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1495 0 0 96 1591
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0041518
X-RAY DIFFRACTIONf_angle_d0.7362045
X-RAY DIFFRACTIONf_dihedral_angle_d4.313199
X-RAY DIFFRACTIONf_chiral_restr0.041230
X-RAY DIFFRACTIONf_plane_restr0.004265
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.87-1.980.27431090.25422146X-RAY DIFFRACTION71
1.98-2.130.23721440.22372924X-RAY DIFFRACTION95
2.14-2.350.26291630.20313020X-RAY DIFFRACTION99
2.35-2.690.2531410.21743093X-RAY DIFFRACTION99
2.69-3.390.21791740.22323084X-RAY DIFFRACTION100
3.39-50.770.21671450.17793266X-RAY DIFFRACTION100
Refinement TLS params.Method: refined / Origin x: 18.7767 Å / Origin y: 27.2906 Å / Origin z: 11.441 Å
111213212223313233
T0.2336 Å2-0.0205 Å2-0.0123 Å2-0.2965 Å20.0416 Å2--0.2646 Å2
L0.8957 °21.0469 °2-0.9246 °2-1.353 °2-1.127 °2--1.1487 °2
S0.0098 Å °0.0866 Å °0.0881 Å °-0.0006 Å °0.1399 Å °0.1995 Å °0.0217 Å °-0.2864 Å °-0.0028 Å °
Refinement TLS groupSelection details: all

+
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