[English] 日本語
Yorodumi
- PDB-6plj: A nucleotidyl transferase from Methanothermobacter thermautotropt... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6plj
TitleA nucleotidyl transferase from Methanothermobacter thermautotroptrophicus (Mth528)
Componentsnucleotidyl transferase
KeywordsTRANSFERASE / Cell wall synthesis / pseudomurein / Methanothermobacter
Function / homologyMobA-like NTP transferase / MobA-like NTP transferase domain / nucleotidyltransferase activity / Nucleotide-diphospho-sugar transferases / MobA-like NTP transferase domain-containing protein
Function and homology information
Biological speciesMethanothermobacter thermautotrophicus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.59 Å
AuthorsCarbone, V. / Schofield, L. / Sutherland-Smith, A. / Ronimus, R.
Funding support New Zealand, 1items
OrganizationGrant numberCountry
Royal Society of New ZealandAGR1301 New Zealand
CitationJournal: To Be Published
Title: A nucleotidyl transferase from Methanothermobacter thermautotroptrophicus (Mth528)
Authors: Carbone, V. / Schofield, L. / Sutherland-Smith, A. / Ronimus, R.
History
DepositionJul 1, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 8, 2020Provider: repository / Type: Initial release
Revision 1.1Oct 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: nucleotidyl transferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,06110
Polymers25,6211
Non-polymers4409
Water4,360242
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: PISA analysis suggests monomer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)50.656, 61.418, 72.227
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein nucleotidyl transferase


Mass: 25621.256 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (archaea)
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H
Gene: MTH_528 / Production host: Escherichia coli (E. coli) / References: UniProt: O26628
#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 242 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.4 Å3/Da / Density % sol: 43.9 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 2.0 M Ammonium sulfate, 0.1 M Bis-Tris, 0.1 M Potassium sodium tartrate tetrahydrate

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Sep 21, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.59→46.79 Å / Num. obs: 30884 / % possible obs: 99.8 % / Redundancy: 14.5 % / CC1/2: 0.999 / Rmerge(I) obs: 0.09 / Net I/σ(I): 21.7 / Num. measured all: 446457 / Scaling rejects: 1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Net I/σ(I) obs% possible all
1.59-1.6213.50.871966414580.9083.696.1
8.72-46.7911.20.04126352360.99953.999.9

-
Phasing

PhasingMethod: molecular replacement
Phasing MRR rigid body: 0.564
Highest resolutionLowest resolution
Rotation46.79 Å1.77 Å

-
Processing

Software
NameVersionClassification
XDSdata reduction
Aimless0.5.21data scaling
Auto-Rickshawphasing
REFMAC5.8.0135refinement
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1hv9

1hv9


Resolution: 1.59→46.79 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.95 / SU B: 1.467 / SU ML: 0.052 / SU R Cruickshank DPI: 0.0831 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.083 / ESU R Free: 0.084
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2024 1535 5 %RANDOM
Rwork0.1712 ---
obs0.1727 29293 99.81 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 50.13 Å2 / Biso mean: 16.827 Å2 / Biso min: 8.37 Å2
Baniso -1Baniso -2Baniso -3
1-1.07 Å20 Å20 Å2
2---0.46 Å20 Å2
3----0.6 Å2
Refinement stepCycle: final / Resolution: 1.59→46.79 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1606 0 28 243 1877
Biso mean--28.57 29.06 -
Num. residues----216
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0191724
X-RAY DIFFRACTIONr_bond_other_d0.0020.021703
X-RAY DIFFRACTIONr_angle_refined_deg1.3771.9862341
X-RAY DIFFRACTIONr_angle_other_deg0.91333899
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4885233
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.4032370
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.60615282
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.2421518
X-RAY DIFFRACTIONr_chiral_restr0.0730.2270
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0212001
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02375
LS refinement shellResolution: 1.592→1.633 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.285 120 -
Rwork0.264 2081 -
all-2201 -
obs--97.35 %

+
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