[English] 日本語
Yorodumi
- PDB-7cwj: Root induced Secreted protein Tsp1 from Biocontrol fungi Trichode... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7cwj
TitleRoot induced Secreted protein Tsp1 from Biocontrol fungi Trichoderma virens
ComponentsRoot induced effector protein Tsp1
KeywordsSIGNALING PROTEIN / Effector / ellicitor / bio-control agent
Function / homologyeffector-mediated perturbation of host innate immune response by symbiont / extracellular region / Effector TSP1
Function and homology information
Biological speciesHypocrea virens (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.61 Å
AuthorsGupta, G.D.
CitationJournal: Int.J.Biol.Macromol. / Year: 2021
Title: Structure-function analysis reveals Trichoderma virens Tsp1 to be a novel fungal effector protein modulating plant defence.
Authors: Gupta, G.D. / Bansal, R. / Mistry, H. / Pandey, B. / Mukherjee, P.K.
History
DepositionAug 28, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 1, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 6, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Root induced effector protein Tsp1
B: Root induced effector protein Tsp1
C: Root induced effector protein Tsp1
D: Root induced effector protein Tsp1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,7618
Polymers59,3924
Non-polymers3684
Water11,277626
1
A: Root induced effector protein Tsp1
hetero molecules

B: Root induced effector protein Tsp1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9725
Polymers29,6962
Non-polymers2763
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_545x,y-1,z1
Buried area4130 Å2
ΔGint-31 kcal/mol
Surface area11380 Å2
MethodPISA
2
C: Root induced effector protein Tsp1
D: Root induced effector protein Tsp1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7883
Polymers29,6962
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3750 Å2
ΔGint-30 kcal/mol
Surface area11220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.658, 67.478, 170.050
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein
Root induced effector protein Tsp1


Mass: 14848.104 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hypocrea virens (strain Gv29-8 / FGSC 10586) (fungus)
Strain: Gv29-8 / FGSC 10586 / Gene: TRIVIDRAFT_215947 / Production host: Escherichia coli (E. coli) / Variant (production host): Rosetta (DE3) / References: UniProt: G9MQD3
#2: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 626 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.32 Å3/Da / Density % sol: 47 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 1.9 M sodium malonate pH 6.5, 5% glycerol

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: RRCAT INDUS-2 / Beamline: PX-BL21 / Wavelength: 0.9788 Å
DetectorType: RAYONIX MX340-HS / Detector: CCD / Date: Oct 13, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9788 Å / Relative weight: 1
ReflectionResolution: 1.6→44.1 Å / Num. obs: 67496 / % possible obs: 96.2 % / Redundancy: 12.1 % / Biso Wilson estimate: 17.55 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.067 / Rpim(I) all: 0.019 / Rrim(I) all: 0.07 / Net I/σ(I): 27.5 / Num. measured all: 818842 / Scaling rejects: 4
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
1.6-1.636.80.4163.525100.8570.1690.45173.2
8.77-44.110.70.0425230.9990.0130.04499.6

-
Phasing

PhasingMethod: SAD

-
Processing

Software
NameVersionClassification
PHENIX1.10.1-2155refinement
XDSdata reduction
Aimless0.5.21data scaling
RESOLVEphasing
PDB_EXTRACT3.25data extraction
AutoSolphasing
RefinementMethod to determine structure: SAD / Resolution: 1.61→23.952 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 19.5 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.1995 3377 5.07 %
Rwork0.1507 63252 -
obs0.1532 66629 96.5 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 80.42 Å2 / Biso mean: 23.802 Å2 / Biso min: 10.17 Å2
Refinement stepCycle: final / Resolution: 1.61→23.952 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3832 0 56 626 4514
Biso mean--35.33 31.98 -
Num. residues----515
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.014007
X-RAY DIFFRACTIONf_angle_d1.0885517
X-RAY DIFFRACTIONf_chiral_restr0.066633
X-RAY DIFFRACTIONf_plane_restr0.007700
X-RAY DIFFRACTIONf_dihedral_angle_d8.5842360
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.61-1.6330.26921040.167206376
1.633-1.65740.25521160.1644210580
1.6574-1.68330.25551270.1653226884
1.6833-1.71090.25031280.164235088
1.7109-1.74040.23551300.1625251393
1.7404-1.7720.24551540.1566260296
1.772-1.80610.24661500.1575266199
1.8061-1.84290.22221510.15762687100
1.8429-1.8830.2241590.15442672100
1.883-1.92680.24991460.15262728100
1.9268-1.97490.22091440.14052698100
1.9749-2.02830.19781210.14522725100
2.0283-2.08790.20161370.14232736100
2.0879-2.15530.19221190.14222745100
2.1553-2.23230.20751340.14572703100
2.2323-2.32160.20631490.14392744100
2.3216-2.42710.1791510.14592726100
2.4271-2.5550.20811590.15692725100
2.555-2.71480.20571260.16852772100
2.7148-2.92410.23281570.16412726100
2.9241-3.21770.16911430.15852779100
3.2177-3.68190.18521420.13652789100
3.6819-4.63330.14891590.12622813100
4.6333-23.950.19721710.1688292299

+
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