[English] 日本語
Yorodumi
- PDB-8zur: Crystal structure of the F99S/M153T/V163A/T203V/E222Q variant of ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8zur
TitleCrystal structure of the F99S/M153T/V163A/T203V/E222Q variant of GFP at pH 5.0
ComponentsGreen fluorescent protein
KeywordsFLUORESCENT PROTEIN / GREEN FLUORESCENT PROTEIN
Function / homologyGreen fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / bioluminescence / generation of precursor metabolites and energy / Green fluorescent protein
Function and homology information
Biological speciesAequorea victoria (jellyfish)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.2 Å
AuthorsTakeda, R. / Takeda, K.
Funding support Japan, 2items
OrganizationGrant numberCountry
Takeda Science Foundation Japan
Gimpu fund from Kyoto University Japan
CitationJournal: Sci Rep / Year: 2024
Title: Structural characterization of green fluorescent protein in the I-state.
Authors: Takeda, R. / Tsutsumi, E. / Okatsu, K. / Fukai, S. / Takeda, K.
History
DepositionJun 10, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 6, 2024Provider: repository / Type: Initial release
Revision 1.1Jun 18, 2025Group: Database references / Category: pdbx_related_exp_data_set

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Green fluorescent protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9123
Polymers25,8411
Non-polymers712
Water7,314406
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area140 Å2
ΔGint-9 kcal/mol
Surface area10200 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.500, 57.790, 68.670
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab

-
Components

#1: Protein Green fluorescent protein


Mass: 25841.000 Da / Num. of mol.: 1 / Mutation: F99S,M153T,V163A,T203V,E222Q
Source method: isolated from a genetically manipulated source
Details: Q80R was caused by a PCR error in the early study (Chalfie, M. et al., Science, 1994)
Source: (gene. exp.) Aequorea victoria (jellyfish) / Gene: GFP / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P42212
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 406 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.98 Å3/Da / Density % sol: 37.79 %
Crystal growTemperature: 308 K / Method: vapor diffusion, sitting drop
Details: PEG 4000, magnesium chloride, MES-NaOH buffer (pH 5.0)

-
Data collection

DiffractionMean temperature: 15 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.7 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 15, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.7 Å / Relative weight: 1
ReflectionResolution: 1.2→44.22 Å / Num. obs: 64730 / % possible obs: 100 % / Redundancy: 6.71 % / Biso Wilson estimate: 11.34 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.087 / Rrim(I) all: 0.094 / Net I/σ(I): 10.78
Reflection shellResolution: 1.2→1.27 Å / Redundancy: 6.42 % / Rmerge(I) obs: 0.798 / Mean I/σ(I) obs: 1.99 / Num. unique obs: 9968 / CC1/2: 0.77 / Rrim(I) all: 0.869 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
XSCALEdata scaling
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.2→41.2 Å / SU ML: 0.1057 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 15.2979
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1662 3226 4.98 %
Rwork0.1287 61494 -
obs0.1305 64720 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 16.18 Å2
Refinement stepCycle: LAST / Resolution: 1.2→41.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1816 0 2 406 2224
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01412106
X-RAY DIFFRACTIONf_angle_d1.3432895
X-RAY DIFFRACTIONf_chiral_restr0.1139317
X-RAY DIFFRACTIONf_plane_restr0.0121386
X-RAY DIFFRACTIONf_dihedral_angle_d13.3337829
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.2-1.220.25711370.20412614X-RAY DIFFRACTION99.96
1.22-1.240.22211350.19752621X-RAY DIFFRACTION99.96
1.24-1.260.19271380.18082663X-RAY DIFFRACTION99.96
1.26-1.280.21981360.17012642X-RAY DIFFRACTION99.93
1.28-1.30.22331300.16592642X-RAY DIFFRACTION100
1.3-1.330.22551370.16392650X-RAY DIFFRACTION100
1.33-1.350.19041420.15652649X-RAY DIFFRACTION99.96
1.35-1.380.19351530.15952658X-RAY DIFFRACTION100
1.38-1.420.20311380.14142608X-RAY DIFFRACTION100
1.42-1.450.19061390.13142655X-RAY DIFFRACTION100
1.45-1.490.17571460.11832656X-RAY DIFFRACTION100
1.49-1.530.16041400.11152652X-RAY DIFFRACTION100
1.53-1.580.15131450.11432651X-RAY DIFFRACTION99.96
1.58-1.640.17041520.10962669X-RAY DIFFRACTION100
1.64-1.710.13911310.11312672X-RAY DIFFRACTION100
1.71-1.780.15291570.11742651X-RAY DIFFRACTION100
1.78-1.880.1541450.11262672X-RAY DIFFRACTION99.96
1.88-20.11861230.1062709X-RAY DIFFRACTION100
2-2.150.15161110.10982734X-RAY DIFFRACTION100
2.15-2.370.15941650.12312670X-RAY DIFFRACTION100
2.37-2.710.18971220.12842732X-RAY DIFFRACTION100
2.71-3.410.1481520.12782754X-RAY DIFFRACTION100
3.41-41.20.16441520.13442870X-RAY DIFFRACTION99.83

+
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