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- PDB-1b9c: Green Fluorescent Protein Mutant F99S, M153T and V163A -

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Basic information

Entry
Database: PDB / ID: 1b9c
TitleGreen Fluorescent Protein Mutant F99S, M153T and V163A
ComponentsPROTEIN (GREEN FLUORESCENT PROTEIN)
KeywordsLUMINESCENT PROTEIN / FLUORESCENT PROTEIN / CHROMOPHORE / GREEN FLUORESCENT PROTEIN / LUMINESCENCE / F99S M153T V163A MUTANT
Function / homology
Function and homology information


bioluminescence / generation of precursor metabolites and energy
Similarity search - Function
Green Fluorescent Protein / Green fluorescent protein / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Green fluorescent protein
Similarity search - Component
Biological speciesAequorea victoria (jellyfish)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsBattistutta, R. / Negro, A. / Zanotti, G.
Citation
Journal: Proteins / Year: 2000
Title: Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein.
Authors: Battistutta, R. / Negro, A. / Zanotti, G.
#1: Journal: Nat.Biotechnol. / Year: 1996
Title: The Molecular Structure of Green Fluorescent Protein
Authors: Yang, F. / Moss, L.G. / Phillips Jr., G.N.
#2: Journal: Science / Year: 1996
Title: Crystal Structure of the Aequorea Victoria Green Fluorescent Protein
Authors: Ormo, M. / Cubitt, A.B. / Kallio, K. / Gross, L.A. / Tsien, R.Y. / Remington, S.J.
History
DepositionFeb 9, 1999Deposition site: PDBE / Processing site: RCSB
Revision 1.0Nov 17, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 14, 2018Group: Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.details
Revision 1.4Aug 9, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.5Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.6Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (GREEN FLUORESCENT PROTEIN)
B: PROTEIN (GREEN FLUORESCENT PROTEIN)
C: PROTEIN (GREEN FLUORESCENT PROTEIN)
D: PROTEIN (GREEN FLUORESCENT PROTEIN)


Theoretical massNumber of molelcules
Total (without water)106,9524
Polymers106,9524
Non-polymers00
Water5,152286
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)83.480, 85.370, 140.060
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.756601, -0.042557, -0.65249), (-0.039778, -0.993036, 0.110893), (-0.652665, 0.109857, 0.74964)57.2579, 62.8255, 17.5084
2given(-0.98742, -0.014388, -0.157461), (0.009254, -0.999403, 0.033287), (-0.157846, 0.031411, 0.986964)27.3828, -0.238, 2.28

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Components

#1: Protein
PROTEIN (GREEN FLUORESCENT PROTEIN)


Mass: 26737.959 Da / Num. of mol.: 4 / Mutation: F99S, M153T, V163A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aequorea victoria (jellyfish) / Description: THE N-TERMINAL HIS-TAG HAS BEEN REMOVED / Plasmid: PRSETB (INVITROGEN) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P42212
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 286 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsTHE FLUOROPHORE IS FORMED BY SER 65, TYR 66 AND GLY 67. THE CARBONYL CARBON OF TYR 66 IS BONDED TO ...THE FLUOROPHORE IS FORMED BY SER 65, TYR 66 AND GLY 67. THE CARBONYL CARBON OF TYR 66 IS BONDED TO THE NITROGEN OF GLY 67. THE CARBONYL OXYGEN IS DELETED. THE SIDE CHAIN OF TYR 66 IS DEHYDROGENATED.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 2.3 Å3/Da / Density % sol: 50 %
Crystal growpH: 8.3
Details: 22% PEG 4000, 50 MM HEPES PH 8.5, 50 MM MGCL2, 10 MM 2-MERCAPTOETHANOL, 23% MG/ ML PROTEINA, pH 8.3
Crystal grow
*PLUS
Temperature: 20 ℃ / pH: 7.4 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
123 mg/mlprotein1drop
210 mMHEPES1drop
322 %PEG40001reservoir
450 mMHEPES1reservoir
550 mM1reservoirMgCl2
610 mM2-mercaptoethanol1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE
RadiationMonochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.37→30 Å / Num. obs: 36746 / % possible obs: 83.9 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 6.9
Reflection shellResolution: 2.37→2.64 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.146 / Mean I/σ(I) obs: 4.2 / % possible all: 45
Reflection
*PLUS
Num. measured all: 165357
Reflection shell
*PLUS
% possible obs: 45 % / Num. unique obs: 5445

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Processing

Software
NameVersionClassification
AMoREphasing
X-PLOR3.8.5refinement
MOSFLMdata reduction
CCP4(SCALA)data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GFL

1gfl


Resolution: 2.4→30 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / Details: APPLIED DATA CUTOFF: F(CALC)/F (OBS) < = 3.5
RfactorNum. reflection% reflectionSelection details
Rfree0.28 -7 %RANDOM
Rwork0.204 ---
obs0.204 33030 89.9 %-
Refinement stepCycle: LAST / Resolution: 2.4→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7184 0 0 286 7470
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.015
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg3.318
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d28.48
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.376
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Refine LS restraints NCSNCS model details: RESTRAINTS
Software
*PLUS
Name: X-PLOR / Version: 3.8.5 / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.4 Å / Lowest resolution: 30 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor Rfree: 0.28
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg28.48
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.376

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