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- PDB-4nxe: Crystal structure of iLOV-I486(2LT) at pH 6.5 -

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Basic information

Entry
Database: PDB / ID: 4nxe
TitleCrystal structure of iLOV-I486(2LT) at pH 6.5
ComponentsPhototropin-2
KeywordsFLAVOPROTEIN / FLUORESCENT PROTEIN
Function / homology
Function and homology information


chloroplast relocation / phototropism / stomatal movement / blue light photoreceptor activity / response to blue light / plastid / circadian rhythm / kinase activity / FMN binding / protein autophosphorylation ...chloroplast relocation / phototropism / stomatal movement / blue light photoreceptor activity / response to blue light / plastid / circadian rhythm / kinase activity / FMN binding / protein autophosphorylation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / Golgi apparatus / ATP binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
PAS domain / PAS-associated, C-terminal / PAC domain profile. / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / Beta-Lactamase / PAS domain / PAS repeat profile. / PAS domain ...PAS domain / PAS-associated, C-terminal / PAC domain profile. / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / Beta-Lactamase / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
FLAVIN MONONUCLEOTIDE / Phototropin-2
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.103 Å
AuthorsWang, J. / Liu, X. / Li, J.
CitationJournal: J.Am.Chem.Soc. / Year: 2014
Title: Significant expansion of fluorescent protein sensing ability through the genetic incorporation of superior photo-induced electron-transfer quenchers.
Authors: Liu, X. / Jiang, L. / Li, J. / Wang, L. / Yu, Y. / Zhou, Q. / Lv, X. / Gong, W. / Lu, Y. / Wang, J.
History
DepositionDec 9, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Sep 24, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2022Group: Database references / Derived calculations
Category: citation / database_2 ...citation / database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.2Nov 8, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Phototropin-2
B: Phototropin-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,8524
Polymers27,9392
Non-polymers9132
Water82946
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3120 Å2
ΔGint-18 kcal/mol
Surface area10590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)37.474, 65.430, 49.565
Angle α, β, γ (deg.)90.00, 102.67, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Phototropin-2 / Defective in chloroplast avoidance protein 1 / Non-phototropic hypocotyl 1-like protein 1 / AtKin7 ...Defective in chloroplast avoidance protein 1 / Non-phototropic hypocotyl 1-like protein 1 / AtKin7 / NPH1-like protein 1


Mass: 13969.408 Da / Num. of mol.: 2 / Fragment: LOV DOMAIN, UNP Residues 388-496 / Mutation: S394T, S409G, I452T, F470L, M475V, I486Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: PHOT2, CAV1, KIN7, NPL1, At5g58140, K21L19.6 / Production host: Escherichia coli (E. coli)
References: UniProt: P93025, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H21N4O9P
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 46 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsRESIDUES C426A IS MUTAGENESIS ACCORDING TO DATABASE P93025.

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.12 Å3/Da / Density % sol: 42.03 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: Protein sample (20-30 mg/ml protein, 20 mM Tris, pH 8.0, 50 mM NaCl), equal volume of reservoir solution (0.2M Magnesium acetate tetrahydrate, 0.1M Sodium cacodylate trihydrate pH 6.5, 20% ...Details: Protein sample (20-30 mg/ml protein, 20 mM Tris, pH 8.0, 50 mM NaCl), equal volume of reservoir solution (0.2M Magnesium acetate tetrahydrate, 0.1M Sodium cacodylate trihydrate pH 6.5, 20% w/v Polyethylene glycol 8000), VAPOR DIFFUSION, SITTING DROP, temperature 289.0K

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Data collection

DiffractionMean temperature: 200 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 20, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. all: 13633 / Num. obs: 12433 / % possible obs: 91.2 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1
Reflection shellResolution: 2.1→2.14 Å / Redundancy: 3.6 % / Num. unique all: 651 / % possible all: 97.5

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Processing

Software
NameVersionClassification
HKL-2000data collection
MLPHAREphasing
PHENIX(phenix.refine: 1.8.1_1168)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EES

4ees


Resolution: 2.103→29.347 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8205 / SU ML: 0.25 / σ(F): 1.36 / Phase error: 25.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2528 564 4.91 %RANDOM
Rwork0.2046 ---
all0.2091 13669 --
obs0.2068 11492 84.07 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 82.51 Å2 / Biso mean: 31.1057 Å2 / Biso min: 10.83 Å2
Refinement stepCycle: LAST / Resolution: 2.103→29.347 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1724 0 62 46 1832
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0031824
X-RAY DIFFRACTIONf_angle_d0.7472478
X-RAY DIFFRACTIONf_dihedral_angle_d18.426692
X-RAY DIFFRACTIONf_chiral_restr0.047259
X-RAY DIFFRACTIONf_plane_restr0.003317
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.1025-2.3140.26581230.2172222369
2.314-2.64870.25881650.2008306695
2.6487-3.33630.23581580.2151304894
3.3363-29.34960.25911180.1964259178
Refinement TLS params.Method: refined / Origin x: -4.8377 Å / Origin y: 2.8614 Å / Origin z: 59.7222 Å
111213212223313233
T0.117 Å20.0061 Å20.0093 Å2-0.0805 Å20.0242 Å2--0.1695 Å2
L1.7715 °20.0147 °20.6332 °2-1.7759 °20.559 °2--3.8827 °2
S-0.024 Å °-0.0734 Å °-0.0569 Å °0.0252 Å °0.0185 Å °-0.0099 Å °0.0894 Å °-0.0317 Å °0.025 Å °
Refinement TLS groupSelection details: ALL

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