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- PDB-8h3i: Crystal Structure of the apo-form Pathogenesis-related Protein Hc... -

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Basic information

Entry
Database: PDB / ID: 8h3i
TitleCrystal Structure of the apo-form Pathogenesis-related Protein HcPR10 from Halostachys caspica
ComponentsPR10
KeywordsALLERGEN / Pathogenesis-related Protein / Halostachys caspica / reservoir for cytokinin
Function / homology
Function and homology information


abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / defense response / signaling receptor activity / nucleus / cytoplasm
Similarity search - Function
Bet v I type allergen / Bet v I/Major latex protein / Pathogenesis-related protein Bet v 1 family / : / START-like domain superfamily
Similarity search - Domain/homology
Biological speciesHalostachys caspica (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsWang, Z. / Ren, Y.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32125008 China
CitationJournal: Front Plant Sci / Year: 2023
Title: Halostachys caspica pathogenesis-related protein 10 acts as a cytokinin reservoir to regulate plant growth and development.
Authors: Feng, Y. / Ren, Y. / Zhang, H. / Heng, Y. / Wang, Z. / Wang, Y.
History
DepositionOct 8, 2022Deposition site: PDBJ / Processing site: PDBC
Revision 1.0May 17, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 8, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.2May 1, 2024Group: Database references / Category: citation / citation_author
Revision 1.3Jul 17, 2024Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PR10


Theoretical massNumber of molelcules
Total (without water)18,1801
Polymers18,1801
Non-polymers00
Water1,67593
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)59.426, 59.426, 92.023
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Space group name HallP322"
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
#4: x-y,-y,-z+1/3
#5: -x,-x+y,-z+2/3
#6: y,x,-z
Components on special symmetry positions
IDModelComponents
11A-261-

HOH

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Components

#1: Protein PR10


Mass: 18179.594 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Halostachys caspica (plant) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A171NYA8
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 93 / Source method: isolated from a natural source / Formula: H2O

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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: 2.58 Å3/Da / Density % sol: 52.33 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1M HEPES sodium 7.5;1.4M Sodium citrate tribasic dihydrate

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17B1 / Wavelength: 0.9793 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Jun 4, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 15377 / % possible obs: 100 % / Redundancy: 19 % / Biso Wilson estimate: 25.94 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 25.8
Reflection shellResolution: 1.9→1.93 Å / Rmerge(I) obs: 0.66 / Num. unique obs: 742

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1BV1

1bv1


Resolution: 1.9→22.46 Å / SU ML: 0.194 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 23.1949 / Stereochemistry target values: GeoStd + Monomer Library
RfactorNum. reflection% reflection
Rfree0.2478 774 5.05 %
Rwork0.1989 14550 -
obs0.2013 15324 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 30.31 Å2
Refinement stepCycle: LAST / Resolution: 1.9→22.46 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1272 0 0 93 1365
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01051302
X-RAY DIFFRACTIONf_angle_d1.09731768
X-RAY DIFFRACTIONf_chiral_restr0.1051197
X-RAY DIFFRACTIONf_plane_restr0.007231
X-RAY DIFFRACTIONf_dihedral_angle_d23.5141475
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-2.020.28041450.20942349X-RAY DIFFRACTION99.88
2.02-2.170.27311140.20642407X-RAY DIFFRACTION100
2.17-2.390.26221470.21072374X-RAY DIFFRACTION99.96
2.39-2.740.29541210.21492415X-RAY DIFFRACTION100
2.74-3.450.23671240.21252448X-RAY DIFFRACTION99.92
3.45-22.460.22081230.182557X-RAY DIFFRACTION99.74

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