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- PDB-7h5a: Crystal structure of endothiapepsin IS_cryo1 in complex with AC39... -

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Basic information

Entry
Database: PDB / ID: 7h5a
TitleCrystal structure of endothiapepsin IS_cryo1 in complex with AC39729 at 100 K
ComponentsEndothiapepsin
KeywordsHYDROLASE / Endopeptidase / room temperature
Function / homology
Function and homology information


endothiapepsin / aspartic-type endopeptidase activity / proteolysis
Similarity search - Function
Aspergillopepsin-like catalytic domain / Eukaryotic aspartyl protease / Aspartic peptidase A1 family / Peptidase family A1 domain / Peptidase family A1 domain profile. / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily
Similarity search - Domain/homology
5-fluoranylpyridin-2-amine / Endothiapepsin
Similarity search - Component
Biological speciesCryphonectria parasitica (chestnut blight fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsHuang, C.-Y. / Aumonier, S. / Olieric, V. / Wang, M.
Funding support Switzerland, European Union, 2items
OrganizationGrant numberCountry
Swiss National Science Foundation182369 Switzerland
H2020 Marie Curie Actions of the European Commission884104European Union
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2024
Title: Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.
Authors: Huang, C.Y. / Aumonier, S. / Olieric, V. / Wang, M.
History
DepositionApr 10, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 7, 2024Provider: repository / Type: Initial release
Revision 1.1Aug 21, 2024Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Nov 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

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Assembly

Deposited unit
A: Endothiapepsin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,66137
Polymers33,8141
Non-polymers2,84736
Water5,224290
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)45.440, 74.110, 53.290
Angle α, β, γ (deg.)90.00, 109.97, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Endothiapepsin / Aspartate protease


Mass: 33813.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Cryphonectria parasitica (chestnut blight fungus)
References: UniProt: P11838, endothiapepsin
#2: Chemical...
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 35 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-U1Q / 5-fluoranylpyridin-2-amine


Mass: 112.105 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H5FN2 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 290 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.49 Å3/Da / Density % sol: 50.68 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: 0.1 M ammonium acetate, 0.1 M sodium acetate pH 4.6, and 26 - 30% (v/v) PEG 4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 15, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→42.71 Å / Num. obs: 18374 / % possible obs: 81.4 % / Redundancy: 7.15 % / Biso Wilson estimate: 29.47 Å2 / Rmerge F all: 0.37 / CC1/2: 0.95 / Net I/σ(I): 7.79
Reflection shellResolution: 2→2.11 Å / Redundancy: 1.81 % / Rmerge F all: 0.8 / Num. unique obs: 1096 / CC1/2: 0.8 / Net I/σ(I) all: 2.61 / % possible all: 65.4

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
BUSTER2.10.4 (23-JAN-2024)refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
PDB_EXTRACT3.28 (Apr. 15, 2021)data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→42.71 Å / Cor.coef. Fo:Fc: 0.905 / Cor.coef. Fo:Fc free: 0.875 / SU R Cruickshank DPI: 0.281 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.316 / SU Rfree Blow DPI: 0.235 / SU Rfree Cruickshank DPI: 0.228
RfactorNum. reflection% reflectionSelection details
Rfree0.2742 918 5 %RANDOM
Rwork0.2118 ---
obs0.2149 18358 81.4 %-
Displacement parametersBiso max: 105.99 Å2 / Biso mean: 32.31 Å2 / Biso min: 16 Å2
Baniso -1Baniso -2Baniso -3
1-5.9012 Å20 Å22.5596 Å2
2--9.2938 Å20 Å2
3----15.195 Å2
Refine analyzeLuzzati coordinate error obs: 0.27 Å
Refinement stepCycle: LAST / Resolution: 2→42.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2376 0 128 287 2791
Biso mean--58.43 36.93 -
Num. residues----330
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0082531HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.013436HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d734SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes412HARMONIC5
X-RAY DIFFRACTIONt_it2531HARMONIC10
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.67
X-RAY DIFFRACTIONt_other_torsion14.1
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion357SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact2460SEMIHARMONIC4
LS refinement shellResolution: 2→2.02 Å / Rfactor Rfree error: 0 / Total num. of bins used: 46
RfactorNum. reflection% reflection
Rfree0.3727 20 4.9 %
Rwork0.2143 388 -
all0.2234 408 -
obs--65.35 %

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