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- PDB-4a2o: STRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WIT... -

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Basic information

Entry
Database: PDB / ID: 4a2o
TitleSTRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH SULFATE ANIONS
ComponentsEOSINOPHIL CATIONIC PROTEIN
KeywordsHYDROLASE / OXIDOREDUCTASE / ANTIMICROBIAL / CYTOTOXIC
Function / homology
Function and homology information


induction of bacterial agglutination / Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA catabolic process / Antimicrobial peptides / RNA nuclease activity / innate immune response in mucosa / lipopolysaccharide binding / antimicrobial humoral immune response mediated by antimicrobial peptide / chemotaxis / azurophil granule lumen ...induction of bacterial agglutination / Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA catabolic process / Antimicrobial peptides / RNA nuclease activity / innate immune response in mucosa / lipopolysaccharide binding / antimicrobial humoral immune response mediated by antimicrobial peptide / chemotaxis / azurophil granule lumen / antibacterial humoral response / endonuclease activity / defense response to Gram-negative bacterium / nucleic acid binding / defense response to Gram-positive bacterium / innate immune response / Neutrophil degranulation / extracellular space / extracellular region
Similarity search - Function
P-30 Protein / Ribonuclease A-like domain / Pancreatic ribonuclease / Ribonuclease A, active site / Ribonuclease A-domain / Ribonuclease A-like domain superfamily / Pancreatic ribonuclease / Pancreatic ribonuclease family signature. / Pancreatic ribonuclease / Roll / Alpha Beta
Similarity search - Domain/homology
Eosinophil cationic protein
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.69 Å
AuthorsBoix, E. / Pulido, D. / Moussaoui, M. / Nogues, V. / Russi, S.
CitationJournal: J.Struct.Biol. / Year: 2012
Title: The Sulfate-Binding Site Structure of the Human Eosinophil Cationic Protein as Revealed by a New Crystal Form.
Authors: Boix, E. / Pulido, D. / Moussaoui, M. / Nogues, V. / Russi, S.
History
DepositionSep 28, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 27, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EOSINOPHIL CATIONIC PROTEIN
B: EOSINOPHIL CATIONIC PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,54316
Polymers31,1982
Non-polymers1,34514
Water6,684371
1
A: EOSINOPHIL CATIONIC PROTEIN
B: EOSINOPHIL CATIONIC PROTEIN
hetero molecules

A: EOSINOPHIL CATIONIC PROTEIN
B: EOSINOPHIL CATIONIC PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,08532
Polymers62,3964
Non-polymers2,69028
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area8730 Å2
ΔGint-351.5 kcal/mol
Surface area28570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.264, 51.290, 55.394
Angle α, β, γ (deg.)90.00, 111.28, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-1137-

SO4

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Components

#1: Protein EOSINOPHIL CATIONIC PROTEIN / ECP / RIBONUCLEASE 3 / RNASE 3


Mass: 15598.876 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell: EOSINOPHIL / Plasmid: PET11C/ECP / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P12724, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 371 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsRECOMBINANT PROTEIN EXPRESSED USING A SYNTHETIC GENE (BOIX ET AL. J.BIOL.CHEM. 274, 15605) BASED ON ...RECOMBINANT PROTEIN EXPRESSED USING A SYNTHETIC GENE (BOIX ET AL. J.BIOL.CHEM. 274, 15605) BASED ON THE NP_002926 NATURAL VARIANT (THR97ARG)

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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: 1.63 Å3/Da / Density % sol: 24.17 % / Description: NONE
Crystal growpH: 8.5 / Details: pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9537
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 1, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.69→51.62 Å / Num. obs: 25341 / % possible obs: 98.5 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 23.6 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.4
Reflection shellResolution: 1.69→1.78 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.3 / % possible all: 90.8

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Processing

Software
NameVersionClassification
REFMAC5.5.0110refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1DYT

1dyt


Resolution: 1.69→51.62 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.929 / SU B: 2.42 / SU ML: 0.081 / Cross valid method: THROUGHOUT / ESU R: 0.12 / ESU R Free: 0.125 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-27 OF P12724 ARE THE SIGNAL PEPTIDE. LOOP 90-92 IS PARTIALLY DISORDERED SIDE CHAINS OF R28, W35, R73, F76, R101, AND R105 ARE PARTIALLY DISORDERED.
RfactorNum. reflection% reflectionSelection details
Rfree0.22251 1343 5 %RANDOM
Rwork0.1622 ---
obs0.16533 25341 98.54 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 16.866 Å2
Baniso -1Baniso -2Baniso -3
1-0.78 Å20 Å20.28 Å2
2---0.62 Å20 Å2
3---0.05 Å2
Refinement stepCycle: LAST / Resolution: 1.69→51.62 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2170 0 70 371 2611
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0240.0212342
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.9411.9523219
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4795276
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.08921.28125
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.06915351
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.4151537
X-RAY DIFFRACTIONr_chiral_restr0.1420.2335
X-RAY DIFFRACTIONr_gen_planes_refined0.0130.0221835
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.2771.51368
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.1122254
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.4433974
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it5.154.5959
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.692→1.736 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.365 81 -
Rwork0.289 1644 -
obs--86.64 %

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