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- PDB-1uoj: CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LECTIN 1 IN THE CALCI... -

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Basic information

Entry
Database: PDB / ID: 1uoj
TitleCRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LECTIN 1 IN THE CALCIUM-FREE STATE
ComponentsPA-I GALACTOPHILIC LECTIN
KeywordsSUGAR BINDING PROTEIN / GALACTOSE BINDING
Function / homology
Function and homology information


heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / carbohydrate binding / periplasmic space / cell surface / cytoplasm
Similarity search - Function
PA-IL-like / PA-IL-like protein / Galactose-binding lectin / Galactose-binding-like domain superfamily / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
PA-I galactophilic lectin
Similarity search - Component
Biological speciesPSEUDOMONAS AERUGINOSA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsCioci, G. / Mitchell, E. / Gautier, C. / Wimmerova, M. / Perez, S. / Gilboa-Garber, N. / Imberty, A.
CitationJournal: FEBS Lett. / Year: 2003
Title: Structural Basis of Calcium and Galactose Recognition by the Lectin Pa-Il of Pseudomonas Aeruginosa
Authors: Cioci, G. / Mitchell, E. / Gautier, C. / Wimmerova, M. / Sudakevitz, D. / Perez, S. / Gilboa-Garber, N. / Imberty, A.
History
DepositionSep 19, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 4, 2003Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2011Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Other / Structure summary / Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 13, 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_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PA-I GALACTOPHILIC LECTIN
B: PA-I GALACTOPHILIC LECTIN
C: PA-I GALACTOPHILIC LECTIN
D: PA-I GALACTOPHILIC LECTIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,2736
Polymers51,0814
Non-polymers1922
Water2,468137
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7140 Å2
ΔGint-17.4 kcal/mol
Surface area23640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)49.675, 51.464, 166.787
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
PA-I GALACTOPHILIC LECTIN / PA-IL GALACTOSE-BINDING LECTIN / PA-IL / GALACTOSE-BINDING LECTIN


Mass: 12770.137 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) PSEUDOMONAS AERUGINOSA (bacteria) / References: UniProt: Q05097
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 137 / Source method: isolated from a natural source / Formula: H2O
Compound detailsD-GALACTOSE SPECIFIC LECTIN THAT BINDS IN DECREASING ORDER OF AFFINITY: MELIBIOSE, METHYL-ALPHA-D- ...D-GALACTOSE SPECIFIC LECTIN THAT BINDS IN DECREASING ORDER OF AFFINITY: MELIBIOSE, METHYL-ALPHA-D-GALACTOSIDE, D-GALACTOSE,METHYL-BETA-D-GALACTOSIDE, N-ACETYL-D- GALACTOSAMINE.

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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 Å3/Da / Density % sol: 37 %
Crystal growMethod: vapor diffusion, hanging drop / pH: 5
Details: HANGING DROP: PROTEIN SOLUTION: PA1L 10 MG/ML + DGAL 0.5 MG/ML. RESERVOIR SOLUTION (NH4)2SO4, 1.5 M 20% ISOPROPANOL PH 4.5 2 UL + 2 UL
Crystal grow
*PLUS
pH: 4.5 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
110 mg/mlprotein1drop
21.5 Mammonium sulfate1reservoirpH4.5
320 %isopropanol1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.932
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 15, 2003 / Details: MIRROR
RadiationMonochromator: SILICON / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.932 Å / Relative weight: 1
ReflectionResolution: 2.4→20.37 Å / Num. obs: 17328 / % possible obs: 99.8 % / Redundancy: 6.54 % / Rmerge(I) obs: 0.089 / Net I/σ(I): 7.6715
Reflection shellResolution: 2.4→2.48 Å / Redundancy: 6.19 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 1.93 / % possible all: 99.8
Reflection
*PLUS
Highest resolution: 2.4 Å / Num. obs: 17451 / Redundancy: 6.5 % / Num. measured all: 114114 / Rmerge(I) obs: 0.089
Reflection shell
*PLUS
% possible obs: 99.8 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 1.9

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1L7L

1l7l


Resolution: 2.4→20.37 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.904 / SU B: 8.76 / SU ML: 0.205 / Cross valid method: THROUGHOUT / ESU R: 0.691 / ESU R Free: 0.306 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.263 882 5.1 %RANDOM
Rwork0.183 ---
obs-16569 99.6 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK
Displacement parametersBiso mean: 27.72 Å2
Baniso -1Baniso -2Baniso -3
1-1.23 Å20 Å20 Å2
2--0.14 Å20 Å2
3----1.38 Å2
Refinement stepCycle: LAST / Resolution: 2.4→20.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3604 0 10 137 3751
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0213704
X-RAY DIFFRACTIONr_bond_other_d0.0020.023160
X-RAY DIFFRACTIONr_angle_refined_deg1.5191.9175064
X-RAY DIFFRACTIONr_angle_other_deg0.80837384
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.1785480
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0950.2544
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.024280
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02704
X-RAY DIFFRACTIONr_nbd_refined0.1870.2645
X-RAY DIFFRACTIONr_nbd_other0.2410.23513
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0840.22118
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1770.2139
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2810.28
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2990.232
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1180.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7591.52380
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.36923812
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.80531324
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.8724.51252
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: 2.4→2.46 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.27 75
Rwork0.2 1211
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.016
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg1.52
LS refinement shell
*PLUS
Rfactor Rfree: 0.27 / Rfactor Rwork: 0.2

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