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- PDB-6qpe: Engineered beta-lactoglobulin: variant L58F -

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Basic information

Entry
Database: PDB / ID: 6qpe
TitleEngineered beta-lactoglobulin: variant L58F
ComponentsBeta-lactoglobulin
KeywordsTRANSPORT PROTEIN / lactoglobuin / lipocalin / mutation
Function / homology
Function and homology information


retinol binding / long-chain fatty acid binding / extracellular region / identical protein binding
Similarity search - Function
Beta-lactoglobulin / Lipocalin / Lipocalin family conserved site / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin beta-barrel core domain / Calycin / Lipocalin / Lipocalin signature. / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / Beta-lactoglobulin
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsLoch, J.I. / Kaczor, K. / Leiwnski, K.
Funding support Poland, 1items
OrganizationGrant numberCountry
Polish National Science Centre2012/05/B/ST5/00278 Poland
CitationJournal: J.Struct.Biol. / Year: 2020
Title: Structure-based design approach to rational site-directed mutagenesis of beta-lactoglobulin.
Authors: Bonarek, P. / Loch, J.I. / Tworzydlo, M. / Cooper, D.R. / Milto, K. / Wrobel, P. / Kurpiewska, K. / Lewinski, K.
History
DepositionFeb 13, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 27, 2019Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Apr 29, 2020Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.3Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-lactoglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,3262
Polymers18,2671
Non-polymers591
Water1,874104
1
A: Beta-lactoglobulin
hetero molecules

A: Beta-lactoglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,6524
Polymers36,5342
Non-polymers1182
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555y,x,-z1
Unit cell
Length a, b, c (Å)52.674, 52.674, 112.013
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein Beta-lactoglobulin / Beta-LG


Mass: 18267.031 Da / Num. of mol.: 1 / Mutation: L1A, I2S, L58F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Gene: LGB / Plasmid: pET-Duet-1 / Production host: Escherichia coli (E. coli) / Strain (production host): Origami B (DE3) / References: UniProt: P02754
#2: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 104 / Source method: isolated from a natural source / Formula: H2O
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: 2.45 Å3/Da / Density % sol: 49.82 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 2.80 M (NH4)2SO4 in 0.1 M Tris-HCl pH 8.0

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Data collection

DiffractionMean temperature: 120 K / Serial crystal experiment: N
Diffraction sourceSource: SEALED TUBE / Type: Agilent SuperNova / Wavelength: 1.54 Å
DetectorType: AGILENT ATLAS CCD / Detector: CCD / Date: Nov 25, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.2→15.23 Å / Num. obs: 9457 / % possible obs: 98.3 % / Redundancy: 2.8 % / CC1/2: 0.99 / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.057 / Rrim(I) all: 0.103 / Net I/σ(I): 6.8 / Num. measured all: 26229 / Scaling rejects: 58
Reflection shell

Diffraction-ID: 1 / Redundancy: 1.8 %

Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.2-2.270.1832.37930.8780.1760.25493.9
8.8-15.230.0471210.9910.0410.06367.8

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Processing

Software
NameVersionClassification
REFMAC5.8.023refinement
Aimless0.7.2data scaling
PDB_EXTRACT3.24data extraction
CrysalisProdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1BSY

1bsy


Resolution: 2.2→13.68 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.887 / WRfactor Rfree: 0.2422 / WRfactor Rwork: 0.1822 / FOM work R set: 0.8076 / SU B: 7.253 / SU ML: 0.179 / SU R Cruickshank DPI: 0.2699 / SU Rfree: 0.2258 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.27 / ESU R Free: 0.226 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2514 782 8.3 %RANDOM
Rwork0.1851 ---
obs0.1907 8651 97.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 121.42 Å2 / Biso mean: 25.017 Å2 / Biso min: 7.59 Å2
Baniso -1Baniso -2Baniso -3
1--0.03 Å2-0.01 Å2-0 Å2
2---0.03 Å20 Å2
3---0.08 Å2
Refinement stepCycle: final / Resolution: 2.2→13.68 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1234 0 4 104 1342
Biso mean--42.08 30 -
Num. residues----157
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0141296
X-RAY DIFFRACTIONr_bond_other_d0.0010.0171241
X-RAY DIFFRACTIONr_angle_refined_deg1.3621.6651755
X-RAY DIFFRACTIONr_angle_other_deg0.7721.6512914
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.1745161
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.44325.61457
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.31815249
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.967153
X-RAY DIFFRACTIONr_chiral_restr0.0680.2176
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.021389
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02211
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_it1.8972.563631
X-RAY DIFFRACTIONr_mcbond_other1.8962.562630
X-RAY DIFFRACTIONr_mcangle_it3.033.83788
X-RAY DIFFRACTIONr_mcangle_other3.0283.831789
X-RAY DIFFRACTIONr_scbond_it2.2792.895662
X-RAY DIFFRACTIONr_scbond_other2.2792.895662
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.7584.197965
X-RAY DIFFRACTIONr_long_range_B_refined6.25830.8961362
X-RAY DIFFRACTIONr_long_range_B_other6.17930.4091341
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.2→2.256 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.264 54 -
Rwork0.219 585 -
all-639 -
obs--94.11 %

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