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- PDB-2a5l: The crystal structure of the Trp repressor binding protein WrbA f... -

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Basic information

Entry
Database: PDB / ID: 2a5l
TitleThe crystal structure of the Trp repressor binding protein WrbA from Pseudomonas aeruginosa
ComponentsTrp repressor binding protein WrbA
KeywordsTRANSCRIPTION / APC5760 / PA0949 / PROTEIN STRUCTURE INITIATIVE / PSI / repressor binding protein / Structural Genomics / Midwest Center for Structural Genomics / MCSG
Function / homology
Function and homology information


NAD(P)H dehydrogenase (quinone) / NADPH dehydrogenase (quinone) activity / NADH:ubiquinone reductase (non-electrogenic) activity / NAD(P)H dehydrogenase (quinone) activity / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / FMN binding / cellular response to oxidative stress / electron transfer activity / membrane
Similarity search - Function
Flavoprotein WrbA-like / NADPH-dependent FMN reductase-like / NADPH-dependent FMN reductase / Flavodoxin, conserved site / Flavodoxin signature. / Flavodoxin domain / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Flavoprotein-like superfamily / Rossmann fold ...Flavoprotein WrbA-like / NADPH-dependent FMN reductase-like / NADPH-dependent FMN reductase / Flavodoxin, conserved site / Flavodoxin signature. / Flavodoxin domain / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Flavoprotein-like superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / NAD(P)H dehydrogenase (quinone)
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.7 Å
AuthorsLunin, V.V. / Evdokimova, E. / Kudritska, M. / Osipiuk, J. / Joachimiak, A. / Edwards, A.M. / Savchenko, A. / Midwest Center for Structural Genomics (MCSG)
CitationJournal: To be Published
Title: The crystal structure of the Trp repressor binding protein WrbA from Pseudomonas aeruginosa
Authors: Lunin, V.V. / Evdokimova, E. / Kudritska, M. / Osipiuk, J. / Joachimiak, A. / Edwards, A.M. / Savchenko, A.
History
DepositionJun 30, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 12, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Trp repressor binding protein WrbA
B: Trp repressor binding protein WrbA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,3754
Polymers42,3272
Non-polymers492
Water8,593477
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2430 Å2
ΔGint-19 kcal/mol
Surface area15160 Å2
MethodPISA
2
A: Trp repressor binding protein WrbA
B: Trp repressor binding protein WrbA
hetero molecules

A: Trp repressor binding protein WrbA
B: Trp repressor binding protein WrbA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,7508
Polymers84,6534
Non-polymers974
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_556y,x,-z+11
Buried area10870 Å2
ΔGint-86 kcal/mol
Surface area24310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.927, 62.927, 190.022
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Components on special symmetry positions
IDModelComponents
11A-199-

MG

21B-199-

MG

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Components

#1: Protein Trp repressor binding protein WrbA


Mass: 21163.279 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Plasmid: PET15B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: GenBank: 15596146, UniProt: Q9I509*PLUS
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 477 / 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: 2.1 Å3/Da / Density % sol: 42 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 30% PEG4K. 0.2M NaAcetate, 0.1M Tris pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9795001 Å
DetectorType: CUSTOM-MADE / Detector: CCD / Date: Jun 20, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795001 Å / Relative weight: 1
ReflectionResolution: 1.7→40 Å / Num. all: 40802 / Num. obs: 40802 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Rsym value: 0.045 / Net I/σ(I): 18.1
Reflection shellResolution: 1.7→1.74 Å / Redundancy: 4.4 % / Mean I/σ(I) obs: 5.9 / Rsym value: 0.276 / % possible all: 99.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASESphasing
RefinementMethod to determine structure: SAD / Resolution: 1.7→37.9 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.946 / SU B: 1.479 / SU ML: 0.051 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.091 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19561 2174 5.1 %RANDOM
Rwork0.15808 ---
all0.16 40802 --
obs0.16 40802 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.887 Å2
Baniso -1Baniso -2Baniso -3
1-0.07 Å20 Å20 Å2
2--0.07 Å20 Å2
3----0.14 Å2
Refinement stepCycle: LAST / Resolution: 1.7→37.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2653 0 2 477 3132
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0222715
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.6221.9823691
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5685359
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.72322.16597
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.44115434
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.8221518
X-RAY DIFFRACTIONr_chiral_restr0.1420.2421
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.022044
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2090.21410
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3060.21902
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1810.2332
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2430.298
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1730.251
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1681.51796
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.84922801
X-RAY DIFFRACTIONr_scbond_it2.96331023
X-RAY DIFFRACTIONr_scangle_it4.044.5890
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.7→1.744 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.232 153 -
Rwork0.177 2958 -
obs--100 %

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