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- PDB-1n5n: Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa -

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Basic information

Entry
Database: PDB / ID: 1n5n
TitleCrystal Structure of Peptide Deformylase from Pseudomonas aeruginosa
ComponentsPeptide deformylase
KeywordsHYDROLASE / metalloenzyme / drug design / deformylation
Function / homology
Function and homology information


co-translational protein modification / peptidyl-methionine modification / N-terminal protein amino acid modification / peptide deformylase / peptide deformylase activity / translation / metal ion binding
Peptide deformylase superfamily / Peptide deformylase / Polypeptide deformylase
Peptide deformylase
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsKreusch, A. / Spraggon, G. / Lee, C.C. / Klock, H. / McMullan, D. / Ng, K. / Shin, T. / Vincent, J. / Warner, I. / Ericson, C. / Lesley, S.A.
CitationJournal: J.MOL.BIOL. / Year: 2003
Title: Structure analysis of peptide deformylases from streptococcus pneumoniae,staphylococcus aureus, thermotoga maritima, and pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase
Authors: Kreusch, A. / Spraggon, G. / Lee, C.C. / Klock, H. / McMullan, D. / Ng, K. / Shin, T. / Vincent, J. / Warner, I. / Ericson, C. / Lesley, S.A.
Validation Report
SummaryFull reportAbout validation report
History
DepositionNov 6, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 24, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Peptide deformylase
B: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,1417
Polymers41,7342
Non-polymers4075
Water4,720262
1
A: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1164
Polymers20,8671
Non-polymers2503
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Peptide deformylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,0243
Polymers20,8671
Non-polymers1582
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)68.612, 73.562, 75.995
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/peptide Peptide deformylase / / PDF / Polypeptide deformylase


Mass: 20866.818 Da / Num. of mol.: 2 / Mutation: D84E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Plasmid: pMH4 / Production host: Escherichia coli (E. coli) / Strain (production host): geneHogs / References: UniProt: Q9I7A8, peptide deformylase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn / Zinc
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3 / Glycerol
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 262 / Source method: isolated from a natural source / Formula: H2O / Water

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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: 2.3 Å3/Da / Density % sol: 46.44 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6
Details: Peg6000, LiCl, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS

Crystal-ID: 1 / Sol-ID: reservoir

IDConc.Common nameChemical formulaDetails
120 %PEG6000
21.0 MLiCl
30.1 MMESpH6.0

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Data collection

DiffractionMean temperature: 90 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 8, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.8→41.87 Å / Num. all: 36473 / Num. obs: 36428 / Observed criterion σ(F): 0 / Observed criterion σ(I): 2 / Redundancy: 26 % / Biso Wilson estimate: 19.4 Å2 / Rsym value: 0.083 / Net I/σ(I): 12
Reflection shellResolution: 1.8→1.83 Å / Num. unique all: 1791 / Rsym value: 0.341 / % possible all: 100
Reflection
*PLUS
Highest resolution: 1.8 Å / Lowest resolution: 50 Å / % possible obs: 99.9 % / Rmerge(I) obs: 0.083
Reflection shell
*PLUS
% possible obs: 100 % / Rmerge(I) obs: 0.341

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Processing

Software
NameClassification
HKL-2000data collection
SCALEPACKdata scaling
AMoREphasing
CNSrefinement
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB Entry 1BS4
Resolution: 1.8→41.87 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.244 1790 -random
Rwork0.196 ---
All-36428 --
Obs-35997 99.1 %-
Displacement parametersBiso mean: 25 Å2
Baniso -1Baniso -2Baniso -3
1-3.53 Å20 Å20 Å2
2---4.73 Å20 Å2
3---1.2 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.27 Å0.21 Å
Luzzati d res low-5 Å
Luzzati sigma a0.26 Å0.22 Å
Refinement stepCycle: LAST / Resolution: 1.8→41.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2675 0 20 262 2957
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.044
X-RAY DIFFRACTIONc_angle_d3.2
X-RAY DIFFRACTIONc_dihedral_angle_d24.5
X-RAY DIFFRACTIONc_improper_angle_d2.53
LS refinement shellResolution: 1.8→1.91 Å / Rfactor Rfree error: 0.023
RfactorNum. reflection% reflection
Rfree0.395 303 -
Rwork0.339 --
Obs-5506 97.9 %
Refinement
*PLUS
Highest resolution: 1.8 Å / Lowest resolution: 50 Å / Rfactor Rfree: 0.245 / Rfactor Rwork: 0.197
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_deg3.2
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg24.5
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg2.53

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