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- PDB-1lm6: Crystal Structure of Peptide Deformylase from Streptococcus pneumoniae -

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Basic information

Entry
Database: PDB / ID: 1lm6
TitleCrystal Structure of Peptide Deformylase from Streptococcus pneumoniae
Componentspeptide deformylase DEFB
KeywordsHYDROLASE / PDF / Metalloenzyme / peptide deformylase
Function / homologyPeptide deformylase / Peptide deformylase superfamily / Polypeptide deformylase / peptide deformylase / peptide deformylase activity / translation / metal ion binding / Peptide deformylase
Function and homology information
Biological speciesStreptococcus pneumoniae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 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
DepositionApr 30, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 24, 2003Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Nov 12, 2014Group: Structure summary

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: peptide deformylase DEFB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,3793
Polymers24,2311
Non-polymers1482
Water3,009167
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)49.709, 49.709, 91.407
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number78
Space group name H-MP43
DetailsThe biological unit is a monomer

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Components

#1: Protein/peptide peptide deformylase DEFB


Mass: 24230.684 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Plasmid: pMH1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9F2F0, peptide deformylase
#2: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe / Iron
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3 / Glycerol
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 167 / Source method: isolated from a natural source / Formula: H2O / Water
Nonpolymer detailsheterogen The modeled Fe(III) ion is a guess and has not been confirmed experimentally.
Sequence detailsTHESE RESIDUES CORRESPOND TO THE FIRST SIX RESIDUES OF THIOREDOXIN FOLLOWED BY A HEXA-HIS ...THESE RESIDUES CORRESPOND TO THE FIRST SIX RESIDUES OF THIOREDOXIN FOLLOWED BY A HEXA-HIS PURIFICATION TAG. THE FULL LENGTH TAG SEQUENCE IS MGSDKIHHHHHH.

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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: 2.33 Å3/Da / Density % sol: 47.23 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8
Details: PEG 8000, 0.2 M MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS

Crystal-ID: 1

IDConc.Common nameSol-IDChemical formulaDetails
125 mg/mlproteindrop
220 %(w/v)PEG8000reservoir
30.2 MreservoirMgCl2
40.1 MTrisreservoirpH8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 13, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.75→35 Å / Num. obs: 22277 / % possible obs: 99.5 % / Observed criterion σ(I): 2 / Redundancy: 8 % / Biso Wilson estimate: 22.7 Å2 / Rsym value: 0.048 / Net I/σ(I): 20.6
Reflection shellResolution: 1.75→1.85 Å / Num. unique all: 3661 / Rsym value: 0.241 / % possible all: 98.1
Reflection
*PLUS
Lowest resolution: 50 Å / Rmerge(I) obs: 0.048
Reflection shell
*PLUS
% possible obs: 98.1 % / Rmerge(I) obs: 0.241

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNS1refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1LM4
Resolution: 1.75→33.65 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 2045273.26 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT
RfactorNum. reflection% reflectionSelection details
Rfree0.256 1119 5 %RANDOM
Rwork0.208 ---
Obs0.208 22277 99.5 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 51.1237 Å2 / ksol: 0.352357 e/Å3
Displacement parametersBiso mean: 29.6 Å2
Baniso -1Baniso -2Baniso -3
1-5.4 Å20 Å20 Å2
2--5.4 Å20 Å2
3----10.79 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.27 Å0.21 Å
Luzzati d res low-5 Å
Luzzati sigma a0.22 Å0.17 Å
Refinement stepCycle: LAST / Resolution: 1.75→33.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1493 0 7 167 1667
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.014
X-RAY DIFFRACTIONc_angle_deg1.7
X-RAY DIFFRACTIONc_dihedral_angle_d24.4
X-RAY DIFFRACTIONc_improper_angle_d1.66
LS refinement shellResolution: 1.75→1.86 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.325 177 4.8 %
Rwork0.269 3484 -
Obs--98.1 %
Xplor file

Refinement-ID: X-RAY DIFFRACTION

Serial noParam fileTopol file
1PROTEIN_REP_NEW.PARAMPROTEIN_NEW.TOP
2WATER_REP.PARAMWATER.TOP
3ION.PARAMION.TOP
4GLYCEROL_NEW.PARAMGLYCEROL.TOP
Refinement
*PLUS
Lowest resolution: 50 Å / % reflection Rfree: 5 % / Rfactor Rwork: 0.207
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg24.4
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.66

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