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- PDB-3fbb: Crystal structure of the Mimivirus NDK N62L-R107G double mutant c... -

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Basic information

Entry
Database: PDB / ID: 3fbb
TitleCrystal structure of the Mimivirus NDK N62L-R107G double mutant complexed with UDP
ComponentsNucleoside diphosphate kinaseNucleoside-diphosphate kinase
KeywordsTRANSFERASE / phosphotransferase nucleotide binding / ATP-binding / Kinase / Magnesium / Metal-binding / Nucleotide metabolism / Nucleotide-binding / Phosphoprotein
Function / homology
Function and homology information


nucleoside-diphosphate kinase / CTP biosynthetic process / UTP biosynthetic process / GTP biosynthetic process / nucleoside diphosphate kinase activity / ATP binding / metal ion binding
Nucleoside diphosphate kinase, active site / Nucleoside diphosphate kinase / Nucleoside diphosphate kinase-like domain / Nucleoside diphosphate kinase-like domain superfamily / Nucleoside diphosphate kinase / Nucleoside diphosphate kinases active site.
Nucleoside diphosphate kinase
Biological speciesAcanthamoeba polyphaga mimivirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsJeudy, S. / Lartigue, A. / Claverie, J.M. / Abergel, C.
CitationJournal: J.Virol. / Year: 2009
Title: Dissecting the unique nucleotide specificity of mimivirus nucleoside diphosphate kinase.
Authors: Jeudy, S. / Lartigue, A. / Claverie, J.M. / Abergel, C.
Validation Report
SummaryFull reportAbout validation report
History
DepositionNov 19, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 11, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nucleoside diphosphate kinase
B: Nucleoside diphosphate kinase
C: Nucleoside diphosphate kinase
D: Nucleoside diphosphate kinase
E: Nucleoside diphosphate kinase
F: Nucleoside diphosphate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,77318
Polymers97,2026
Non-polymers2,57112
Water3,279182
1
A: Nucleoside diphosphate kinase
C: Nucleoside diphosphate kinase
E: Nucleoside diphosphate kinase
hetero molecules

A: Nucleoside diphosphate kinase
C: Nucleoside diphosphate kinase
E: Nucleoside diphosphate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,77318
Polymers97,2026
Non-polymers2,57112
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555x,-y,-z1
2
B: Nucleoside diphosphate kinase
D: Nucleoside diphosphate kinase
F: Nucleoside diphosphate kinase
hetero molecules

B: Nucleoside diphosphate kinase
D: Nucleoside diphosphate kinase
F: Nucleoside diphosphate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,77318
Polymers97,2026
Non-polymers2,57112
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_755-x+2,y,-z+1/21
Unit cell
γ
α
β
Length a, b, c (Å)79.676, 152.899, 184.534
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein/peptide
Nucleoside diphosphate kinase / Nucleoside-diphosphate kinase / NDP kinase / NDK


Mass: 16200.407 Da / Num. of mol.: 6 / Mutation: N62L, R107G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acanthamoeba polyphaga mimivirus / Gene: MIMI_R418, NDK / Plasmid: pDIGS02 / Production host: Escherichia coli (E. coli) / Strain (production host): rosetta(DE3)pLysS / References: UniProt: Q5UQL3, nucleoside-diphosphate kinase
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg / Magnesium
#3: Chemical
ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Mass: 404.161 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Uridine diphosphate / Comment: UDP *YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 182 / 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: 2.89 Å3/Da / Density % sol: 57.45 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4
Details: 40-44% MPD, 0.1M MOPS, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 105 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 9, 2007
RadiationMonochromator: Diamond (111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 2.4→70 Å / Num. obs: 44282 / % possible obs: 99.6 % / Redundancy: 6.7 % / Biso Wilson estimate: 48.801 Å2 / Rsym value: 0.056 / Net I/σ(I): 10.5
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 6.8 % / Mean I/σ(I) obs: 2.3 / Num. unique all: 6333 / Rsym value: 0.321 / % possible all: 99.8

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
AMoREphasing
PHENIX(phenix.refine)refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2b8p
Resolution: 2.4→28.549 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.53 / Phase error: 21.84 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.227 2230 5.04 %random
Rwork0.181 42052 --
Obs0.184 44282 99.77 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 53.162 Å2 / ksol: 0.362 e/Å3
Displacement parametersBiso max: 93.84 Å2 / Biso mean: 41.236 Å2 / Biso min: 23.09 Å2
Baniso -1Baniso -2Baniso -3
1--0.115 Å20 Å20 Å2
2---1.393 Å20 Å2
3---1.509 Å2
Refinement stepCycle: LAST / Resolution: 2.4→28.549 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6295 0 156 182 6633
Refine LS restraints

Refinement-ID: X-RAY DIFFRACTION

TypeDev idealNumber
f_bond_d0.0096571
f_angle_d1.2728896
f_chiral_restr0.079986
f_plane_restr0.0051124
f_dihedral_angle_d20.672470
LS refinement shell

Refinement-ID: X-RAY DIFFRACTION / Total num. of bins used: 16

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.4520.2781390.21825962735100
2.452-2.5090.3111300.21525832713100
2.509-2.5720.2641500.22125942744100
2.572-2.6410.2751300.20626152745100
2.641-2.7190.2671660.19525802746100
2.719-2.8070.2411470.20125892736100
2.807-2.9070.241390.19526322771100
2.907-3.0230.291350.20626142749100
3.023-3.1610.2851500.20326052755100
3.161-3.3270.2741250.1926652790100
3.327-3.5350.2121430.17625892732100
3.535-3.8070.2121340.16726672801100
3.807-4.190.1931290.15426532782100
4.19-4.7930.1891310.14626832814100
4.793-6.030.21500.16726662816100
6.03-28.5510.1821320.1782721285397

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