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- PDB-2c2f: Dps from Deinococcus radiodurans -

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Basic information

Entry
Database: PDB / ID: 2c2f
TitleDps from Deinococcus radiodurans
ComponentsDNA-BINDING STRESS RESPONSE PROTEIN
KeywordsDNA BINDING PROTEIN / DPS / IRON / DEINOCOCCUS RADIODURANS / DNA-BINDING PROTEIN
Function / homology
Function and homology information


Oxidoreductases; Oxidizing metal ions / oxidoreductase activity, acting on metal ions / nucleoid / ferric iron binding / intracellular iron ion homeostasis / DNA binding / cytoplasm
Similarity search - Function
Dps protein family signature 1. / DNA-binding protein Dps, conserved site / DNA-binding protein Dps / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
: / DNA protection during starvation protein 1
Similarity search - Component
Biological speciesDEINOCOCCUS RADIODURANS (radioresistant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.61 Å
AuthorsRomao, C.V. / Mitchell, E. / McSweeney, S.
CitationJournal: J.Biol.Inorg.Chem. / Year: 2006
Title: The Crystal Structure of Deinococcus Radiodurans Dps Protein (Dr2263) Reveals the Presence of a Novel Metal Centre in the N Terminus.
Authors: Romao, C.V. / Mitchell, E. / Mcsweeney, S.
History
DepositionSep 28, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 26, 2006Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 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: DNA-BINDING STRESS RESPONSE PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,6569
Polymers23,0511
Non-polymers6058
Water5,008278
1
A: DNA-BINDING STRESS RESPONSE PROTEIN
hetero molecules
x 12


Theoretical massNumber of molelcules
Total (without water)283,872108
Polymers276,60912
Non-polymers7,26396
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_555z,x,y1
crystal symmetry operation9_555y,z,x1
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation6_566z,-x+1,-y+11
crystal symmetry operation12_665-y+1,-z+1,x1
crystal symmetry operation7_665-z+1,-x+1,y1
crystal symmetry operation11_566y,-z+1,-x+11
crystal symmetry operation4_566x,-y+1,-z+11
crystal symmetry operation10_656-y+1,z,-x+11
crystal symmetry operation8_656-z+1,x,-y+11
crystal symmetry operation3_656-x+1,y,-z+11
MethodPQS
Unit cell
Length a, b, c (Å)90.616, 90.616, 90.616
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number195
Space group name H-MP23
Components on special symmetry positions
IDModelComponents
11A-1209-

FE

21A-1210-

FE

31A-1212-

SO4

41A-2076-

HOH

51A-2123-

HOH

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Components

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Protein , 1 types, 1 molecules A

#1: Protein DNA-BINDING STRESS RESPONSE PROTEIN / DPS


Mass: 23050.719 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) DEINOCOCCUS RADIODURANS (radioresistant)
Strain: R1 / Plasmid: PDEST14 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9RS64

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Non-polymers , 5 types, 286 molecules

#2: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Fe
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


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


Mass: 18.015 Da / Num. of mol.: 278 / 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: 2.6 Å3/Da / Density % sol: 53 %
Description: DATA WERE COLLECTED REMOTE TO THE ANOMALOUS ABSORPTION EDGES OF ZN AND FE.
Crystal growpH: 8
Details: 200MM LITHIUM SULFATE, 100MM TRIS-HCL PH8.5, 15% PEG4000, pH 8.00

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934
DetectorType: ADSC CCD / Detector: CCD / Date: Sep 23, 2004 / Details: MULTI-LAYER MIRROR
RadiationMonochromator: DIAMOND / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 1.6→31.91 Å / Num. obs: 32579 / % possible obs: 100 % / Redundancy: 84 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 56.5
Reflection shellResolution: 1.6→1.64 Å / Redundancy: 84.7 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 11.1 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
MOSFLMdata reduction
SCALAdata scaling
autoSHARPphasing
RefinementMethod to determine structure: SAD / Resolution: 1.61→64.02 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.967 / SU B: 0.93 / SU ML: 0.033 / Cross valid method: THROUGHOUT / ESU R: 0.058 / ESU R Free: 0.06 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE OCCUPANIES OF ATOMS HAVING OCCUPANCIES LOWER THAN 1 WERE ESTIMATED FROM THEIR ATOMIC B-FACTORS. THE FIRST 29 AMINO ACID RESIDUES WERE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE OCCUPANIES OF ATOMS HAVING OCCUPANCIES LOWER THAN 1 WERE ESTIMATED FROM THEIR ATOMIC B-FACTORS. THE FIRST 29 AMINO ACID RESIDUES WERE NOT MODELLED BECAUSE IT WAS NOT POSSIBLE TO ALLOCATE THE ELECTRON DENSITY.
RfactorNum. reflection% reflectionSelection details
Rfree0.153 1638 5 %RANDOM
Rwork0.131 ---
obs0.132 30939 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: 14.81 Å2
Refinement stepCycle: LAST / Resolution: 1.61→64.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1416 0 27 278 1721
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0211516
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.6371.9552056
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.8445179
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.59323.88285
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.00315251
X-RAY DIFFRACTIONr_dihedral_angle_4_deg10.4831515
X-RAY DIFFRACTIONr_chiral_restr0.1220.2227
X-RAY DIFFRACTIONr_gen_planes_refined0.010.021169
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2250.2696
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3070.21051
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1960.2191
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1920.285
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2140.247
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.0881.5920
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.61821453
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.5483662
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.0494.5603
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.61→1.65 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.189 120
Rwork0.156 2252

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