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- PDB-1ey7: STRUCTURE OF S. NUCLEASE STABILIZING MUTANT S128A -

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Basic information

Entry
Database: PDB / ID: 1ey7
TitleSTRUCTURE OF S. NUCLEASE STABILIZING MUTANT S128A
ComponentsSTAPHYLOCOCCAL NUCLEASEMicrococcal nuclease
KeywordsHYDROLASE
Function / homology
Function and homology information


micrococcal nuclease / nucleic acid binding / endonuclease activity / membrane / extracellular region / metal ion binding
Thermonuclease active site / Staphylococcal nuclease (SNase-like), OB-fold / SNase-like, OB-fold superfamily / Staphylococcal nuclease homologue / Thermonuclease family signature 1. / Thermonuclease family signature 2. / Thermonuclease domain profile.
Thermonuclease
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / AB INITIO / Resolution: 1.88 Å
AuthorsChen, J. / Lu, Z. / Sakon, J. / Stites, W.E.
Citation
Journal: J.Mol.Biol. / Year: 2000
Title: Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.
Authors: Chen, J. / Lu, Z. / Sakon, J. / Stites, W.E.
#1: Journal: Biochemistry / Year: 1992
Title: Contributions of the Polar, Uncharged Amino Acids to the Stability of Staphylococcal Nuclease: Evidence for Mutational Effects on the Free Energy of the Denatured State.
Authors: Green, S.M. / Meeker, A.K. / Shortle, D.
Validation Report
SummaryFull reportAbout validation report
History
DepositionMay 5, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 18, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 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: STAPHYLOCOCCAL NUCLEASE


Theoretical massNumber of molelcules
Total (without water)16,8271
Polymers16,8271
Non-polymers00
Water1,17165
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)47.956, 47.956, 63.805
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number76
Space group name H-MP41

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Components

#1: Protein/peptide STAPHYLOCOCCAL NUCLEASE / Micrococcal nuclease


Mass: 16827.330 Da / Num. of mol.: 1 / Mutation: S128A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Strain: FOGGI / Production host: Escherichia coli (E. coli) / References: UniProt: P00644, micrococcal nuclease
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 65 / 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 Å3/Da / Density % sol: 43.56 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7
Details: MPD, Sodium phosphate buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystal grow
*PLUS
Details: MPD, Sodium phosphate buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Components of the solutions
*PLUS

Crystal-ID: 1 / Sol-ID: reservoir

IDConc.Common name
140-60 %(v/v)MPD
225 mMsodium phosphate

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Data collection

DiffractionMean temperature: 297 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
Reflection
*PLUS
Highest resolution: 1.88 Å / Lowest resolution: 6 Å / % possible obs: 94.8 %

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Processing

Software
NameClassification
SHELXmodel building
SHELXL-97refinement
DENZOdata reduction
SCALEPACKdata scaling
SHELXphasing
RefinementMethod to determine structure: AB INITIO / Resolution: 1.88→6 Å / Num. parameters: 4660 / Num. restraintsaints: 4488 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
RfactorNum. reflection% reflectionSelection details
Rfree0.2661 571 -RANDOM
All0.1957 10853 --
Obs--94.8 %-
Solvent computationSolvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228
Refine analyzeNum. disordered residues: 5 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 1147
Refinement stepCycle: LAST / Resolution: 1.88→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1097 0 0 65 1162
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.006
X-RAY DIFFRACTIONs_angle_d0.024
X-RAY DIFFRACTIONs_similar_dist0
X-RAY DIFFRACTIONs_from_restr_planes0.024
X-RAY DIFFRACTIONs_zero_chiral_vol0.036
X-RAY DIFFRACTIONs_non_zero_chiral_vol0.039
X-RAY DIFFRACTIONs_anti_bump_dis_restr0.005
X-RAY DIFFRACTIONs_rigid_bond_adp_cmpnt0
X-RAY DIFFRACTIONs_similar_adp_cmpnt0.186
X-RAY DIFFRACTIONs_approx_iso_adps0
Software
*PLUS
Name: SHELXL-97 / Classification: refinement
Refinement
*PLUS
Num. reflection obs: 7854 / σ(I): 4 / Rfactor obs: 0.1548
Displacement parameters
*PLUS
Biso mean: 38.6 Å2

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