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- PDB-1a6f: RNASE P PROTEIN FROM BACILLUS SUBTILIS -

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Basic information

Entry
Database: PDB / ID: 1a6f
TitleRNASE P PROTEIN FROM BACILLUS SUBTILIS
ComponentsRIBONUCLEASE P PROTEIN
KeywordsENDONUCLEASE / RNASE / SUBUNIT
Function / homology
Function and homology information


anion binding / tRNA 3'-trailer cleavage, endonucleolytic / 3'-tRNA processing endoribonuclease activity / ribonuclease P RNA binding / ribonuclease P complex / ribonuclease P / sulfate binding / ribonuclease P activity / tRNA 5'-leader removal / chloride ion binding ...anion binding / tRNA 3'-trailer cleavage, endonucleolytic / 3'-tRNA processing endoribonuclease activity / ribonuclease P RNA binding / ribonuclease P complex / ribonuclease P / sulfate binding / ribonuclease P activity / tRNA 5'-leader removal / chloride ion binding / phosphate ion binding / tRNA binding
Similarity search - Function
Bacterial ribonuclease P protein component signature. / Ribonuclease P, conserved site / Ribonuclease P / Ribonuclease P / Ribosomal Protein S5; domain 2 - #10 / Ribosomal Protein S5; domain 2 / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Ribonuclease P protein component
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodX-RAY DIFFRACTION / MIRAS / Resolution: 2.6 Å
AuthorsStams, T. / Christianson, D.W.
CitationJournal: Science / Year: 1998
Title: Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
Authors: Stams, T. / Niranjanakumari, S. / Fierke, C.A. / Christianson, D.W.
History
DepositionFeb 24, 1998Processing site: BNL
Revision 1.0Mar 23, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Nov 16, 2011Group: Atomic model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RIBONUCLEASE P PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,3814
Polymers14,1551
Non-polymers2273
Water18010
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: RIBONUCLEASE P PROTEIN
hetero molecules

A: RIBONUCLEASE P PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,7638
Polymers28,3092
Non-polymers4546
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_565-x,-y+1,z1
Buried area1600 Å2
ΔGint-131 kcal/mol
Surface area12710 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)82.400, 82.400, 33.500
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number172
Space group name H-MP64
Components on special symmetry positions
IDModelComponents
11A-201-

ZN

21A-300-

HOH

31A-301-

HOH

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Components

#1: Protein RIBONUCLEASE P PROTEIN / / RNASE P PROTEIN


Mass: 14154.549 Da / Num. of mol.: 1
Mutation: ALA 2, HIS 3, LEU 4 ARE INSERTED BETWEEN MET 1 AND LYS 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Cell line: BL21 / Plasmid: BL21 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P25814, ribonuclease P
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 10 / 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: 2.35 Å3/Da / Density % sol: 47.7 %
Crystal growpH: 6.5 / Details: pH 6.5
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Details: drop contains equal volume of protein and reservoir solutions
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
124 mg/mlprotein1drop
210 mMTris-HCl1drop
323 %mPEG5501reservoir
410 mM1reservoirZnSO4
5100 mMMES1reservoir

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 1, 1997 / Details: MIRRORS
RadiationMonochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.6→20 Å / Num. obs: 4058 / % possible obs: 99 % / Redundancy: 3.7 % / Rsym value: 0.086 / Net I/σ(I): 6
Reflection shellResolution: 2.6→2.67 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 2.2 / Rsym value: 0.357 / % possible all: 100
Reflection
*PLUS
Num. measured all: 15148 / Rmerge(I) obs: 0.086
Reflection shell
*PLUS
% possible obs: 100 % / Rmerge(I) obs: 0.357

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Processing

Software
NameVersionClassification
SOLOMONphasing
X-PLOR3.1model building
X-PLOR3.1refinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3.1phasing
RefinementMethod to determine structure: MIRAS / Resolution: 2.6→20 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.1 / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.317 293 8 %RANDOM
Rwork0.205 ---
obs0.205 3654 90 %-
Displacement parametersBiso mean: 46 Å2
Refinement stepCycle: LAST / Resolution: 2.6→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms950 0 7 10 967
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.011
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.8
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d25.5
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.5
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 2.6→2.72 Å / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.404 30 5.8 %
Rwork0.376 398 -
obs--88.55 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.5
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.5
LS refinement shell
*PLUS
Rfactor obs: 0.376

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