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- PDB-1mji: DETAILED ANALYSIS OF RNA-PROTEIN INTERACTIONS WITHIN THE BACTERIA... -

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Basic information

Entry
Database: PDB / ID: 1mji
TitleDETAILED ANALYSIS OF RNA-PROTEIN INTERACTIONS WITHIN THE BACTERIAL RIBOSOMAL PROTEIN L5/5S RRNA COMPLEX
Components
  • 50S ribosomal protein L5
  • 5S rRNA fragment
KeywordsRIBOSOME / ribosomal protein - 5S rRNA complex
Function / homology
Function and homology information


cytosolic large ribosomal subunit / tRNA binding / rRNA binding / structural constituent of ribosome / translation
Similarity search - Function
50s Ribosomal Protein L5; Chain: A, / Ribosomal protein L5 / Ribosomal protein L5, bacterial-type / Ribosomal protein L5, conserved site / Ribosomal protein L5 signature. / Ribosomal protein L5, N-terminal / Ribosomal protein L5 / Ribosomal protein L5, C-terminal / ribosomal L5P family C-terminus / Ribosomal protein L5 ...50s Ribosomal Protein L5; Chain: A, / Ribosomal protein L5 / Ribosomal protein L5, bacterial-type / Ribosomal protein L5, conserved site / Ribosomal protein L5 signature. / Ribosomal protein L5, N-terminal / Ribosomal protein L5 / Ribosomal protein L5, C-terminal / ribosomal L5P family C-terminus / Ribosomal protein L5 / Ribosomal protein L5 domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
: / RNA / RNA (> 10) / Large ribosomal subunit protein uL5
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Thermus thermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.5 Å
AuthorsPerederina, A. / Nevskaya, N. / Nikonov, O. / Nikulin, A. / Dumas, P. / Yao, M. / Tanaka, I. / Garber, M. / Gongadze, G. / Nikonov, S.
CitationJournal: RNA / Year: 2002
Title: Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex
Authors: Perederina, A. / Nevskaya, N. / Nikonov, O. / Nikulin, A. / Dumas, P. / Yao, M. / Tanaka, I. / Garber, M. / Gongadze, G. / Nikonov, S.
History
DepositionAug 28, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 21, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: 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
C: 5S rRNA fragment
D: 5S rRNA fragment
A: 50S ribosomal protein L5
B: 50S ribosomal protein L5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,18110
Polymers64,0064
Non-polymers1756
Water3,369187
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)51.89, 99.60, 65.73
Angle α, β, γ (deg.)90.00, 100.05, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: RNA chain 5S rRNA fragment


Mass: 10847.543 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Description: in vitro transcription
#2: Protein 50S ribosomal protein L5


Mass: 21155.387 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P41201
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 187 / 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: 2.61 Å3/Da / Density % sol: 52.91 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: sodium cacodylate, magnesium acetate, potassium chlorate, PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Components of the solutions
IDNameCrystal-IDSol-ID
1sodium cacodylate11
2magnesium acetate11
3potassium chlorate11
4PEG 800011
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
12 mg/mlprotein1drop
250 mMsodium cacodylate1droppH6.5
3100 mMmagnesium acetate1drop
450 mM1dropKF
510 %PEG80001drop
650 mMsodium cacodylate1reservoirpH6.5
7100 mMmagnesium acetate1reservoir
8200 mM1reservoirKCl
910 %PEG80001reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.968 Å
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.968 Å / Relative weight: 1
ReflectionResolution: 2.5→15 Å / Num. all: 22650 / Num. obs: 22650 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: 39.3 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 13.2
Reflection shellResolution: 2.5→2.59 Å / Redundancy: 3 % / Rmerge(I) obs: 0.186 / Mean I/σ(I) obs: 3.3 / Num. unique all: 1908 / % possible all: 84.1
Reflection
*PLUS
Lowest resolution: 15 Å / Num. obs: 22852 / % possible obs: 99.9 % / Redundancy: 3.02 %
Reflection shell
*PLUS
Highest resolution: 2.5 Å / % possible obs: 84.1 % / Redundancy: 3 % / Num. unique obs: 1908

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing
RefinementMethod to determine structure: MAD / Resolution: 2.5→14.91 Å / Rfactor Rfree error: 0.006 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.288 2146 9.9 %RANDOM
Rwork0.21 ---
obs0.21 21043 95.3 %-
all-21650 --
Solvent computationSolvent model: FLAT MODEL / Bsol: 52.9597 Å2 / ksol: 0.324816 e/Å3
Displacement parametersBiso mean: 39.4 Å2
Baniso -1Baniso -2Baniso -3
1-7.03 Å20 Å23.4 Å2
2---3.38 Å20 Å2
3----3.65 Å2
Refine analyzeLuzzati coordinate error free: 0.44 Å / Luzzati sigma a free: 0.44 Å
Refinement stepCycle: LAST / Resolution: 2.5→14.91 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2926 1434 6 187 4553
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_dihedral_angle_d20.7
X-RAY DIFFRACTIONc_improper_angle_d1.39
X-RAY DIFFRACTIONc_mcbond_it1.71.5
X-RAY DIFFRACTIONc_mcangle_it3.12
X-RAY DIFFRACTIONc_scbond_it1.92
X-RAY DIFFRACTIONc_scangle_it3.132.5
LS refinement shellResolution: 2.5→2.66 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.365 339 10.5 %
Rwork0.309 2883 -
obs--85.3 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2DNA-RNA_REP.PARAMDNA-RNA.TOP
X-RAY DIFFRACTION3WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION4ION.PARAMION.TOP
Refinement
*PLUS
Highest resolution: 2.5 Å / Lowest resolution: 15 Å / Rfactor Rwork: 0.21
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.31
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg20.7
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.39

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