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- PDB-1mhn: High resolution crystal structure of the SMN Tudor domain -

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Basic information

Database: PDB / ID: 1mhn
TitleHigh resolution crystal structure of the SMN Tudor domain
ComponentsSurvival motor neuron proteinSurvival of motor neuron
KeywordsRNA BINDING PROTEIN / SMN / SMA / spinal muscular atrophy
Function / homology
Function and homology information

Gemini of coiled bodies / SMN complex / import into nucleus / SMN-Sm protein complex / snRNP Assembly / spliceosomal complex assembly / spliceosomal snRNP assembly / Cajal body / DNA-templated transcription, termination / cytoplasmic ribonucleoprotein granule ...Gemini of coiled bodies / SMN complex / import into nucleus / SMN-Sm protein complex / snRNP Assembly / spliceosomal complex assembly / spliceosomal snRNP assembly / Cajal body / DNA-templated transcription, termination / cytoplasmic ribonucleoprotein granule / Z disc / nervous system development / perikaryon / nuclear body / neuron projection / axon / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Survival motor neuron / Survival motor neuron protein (SMN) / Tudor domain profile. / Tudor domain / Tudor domain / SH3 type barrels. - #140 / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Survival motor neuron protein
Similarity search - Component
Biological speciesHomo sapiens (human)
AuthorsSprangers, R. / Groves, M.R. / Sinning, I. / Sattler, M.
Journal: J.Mol.Biol. / Year: 2003
Title: High Resolution X-ray and NMR Structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginine residues
Authors: Sprangers, R. / Groves, M.R. / Sinning, I. / Sattler, M.
#1: Journal: To be Published
Title: Definition of domain boundaries and crystallization of the SMN Tudor domain
Authors: Sprangers, R. / Selenko, P. / Sattler, M. / Sinning, I. / Groves, M.R.
DepositionAug 20, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 25, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

Structure visualization

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Deposited unit
A: Survival motor neuron protein

Theoretical massNumber of molelcules
Total (without water)6,6491

  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)27.652, 27.652, 110.299
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65


#1: Protein Survival motor neuron protein / Survival of motor neuron / SMN / Component of gems 1 / Gemin1

Mass: 6649.454 Da / Num. of mol.: 1 / Fragment: Tudor domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: smn1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q16637
#2: Water ChemComp-HOH / water / Water

Mass: 18.015 Da / Num. of mol.: 65 / Source method: isolated from a natural source / Formula: H2O

Experimental details


ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

CrystalDensity Matthews: 1.83 Å3/Da / Density % sol: 32.79 %
Crystal growTemperature: 285 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: Amonium Sulphate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Crystal grow
Details: Sprangers, R., (2003) Acta Crystallogr., D59, 366.

Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.934 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 1, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 1.8→23.95 Å / Num. all: 4489 / Num. obs: 4499 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 11.4 %
Reflection shellResolution: 1.8→1.9 Å / % possible all: 100


MOSFLMdata reduction
SCALAdata scaling
CCP4(SCALA)data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→23.947 Å / Isotropic thermal model: Isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.1871 465 -RANDOM
Rwork0.1445 ---
all0.1466 4440 --
obs0.1466 4440 100 %-
Refinement stepCycle: LAST / Resolution: 1.8→23.947 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms465 0 0 65 530
LS refinement shellResolution: 1.8→1.9 Å
Solvent computation
Displacement parameters
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.0143
X-RAY DIFFRACTIONx_angle_deg1.341
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg3.42

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