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- PDB-2xu6: MDV1 coiled coil domain -

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Basic information

Entry
Database: PDB / ID: 2xu6
TitleMDV1 coiled coil domain
ComponentsMDV1 COILED COIL
KeywordsPROTEIN BINDING / MITOCHONDRIAL OUTER MEMBRANE / ADAPTER PROTEIN / ORGANELLE DIVISION
Function / homology
Function and homology information


peroxisome fission / mitochondrial genome maintenance / mitochondrial fission / positive regulation of mitochondrial fission / ubiquitin binding / mitochondrial outer membrane / mitochondrion
Similarity search - Function
Mitochondrial division protein 1 / Mitochondrial division protein 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat ...Mitochondrial division protein 1 / Mitochondrial division protein 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Mitochondrial division protein 1
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.7 Å
AuthorsKoirala, S. / Bui, H.T. / Schubert, H.L. / Eckert, D.M. / Hill, C.P. / Kay, M.S. / Shaw, J.M.
CitationJournal: J.Cell Biol. / Year: 2010
Title: Molecular Architecture of a Dynamin Adaptor: Implications for Assembly of Mitochondrial Fission Complexes
Authors: Koirala, S. / Bui, H.T. / Schubert, H.L. / Eckert, D.M. / Hill, C.P. / Kay, M.S. / Shaw, J.M.
History
DepositionOct 14, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 27, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 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: MDV1 COILED COIL
B: MDV1 COILED COIL


Theoretical massNumber of molelcules
Total (without water)17,0732
Polymers17,0732
Non-polymers00
Water37821
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3170 Å2
ΔGint-30.2 kcal/mol
Surface area9360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)41.380, 41.380, 227.378
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.789, 0.613, 0.042), (0.613, -0.79, 0.022), (0.047, 0.009, -0.999)
Vector: -9.15117, 12.50437, 211.679)

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Components

#1: Protein MDV1 COILED COIL


Mass: 8536.310 Da / Num. of mol.: 2 / Fragment: COILED COIL, RESIDUES 231-300 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): RIPL / References: UniProt: P47025
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 21 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsSEMET DERIVATIVE L248M, L281M ADDITIONAL MET RESIDUES ADDED FOR SEMET PHASING.

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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: 2.85 Å3/Da / Density % sol: 56.85 % / Description: NONE
Crystal growpH: 7.5
Details: 16% PEG 3350 0.1 M BIS-TRIS-PROPANE, PH 7.5 0.4 M NACL

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Data collection

DiffractionMean temperature: 287 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.97982
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 2, 2009 / Details: RH COATED FLAT MIRROR.
RadiationMonochromator: SIDE SCATTERING I-BEAM BENT SINGLE CRYSTAL ASYMMETRIC CUT 4.9650 DEG
Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97982 Å / Relative weight: 1
ReflectionResolution: 2.7→38 Å / Num. obs: 10392 / % possible obs: 99.2 % / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Biso Wilson estimate: 60.8 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 10
Reflection shellResolution: 2.7→2.79 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 2.4 / % possible all: 99.2

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Processing

Software
NameVersionClassification
REFMAC5.5.0062refinement
HKL-2000data reduction
HKL-2000data scaling
SOLVEphasing
RefinementMethod to determine structure: MAD
Starting model: NONE

Resolution: 2.7→38 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.915 / SU B: 14.906 / SU ML: 0.287 / Cross valid method: THROUGHOUT / ESU R: 0.704 / ESU R Free: 0.382
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.31381 278 4.6 %RANDOM
Rwork0.2704 ---
obs0.27251 5730 99.11 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 57.684 Å2
Baniso -1Baniso -2Baniso -3
1-0.99 Å20 Å20 Å2
2--0.99 Å20 Å2
3----1.97 Å2
Refinement stepCycle: LAST / Resolution: 2.7→38 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1031 0 0 21 1052
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0221114
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5021.9941512
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.3175146
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.77828.0667
X-RAY DIFFRACTIONr_dihedral_angle_3_deg23.87515250
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.464155
X-RAY DIFFRACTIONr_chiral_restr0.0940.2177
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.02838
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6941.5667
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.37621096
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.2273447
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.1334.5404
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: 2.7→2.77 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.436 22 -
Rwork0.39 419 -
obs--99.55 %

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