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- PDB-2uyi: Crystal structure of KSP in complex with ADP and thiophene contai... -

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Basic information

Entry
Database: PDB / ID: 2uyi
TitleCrystal structure of KSP in complex with ADP and thiophene containing inhibitor 33
ComponentsKINESIN-LIKE PROTEIN KIF11
KeywordsCELL CYCLE / KSP / EG5 / COMPLEX / MITOSIS / THIOPHENE / INHIBITOR / NUCLEOTIDE-BINDING / KINESIN SPINDLE PROTEIN / MOTOR PROTEIN / CELL DIVISION / PHOSPHORYLATION / MICROTUBULE / COILED COIL / ATP-BINDING
Function / homology
Function and homology information


Kinesins / plus-end-directed microtubule motor activity / regulation of mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / mitotic centrosome separation / microtubule motor activity / kinesin complex / spindle organization / mitotic spindle assembly / microtubule-based movement ...Kinesins / plus-end-directed microtubule motor activity / regulation of mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / mitotic centrosome separation / microtubule motor activity / kinesin complex / spindle organization / mitotic spindle assembly / microtubule-based movement / MHC class II antigen presentation / mitotic spindle organization / mitotic spindle / spindle / spindle pole / mitotic cell cycle / microtubule binding / microtubule / cell division / protein kinase binding / protein-containing complex / membrane / ATP binding / nucleus / cytosol
Similarity search - Function
Kinesin-associated microtubule-binding / Kinesin-associated microtubule-binding domain / Kinesin motor domain / Kinesin / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain profile. / Kinesin motor domain / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain ...Kinesin-associated microtubule-binding / Kinesin-associated microtubule-binding domain / Kinesin motor domain / Kinesin / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain profile. / Kinesin motor domain / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Chem-K02 / Kinesin-like protein KIF11
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.1 Å
AuthorsLee, T.T.
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2007
Title: Synthesis and Sar of Thiophene Containing Kinesin Spindle Protein (Ksp) Inhibitors.
Authors: Pinkerton, A.B. / Lee, T.T. / Hoffman, T.Z. / Wang, Y. / Kahraman, M. / Cook, T.G. / Severance, D. / Gahman, T.C. / Noble, S.A. / Shiau, A.K. / Davis, R.L.
History
DepositionApr 7, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 22, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: KINESIN-LIKE PROTEIN KIF11
B: KINESIN-LIKE PROTEIN KIF11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,7678
Polymers82,1112
Non-polymers1,6566
Water4,972276
1
A: KINESIN-LIKE PROTEIN KIF11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,8844
Polymers41,0561
Non-polymers8283
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: KINESIN-LIKE PROTEIN KIF11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,8844
Polymers41,0561
Non-polymers8283
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
γ
α
β
Length a, b, c (Å)69.535, 80.139, 159.036
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein KINESIN-LIKE PROTEIN KIF11 / KINESIN-RELATED MOTOR PROTEIN EG5 / KINESIN-LIKE SPINDLE PROTEIN HKSP / THYROID RECEPTOR- ...KINESIN-RELATED MOTOR PROTEIN EG5 / KINESIN-LIKE SPINDLE PROTEIN HKSP / THYROID RECEPTOR-INTERACTING PROTEIN 5 / TRIP-5 / KINESIN-LIKE PROTEIN 1 / KINESIN SPINDLE PROTEIN


Mass: 41055.582 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 1-368
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P52732
#2: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-K02 / (5R)-N,N-DIETHYL-5-METHYL-2-[(THIOPHEN-2-YLCARBONYL)AMINO]-4,5,6,7-TETRAHYDRO-1-BENZOTHIOPHENE-3-CARBOXAMIDE


Mass: 376.536 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H24N2O2S2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 276 / 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: 2.7 Å3/Da / Density % sol: 54 %
Crystal growpH: 6
Details: 100 MM BIS-TRIS (PH 6.0) 200 MM AMMONIUM SULFATE, AND 18-20% PEG3350. 10 MM SRCL2

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Data collection

DiffractionMean temperature: 277 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 28, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. obs: 52737 / % possible obs: 97 % / Observed criterion σ(I): 2 / Redundancy: 6.1 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 11.2

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: OTHER / Resolution: 2.1→79.56 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.899 / SU B: 5.541 / SU ML: 0.151 / Cross valid method: THROUGHOUT / ESU R: 0.236 / ESU R Free: 0.215 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.294 2615 5.1 %RANDOM
Rwork0.237 ---
obs0.24 48485 96.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 32.58 Å2
Baniso -1Baniso -2Baniso -3
1-0.51 Å20 Å20 Å2
2---1.02 Å20 Å2
3---0.5 Å2
Refinement stepCycle: LAST / Resolution: 2.1→79.56 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5198 0 106 276 5580
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0240.0225386
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.2681.9947294
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4055658
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.46224.017234
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.915976
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.6111542
X-RAY DIFFRACTIONr_chiral_restr0.1630.2850
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.023954
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2320.22465
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3080.23541
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1640.2340
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2440.263
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1970.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.4191.53440
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.20425350
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it3.3632238
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.8954.51944
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: 2.1→2.15 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.377 192
Rwork0.261 3510

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