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- PDB-2bil: The human protein kinase Pim1 in complex with its consensus pepti... -

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Basic information

Entry
Database: PDB / ID: 2bil
TitleThe human protein kinase Pim1 in complex with its consensus peptide Pimtide
Components
  • CONSENSUS PIM1 PEPTIDE PIMTIDE
  • PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1
KeywordsTRANSFERASE / PIM1 / KINASE / CANCER / LEUKEMIA
Function / homology
Function and homology information


positive regulation of cardioblast proliferation / regulation of hematopoietic stem cell proliferation / cellular detoxification / vitamin D receptor signaling pathway / STAT5 activation downstream of FLT3 ITD mutants / transcription factor binding / ribosomal small subunit binding / positive regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of cardiac muscle cell proliferation / positive regulation of TORC1 signaling ...positive regulation of cardioblast proliferation / regulation of hematopoietic stem cell proliferation / cellular detoxification / vitamin D receptor signaling pathway / STAT5 activation downstream of FLT3 ITD mutants / transcription factor binding / ribosomal small subunit binding / positive regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of cardiac muscle cell proliferation / positive regulation of TORC1 signaling / Signaling by FLT3 fusion proteins / negative regulation of innate immune response / positive regulation of brown fat cell differentiation / protein serine/threonine kinase activator activity / regulation of transmembrane transporter activity / positive regulation of protein serine/threonine kinase activity / negative regulation of DNA-binding transcription factor activity / cellular response to type II interferon / manganese ion binding / Interleukin-4 and Interleukin-13 signaling / protein autophosphorylation / protein stabilization / non-specific serine/threonine protein kinase / cell cycle / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / nucleolus / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / nucleoplasm / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Serine/threonine-protein kinase pim-1/2/3 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site ...Serine/threonine-protein kinase pim-1/2/3 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-BI1 / Serine/threonine-protein kinase pim-1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsKnapp, S. / Debreczeni, J. / Bullock, A. / von Delft, F. / Sundstrom, M. / Arrowsmith, C. / Edwards, A. / Guo, K.
CitationJournal: To be Published
Title: The Human Protein Kinase Pim1 in Complex with its Consensus Peptide Pimtide
Authors: Knapp, S. / Debreczeni, J. / Bullock, A. / von Delft, F. / Sundstrom, M. / Arrowsmith, C. / Edwards, A. / Guo, K.
History
DepositionJan 22, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 7, 2005Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jan 24, 2018Group: Database references / Structure summary / Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.3Mar 6, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.4May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.5Oct 23, 2019Group: Data collection / Database references / Other / Category: pdbx_database_status / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_sf / _struct_ref_seq_dif.details
Revision 1.6Dec 13, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CONSENSUS PIM1 PEPTIDE PIMTIDE
B: PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,6383
Polymers37,2252
Non-polymers4121
Water86548
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)98.100, 98.100, 80.040
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65

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Components

#1: Protein/peptide CONSENSUS PIM1 PEPTIDE PIMTIDE


Mass: 1592.850 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human)
#2: Protein PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1 / PIM1


Mass: 35632.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: P11-TORONTO / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P11309, EC: 2.7.1.37
#3: Chemical ChemComp-BI1 / 3-{1-[3-(DIMETHYLAMINO)PROPYL]-1H-INDOL-3-YL}-4-(1H-INDOL-3-YL)-1H-PYRROLE-2,5-DIONE / RBT205 INHIBITOR


Mass: 412.484 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C25H24N4O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE VARIANT DESCRIBED IN THE SEQADV RECORDS BELOW HAS NOT BEEN ANNOTATED IN THE UNIPROT SEQUENCE ...THE VARIANT DESCRIBED IN THE SEQADV RECORDS BELOW HAS NOT BEEN ANNOTATED IN THE UNIPROT SEQUENCE DATABASE ENTRY P11309.

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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: 3.7 Å3/Da / Density % sol: 67 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 0.1 M MSPG, 30% PEG1K, 0.5% DMSO, SITTING DROP, VAPOR DIFFUSION, 277 K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS HTC / Detector: IMAGE PLATE / Date: Dec 4, 2004 / Details: MULTILAYER MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.55→42.48 Å / Num. obs: 14259 / % possible obs: 99 % / Observed criterion σ(I): 2.5 / Redundancy: 6.7 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 9.7
Reflection shellResolution: 2.55→2.65 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 2.7 / % possible all: 97

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XWS

1xws


Resolution: 2.55→24.5 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.901 / SU B: 16.946 / SU ML: 0.181 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.377 / ESU R Free: 0.269 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.248 714 5 %RANDOM
Rwork0.192 ---
obs0.195 13501 98.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 33.66 Å2
Baniso -1Baniso -2Baniso -3
1-1.37 Å20.69 Å20 Å2
2--1.37 Å20 Å2
3----2.06 Å2
Refinement stepCycle: LAST / Resolution: 2.55→24.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2264 0 31 48 2343
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.0212360
X-RAY DIFFRACTIONr_bond_other_d0.0010.022127
X-RAY DIFFRACTIONr_angle_refined_deg1.9741.9633206
X-RAY DIFFRACTIONr_angle_other_deg0.85834911
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1885279
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.73622.821117
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.56715379
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1141522
X-RAY DIFFRACTIONr_chiral_restr0.0910.2337
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022628
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02519
X-RAY DIFFRACTIONr_nbd_refined0.2210.2454
X-RAY DIFFRACTIONr_nbd_other0.1860.22106
X-RAY DIFFRACTIONr_nbtor_refined0.1890.21124
X-RAY DIFFRACTIONr_nbtor_other0.0880.21424
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.150.279
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1170.29
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2760.242
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1140.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7291.51430
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.23622258
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.79131070
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.9954.5948
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: 2.55→2.62 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.341 48
Rwork0.311 956
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.5806-1.11041.01194.07060.1793.0334-0.0364-0.0278-0.23770.09950.06820.03950.19090.0221-0.03180.0122-0.029-0.026-0.0657-0.00110.0207-38.1785-1.36296.8656
21.6059-0.00050.10991.4922-0.13421.68590.04760.1302-0.02470.01410.01220.0769-0.024-0.0307-0.0598-0.0385-0.00950.0091-0.0621-0.0073-0.0497-40.207920.2744-1.8076
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 9
2X-RAY DIFFRACTION1B33 - 125
3X-RAY DIFFRACTION2B126 - 306

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