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- PDB-1d7h: FKBP COMPLEXED WITH DMSO -

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Basic information

Entry
Database: PDB / ID: 1d7h
TitleFKBP COMPLEXED WITH DMSO
ComponentsPROTEIN (FK506-BINDING PROTEIN)
KeywordsISOMERASE / IMMUNOPHILIN / DMSO / FKBP
Function / homology
Function and homology information


negative regulation of transforming growth factor beta1 activation / macrolide binding / regulation of activin receptor signaling pathway / extrinsic component of organelle membrane / cytoplasmic side of membrane / regulation of amyloid precursor protein catabolic process / SMAD protein complex assembly / heart trabecula formation / type I transforming growth factor beta receptor binding / transforming growth factor beta receptor binding ...negative regulation of transforming growth factor beta1 activation / macrolide binding / regulation of activin receptor signaling pathway / extrinsic component of organelle membrane / cytoplasmic side of membrane / regulation of amyloid precursor protein catabolic process / SMAD protein complex assembly / heart trabecula formation / type I transforming growth factor beta receptor binding / transforming growth factor beta receptor binding / terminal cisterna / ryanodine receptor complex / activin binding / protein maturation by protein folding / 'de novo' protein folding / ventricular cardiac muscle tissue morphogenesis / FK506 binding / supramolecular fiber organization / negative regulation of phosphoprotein phosphatase activity / SMAD binding / heart morphogenesis / protein peptidyl-prolyl isomerization / regulation of ryanodine-sensitive calcium-release channel activity / chaperone-mediated protein folding / T cell activation / calcium ion transmembrane transport / positive regulation of protein ubiquitination / sarcoplasmic reticulum / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / regulation of protein localization / Z disc / transforming growth factor beta receptor signaling pathway / regulation of immune response / ion channel binding / positive regulation of I-kappaB kinase/NF-kappaB signaling / protein refolding / protein folding / positive regulation of protein binding / amyloid fibril formation / membrane / cytosol / cytoplasm
FKBP-type peptidyl-prolyl cis-trans isomerase domain / Chitinase A; domain 3 - #40 / Chitinase A; domain 3 / Roll / Alpha Beta
Peptidyl-prolyl cis-trans isomerase FKBP1A
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsBurkhard, P. / Taylor, P. / Walkinshaw, M.D.
Citation
Journal: J.Mol.Biol. / Year: 2000
Title: X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies.
Authors: Burkhard, P. / Taylor, P. / Walkinshaw, M.D.
#1: Journal: J.Am.Chem.Soc. / Year: 1991
Title: Atomic Structure of the Rapamycin Human Immunophilin FKBP-12 Complex
Authors: Van Duyne, G.D. / Standaert, R.F. / Schreiber, S.L. / Clardy, J.
Validation Report
SummaryFull reportAbout validation report
History
DepositionOct 18, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 21, 1999Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Oct 4, 2017Group: Derived calculations / Refinement description / Category: software / struct_conf / struct_conf_type / Item: _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (FK506-BINDING PROTEIN)
B: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0578
Polymers23,6732
Non-polymers3846
Water2,702150
1
A: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,0294
Polymers11,8371
Non-polymers1923
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,0294
Polymers11,8371
Non-polymers1923
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules

A: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0578
Polymers23,6732
Non-polymers3846
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,y,-z1
Buried area1980 Å2
ΔGint-40 kcal/mol
Surface area10570 Å2
MethodPISA, PQS
4
B: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules

B: PROTEIN (FK506-BINDING PROTEIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0578
Polymers23,6732
Non-polymers3846
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_654-x+1,y,-z-11
MethodPQS
Unit cell
γ
α
β
Length a, b, c (Å)102.800, 36.450, 56.000
Angle α, β, γ (deg.)90.00, 96.00, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-401-

NH4

21A-403-

SO4

31B-402-

NH4

41B-404-

SO4

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Components

#1: Protein PROTEIN (FK506-BINDING PROTEIN) / FKBP-12


Mass: 11836.508 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P62942, peptidylprolyl isomerase
#2: Chemical ChemComp-NH4 / AMMONIUM ION / Ammonium


Mass: 18.038 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: H4N
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 150 / 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: 2.2 Å3/Da / Density % sol: 44.15 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 56 % SAT. AMMONIUM SULFATE 5 % DMSO, 100 MM TRIS (PH 8.0), VAPOR DIFFUSION, HANGING DROP, temperature 297K
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
10.6 mMprotein1drop
2340 mMDMSO1drop
350 mMTris-HCl1drop
428 %(w/v)ammonium sulfate1drop
71 MTris-HCl1reservoir
5ammonium sulfate1reservoir
6DMSO1reservoir

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Data collection

DiffractionMean temperature: 297 K
Diffraction sourceSource: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.5418
DetectorType: ENRAF-NONIUS / Detector: AREA DETECTOR / Date: Jan 1, 1995 / Details: COLLIMATOR
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.9→100 Å / Num. obs: 14868 / % possible obs: 97 % / Rmerge(I) obs: 0.07

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Processing

Software
NameVersionClassification
X-PLORmodel building
X-PLOR3.1refinement
MADNESSdata reduction
CCP4(AGROVATAdata scaling
ROTAVATAdata scaling
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→20 Å / Cross valid method: A POSTERIORI / σ(F): 3 / Stereochemistry target values: ENGH & HUBER
RfactorNum. reflection% reflectionSelection details
Rfree0.273 488 3 %RANDOM
Rwork0.213 ---
Obs0.213 12997 97 %-
Refinement stepCycle: LAST / Resolution: 1.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1664 0 20 150 1834
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.627
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refine LS restraints
*PLUS
Type: x_dihedral_angle_deg / Dev ideal: 27.221

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