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- PDB-3sd7: 1.7 Angstrom Resolution Crystal Structure of Putative Phosphatase... -

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Basic information

Entry
Database: PDB / ID: 3sd7
Title1.7 Angstrom Resolution Crystal Structure of Putative Phosphatase from Clostridium difficile
ComponentsPutative phosphatase
KeywordsHYDROLASE / Structural Genomics / haloacid dehalogenase-like hydrolase / Center for Structural Genomics of Infectious Diseases / CSGID
Function / homology
Function and homology information


Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases / hydrolase activity
Similarity search - Function
Putative phosphatase; domain 2 / Phosphoglycolate phosphatase-like, domain 2 / Haloacid dehalogenase-like hydrolase / Haloacid dehalogenase-like hydrolase / HAD hydrolase, subfamily IA / HAD superfamily/HAD-like / HAD superfamily / HAD-like superfamily / DNA polymerase; domain 1 / Rossmann fold ...Putative phosphatase; domain 2 / Phosphoglycolate phosphatase-like, domain 2 / Haloacid dehalogenase-like hydrolase / Haloacid dehalogenase-like hydrolase / HAD hydrolase, subfamily IA / HAD superfamily/HAD-like / HAD superfamily / HAD-like superfamily / DNA polymerase; domain 1 / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
TRIETHYLENE GLYCOL / Putative phosphatase
Similarity search - Component
Biological speciesClostridium difficile (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsMinasov, G. / Shuvalova, L. / Dubrovska, I. / Winsor, J. / Papazisi, L. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID)
CitationJournal: TO BE PUBLISHED
Title: 1.7 Angstrom Resolution Crystal Structure of Putative Phosphatase from Clostridium difficile.
Authors: Minasov, G. / Shuvalova, L. / Dubrovska, I. / Winsor, J. / Papazisi, L. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID)
History
DepositionJun 8, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 29, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Putative phosphatase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,2086
Polymers27,8161
Non-polymers3935
Water2,900161
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)116.333, 116.333, 36.080
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number80
Space group name H-MI41

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Putative phosphatase /


Mass: 27815.605 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium difficile (bacteria) / Strain: 630 / Gene: CD3605 / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q181K6

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Non-polymers , 5 types, 166 molecules

#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#3: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 161 / 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: 2.19 Å3/Da / Density % sol: 43.94 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.3
Details: Protein: 7.1mG/mL, 0.5M Sodium chloride, 0.01M Tris, pH 8.3, Screen: JCSG+, D12, 0.04M Potassium Phosphate, 16% (w/v) PEG 8000, 20% (v/v) Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 6, 2011 / Details: Beryllium lenses
RadiationMonochromator: Diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.7→30 Å / Num. all: 26648 / Num. obs: 26648 / % possible obs: 99.2 % / Observed criterion σ(I): -3 / Redundancy: 7.2 % / Biso Wilson estimate: 29.7 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 35
Reflection shellResolution: 1.7→1.73 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.541 / Mean I/σ(I) obs: 2.8 / Num. unique all: 1216 / % possible all: 91.1

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Processing

Software
NameVersionClassification
Blu-IceMaxdata collection
PHASERphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3MC1

3mc1


Resolution: 1.7→29.65 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.964 / SU B: 4.094 / SU ML: 0.062
Isotropic thermal model: Thermal Factors Individually Refined
Cross valid method: THROUGHOUT / ESU R: 0.1 / ESU R Free: 0.095 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19298 1344 5 %RANDOM
Rwork0.16745 ---
all0.16877 25299 --
obs0.16877 25299 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: 39.35 Å2
Baniso -1Baniso -2Baniso -3
1--0.78 Å20 Å20 Å2
2---0.78 Å2-0 Å2
3---1.56 Å2
Refinement stepCycle: LAST / Resolution: 1.7→29.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1759 0 24 161 1944
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0221903
X-RAY DIFFRACTIONr_bond_other_d0.0010.021318
X-RAY DIFFRACTIONr_angle_refined_deg1.2981.9882569
X-RAY DIFFRACTIONr_angle_other_deg0.82733246
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.0445234
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.62125.76192
X-RAY DIFFRACTIONr_dihedral_angle_3_deg10.39215364
X-RAY DIFFRACTIONr_dihedral_angle_4_deg5.366155
X-RAY DIFFRACTIONr_chiral_restr0.0880.2276
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.022121
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02372
X-RAY DIFFRACTIONr_mcbond_it1.2261.51126
X-RAY DIFFRACTIONr_mcbond_other0.3811.5458
X-RAY DIFFRACTIONr_mcangle_it2.04921842
X-RAY DIFFRACTIONr_scbond_it3.0833777
X-RAY DIFFRACTIONr_scangle_it4.9944.5727
LS refinement shellResolution: 1.701→1.745 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.407 72 -
Rwork0.286 1722 -
obs-1722 91.11 %
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)
13.4201-0.598-0.39835.76751.71481.8758-0.1134-0.40360.40520.11560.1318-0.1982-0.05230.1466-0.01840.01910.0215-0.01840.0762-0.04180.054772.427653.60165.0911
23.5849-1.0150.01215.17720.26231.5857-0.1136-0.19811.0757-0.07340.1918-0.6929-0.20960.201-0.07820.0746-0.0196-0.00150.175-0.08080.362374.422263.71275.5677
33.2322-0.5034-0.34673.2060.65071.7715-0.0426-0.0958-0.0075-0.11980.0972-0.2316-0.07050.0462-0.05460.03240.02640.03070.05370.01420.035877.795742.9889-1.9106
44.4412-2.0475-0.95524.50071.04011.2481-0.01870.2177-0.4821-0.2118-0.11810.5847-0.013-0.1740.13680.02130.0047-0.02480.0345-0.02690.101362.351643.1252-3.4063
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 37
2X-RAY DIFFRACTION2A38 - 92
3X-RAY DIFFRACTION3A93 - 155
4X-RAY DIFFRACTION4A156 - 216

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