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- PDB-5aoh: Crystal Structure of CarF -

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Basic information

Entry
Database: PDB / ID: 5aoh
TitleCrystal Structure of CarF
ComponentsSpore coat protein CotH
KeywordsUNKNOWN FUNCTION / CARBAPENEM RESISTANCE / ANTIBIOTIC RESISTANCE / FGE HOMOLOGUE
Function / homologySulfatase-modifying factor enzyme / Sulfatase-modifying factor enzyme 1 / Sulfatase-modifying factor enzyme superfamily / C-type lectin fold / : / Spore coat protein CotH
Function and homology information
Biological speciesSerratia sp. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsTichy, E.M. / Hardwick, S.W. / Luisi, B.F. / C Salmond, G.P.
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2017
Title: 1.8 angstrom resolution crystal structure of the carbapenem intrinsic resistance protein CarF.
Authors: Tichy, E.M. / Hardwick, S.W. / Luisi, B.F. / Salmond, G.P.C.
History
DepositionSep 10, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 25, 2017Provider: repository / Type: Initial release
Revision 1.1Jul 19, 2017Group: Database references / Category: citation
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Sep 25, 2019Group: Data collection / Database references ...Data collection / Database references / Other / Source and taxonomy / Structure summary
Category: entity / entity_src_gen ...entity / entity_src_gen / pdbx_database_status / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity_src_gen.gene_src_strain ..._entity.pdbx_description / _entity_src_gen.gene_src_strain / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _pdbx_database_status.status_code_sf / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq_dif.pdbx_seq_db_accession_code

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Spore coat protein CotH
B: Spore coat protein CotH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,9664
Polymers59,8882
Non-polymers782
Water5,495305
1
A: Spore coat protein CotH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9832
Polymers29,9441
Non-polymers391
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Spore coat protein CotH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9832
Polymers29,9441
Non-polymers391
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)49.470, 55.450, 176.200
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 Spore coat protein CotH


Mass: 29944.049 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Serratia sp. (strain ATCC 39006) (bacteria)
Strain: ATCC 39006 / Gene: Ser39006_009945 / Plasmid: PQE80ORIT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A0A2I5TIN5
#2: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 305 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.6 % / Description: NONE

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Data collection

DiffractionMean temperature: 180 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.978
DetectorType: DECTRIS PILATUS / Detector: PIXEL / Date: Jun 27, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 1.8→36.13 Å / Num. obs: 44709 / % possible obs: 97.5 % / Observed criterion σ(I): 2 / Redundancy: 3.2 % / Rmerge(I) obs: 0.09
Reflection shellResolution: 1.8→1.84 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.41 / % possible all: 99.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0131refinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→88.1 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.942 / SU B: 6.963 / SU ML: 0.095 / Cross valid method: THROUGHOUT / ESU R: 0.266 / ESU R Free: 0.122 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.20813 2185 4.9 %RANDOM
Rwork0.13675 ---
obs0.14025 42457 97.17 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 25.387 Å2
Baniso -1Baniso -2Baniso -3
1--0.21 Å20 Å20 Å2
2---1.37 Å20 Å2
3---1.58 Å2
Refinement stepCycle: LAST / Resolution: 1.8→88.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3980 0 2 305 4287
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0194099
X-RAY DIFFRACTIONr_bond_other_d0.0120.023638
X-RAY DIFFRACTIONr_angle_refined_deg1.8781.9325593
X-RAY DIFFRACTIONr_angle_other_deg1.87638359
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.1385525
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.44424.301186
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.55415575
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.1121517
X-RAY DIFFRACTIONr_chiral_restr0.1160.2584
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.0214829
X-RAY DIFFRACTIONr_gen_planes_other0.0090.02992
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_it4.4212.3492103
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it5.1093.5262624
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr5.79534097
X-RAY DIFFRACTIONr_sphericity_free43.848562
X-RAY DIFFRACTIONr_sphericity_bonded27.92454223
LS refinement shellResolution: 1.8→1.847 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.255 133 -
Rwork0.187 3183 -
obs--98.84 %

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