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- PDB-8pgw: Crystal structure of the metallo-beta-lactamase VIM1 with 3460 -

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Basic information

Entry
Database: PDB / ID: 8pgw
TitleCrystal structure of the metallo-beta-lactamase VIM1 with 3460
ComponentsBeta-lactamase VIM-1
KeywordsANTIMICROBIAL PROTEIN / Complex / metallo-beta-lactamase / inhibitor / zinc / indole carboxylate
Function / homology: / : / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like / metal ion binding / : / Beta-lactamase VIM-1
Function and homology information
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsCalvopina, K. / Brem, J. / Farley, A.J.M. / Allen, M.D. / Schofield, C.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome Trust099141/Z/12/Z United Kingdom
CitationJournal: To Be Published
Title: Crystal structure of the metallo-beta-lactamase VIM1 with 3460
Authors: Calvopina, K. / Brem, J. / Farley, A.J.M. / Allen, M.D. / Schofield, C.J.
History
DepositionJun 18, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 10, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Beta-lactamase VIM-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,6494
Polymers28,0511
Non-polymers5973
Water5,242291
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area200 Å2
ΔGint-79 kcal/mol
Surface area9670 Å2
Unit cell
Length a, b, c (Å)39.430, 68.040, 40.340
Angle α, β, γ (deg.)90.000, 93.530, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

#1: Protein Beta-lactamase VIM-1 / Class B carbapenemase VIM-1 / Metallo-beta-lactamase / Metallo-beta-lactamase VIM-1 / Metallobeta- ...Class B carbapenemase VIM-1 / Metallo-beta-lactamase / Metallo-beta-lactamase VIM-1 / Metallobeta-lactamase / Subclass B1 metallo-beta-lactamase VIM-1 / VIM-1 / VIM-1 metallo-beta-lactamase / VIM-1 protein


Mass: 28051.371 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Gene: blaVIM, blaVIM-1, CAZ10_38240, CAZ10_38245 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q9XAY4
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-YRK / 7-[(1~{S})-1-[2-(aminomethyl)-6-oxidanylidene-5-oxa-7-azaspiro[3.4]octan-7-yl]ethyl]-3-(5-methoxy-6-oxidanyl-pyridin-3-yl)-1~{H}-indole-2-carboxylic acid


Mass: 466.486 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H26N4O6 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 291 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 1.93 Å3/Da / Density % sol: 36.12 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 / Details: ammonium / PH range: 8.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.81564 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jul 16, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.81564 Å / Relative weight: 1
ReflectionResolution: 1.5→40.26 Å / Num. obs: 34097 / % possible obs: 100 % / Redundancy: 7 % / Biso Wilson estimate: 14.58 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.083 / Rpim(I) all: 0.034 / Rrim(I) all: 0.09 / Net I/σ(I): 13.1
Reflection shellResolution: 1.5→1.54 Å / Redundancy: 7 % / Rmerge(I) obs: 0.771 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 2511 / CC1/2: 0.789 / Rpim(I) all: 0.313 / Rrim(I) all: 0.833 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
xia2data reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.5→40.26 Å / SU ML: 0.1311 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 16.3693
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1782 1745 5.12 %
Rwork0.1506 32326 -
obs0.152 34071 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 18.7 Å2
Refinement stepCycle: LAST / Resolution: 1.5→40.26 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1731 0 36 291 2058
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00542028
X-RAY DIFFRACTIONf_angle_d0.92962804
X-RAY DIFFRACTIONf_chiral_restr0.0541312
X-RAY DIFFRACTIONf_plane_restr0.0182380
X-RAY DIFFRACTIONf_dihedral_angle_d9.6308313
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5-1.540.22881180.18682730X-RAY DIFFRACTION99.96
1.54-1.590.20941400.17522659X-RAY DIFFRACTION99.93
1.59-1.650.23861420.17282710X-RAY DIFFRACTION100
1.65-1.720.18461520.16122673X-RAY DIFFRACTION100
1.72-1.80.21441550.14092674X-RAY DIFFRACTION100
1.8-1.890.20021210.13532704X-RAY DIFFRACTION100
1.89-2.010.16711650.13252668X-RAY DIFFRACTION99.93
2.01-2.160.15441730.12712646X-RAY DIFFRACTION99.96
2.16-2.380.16531540.13342689X-RAY DIFFRACTION100
2.38-2.730.15821450.14362717X-RAY DIFFRACTION99.86
2.73-3.430.18421210.15232720X-RAY DIFFRACTION100
3.43-40.260.17541590.16592736X-RAY DIFFRACTION99.93

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