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- PDB-1rf2: Cholera Toxin B-Pentamer Complexed With Bivalent Nitrophenol-Gala... -

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Basic information

Entry
Database: PDB / ID: 1rf2
TitleCholera Toxin B-Pentamer Complexed With Bivalent Nitrophenol-Galactoside Ligand BV4
Componentscholera toxin B protein (CTB)
KeywordsTOXIN / Bivalent / Cholera / Pentamer / Complex
Function / homology
Function and homology information


host cell surface binding / galactose binding / catalytic complex / positive regulation of tyrosine phosphorylation of STAT protein / toxin activity / periplasmic space / host cell plasma membrane / extracellular region / membrane
Similarity search - Function
Heat-labile enterotoxin, B chain / Heat-labile enterotoxin beta chain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #110 / Enterotoxin / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Chem-BV4 / TRIETHYLENE GLYCOL / Cholera enterotoxin subunit B
Similarity search - Component
Biological speciesVibrio cholerae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.35 Å
AuthorsPickens, J.C. / Mitchell, D.D. / Liu, J. / Tan, X. / Zhang, Z. / Verlinde, C.L. / Hol, W.G. / Fan, E.
CitationJournal: Chem.Biol. / Year: 2004
Title: Nonspanning bivalent ligands as improved surface receptor binding inhibitors of the cholera toxin B pentamer.
Authors: Pickens, J.C. / Mitchell, D.D. / Liu, J. / Tan, X. / Zhang, Z. / Verlinde, C.L. / Hol, W.G. / Fan, E.
History
DepositionNov 7, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 26, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 23, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: cholera toxin B protein (CTB)
E: cholera toxin B protein (CTB)
F: cholera toxin B protein (CTB)
G: cholera toxin B protein (CTB)
H: cholera toxin B protein (CTB)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,36312
Polymers58,1165
Non-polymers9,2477
Water8,971498
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15730 Å2
ΔGint-85 kcal/mol
Surface area20230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.235, 66.028, 78.642
Angle α, β, γ (deg.)90.00, 105.80, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11F-1321-

HOH

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Components

#1: Protein
cholera toxin B protein (CTB)


Mass: 11623.267 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria) / Gene: ctxB / Plasmid: pBAD / Production host: Escherichia coli (E. coli) / Strain (production host): Top10 / References: UniProt: P01556
#2: Chemical
ChemComp-BV4 / 1,3-BIS-([3-[3-[3-(4-{3-[3-NITRO-5-(GALACTOPYRANOSYLOXY)-BENZOYLAMINO]-PROPYL}-PIPERAZIN-1-YL)-PROPYLAMINO-3,4-DIOXO-CYCLOBUTENYL]-AMINO-PROPOXY-ETHOXY-ETHOXY]-PROPYL-]AMINO-CARBONYLOXY)-2-AMINO-PROPANE / BV4


Mass: 1794.903 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C79H123N15O32
#3: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER / Tris


Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#4: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 498 / 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: 44.01 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 16% PEG 8000, 50 mM NaCl, 100 mM Tris-HCl, 20mM MgCl2, and 2.3mM BV4, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 0.9626 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 29, 2003
RadiationMonochromator: Double-crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9626 Å / Relative weight: 1
ReflectionResolution: 1.35→50 Å / Num. all: 111363 / Num. obs: 104314 / % possible obs: 94.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Biso Wilson estimate: 13.4 Å2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 13.5
Reflection shellResolution: 1.35→1.4 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.591 / Mean I/σ(I) obs: 1.8 / Num. unique all: 7606 / % possible all: 69.3

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
XTALVIEWrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3CHB

3chb


Resolution: 1.35→49.39 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.971 / SU B: 0.934 / SU ML: 0.037 / Isotropic thermal model: Anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.053 / ESU R Free: 0.053 / Stereochemistry target values: Engh & Huber
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS, Maximum Likelihood
RfactorNum. reflection% reflectionSelection details
Rfree0.17389 5219 5 %RANDOM
Rwork0.13232 ---
all0.13439 104314 --
obs0.13439 104314 93.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 10.455 Å2
Baniso -1Baniso -2Baniso -3
1-0.04 Å20 Å20.03 Å2
2---0.06 Å20 Å2
3---0.04 Å2
Refinement stepCycle: LAST / Resolution: 1.35→49.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4074 0 138 498 4710
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0224290
X-RAY DIFFRACTIONr_bond_other_d0.0010.023717
X-RAY DIFFRACTIONr_angle_refined_deg1.4171.9755808
X-RAY DIFFRACTIONr_angle_other_deg0.8623.0018706
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.9545510
X-RAY DIFFRACTIONr_chiral_restr0.0860.2677
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.024624
X-RAY DIFFRACTIONr_gen_planes_other0.0080.02760
X-RAY DIFFRACTIONr_nbd_refined0.220.3802
X-RAY DIFFRACTIONr_nbd_other0.2980.34668
X-RAY DIFFRACTIONr_nbtor_other0.0860.52229
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.160.5610
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.230.316
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3480.339
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2650.521
X-RAY DIFFRACTIONr_mcbond_it2.48532576
X-RAY DIFFRACTIONr_mcangle_it3.39844178
X-RAY DIFFRACTIONr_scbond_it5.23761714
X-RAY DIFFRACTIONr_scangle_it7.19481630
X-RAY DIFFRACTIONr_rigid_bond_restr2.12134290
X-RAY DIFFRACTIONr_sphericity_free21.15115498
X-RAY DIFFRACTIONr_sphericity_bonded6.669154212
LS refinement shellResolution: 1.347→1.382 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.304 260 -
Rwork0.236 5046 -
obs-5046 64.75 %

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