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- PDB-2era: RECOMBINANT ERABUTOXIN A, S8G MUTANT -

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Basic information

Entry
Database: PDB / ID: 2era
TitleRECOMBINANT ERABUTOXIN A, S8G MUTANT
ComponentsERABUTOXIN A
KeywordsNEUROTOXIN / SNAKE NEUROTOXIN / VENOM / POSTSYNAPTIC NEUROTOXIN
Function / homology
Function and homology information


acetylcholine receptor inhibitor activity / ion channel regulator activity / toxin activity / extracellular region
Similarity search - Function
Snake three-finger toxin / Snake toxins signature. / Snake toxin, conserved site / CD59 / CD59 / Snake toxin-like superfamily / Ribbon / Mainly Beta
Similarity search - Domain/homology
Biological speciesLaticauda semifasciata (broad-banded blue sea krait)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.81 Å
AuthorsGaucher, J.F. / Menez, R. / Arnoux, B. / Menez, A. / Ducruix, A.
Citation
Journal: Eur.J.Biochem. / Year: 2000
Title: High resolution x-ray analysis of two mutants of a curaremimetic snake toxin
Authors: Gaucher, J.F. / Menez, R. / Arnoux, B. / Menez, A. / Ducruix, A.
#1: Journal: J.Biol.Chem. / Year: 1995
Title: Genetic Engineering of Snake Toxins. The Functional Site of Erabutoxin A, as Delineated by Site-Directed Mutagenesis, Includes Variant Residues
Authors: Tremeau, O. / Lemaire, C. / Drevet, P. / Pinkasfeld, S. / Ducancel, F. / Boulain, J.C. / Menez, A.
#2: Journal: FEBS Lett. / Year: 1994
Title: Three-Dimensional Crystal Structure of Recombinant Erabutoxin a at 2.0 A Resolution
Authors: Arnoux, B. / Menez, R. / Drevet, P. / Boulain, J.C. / Ducruix, A. / Menez, A.
#3: Journal: J.Biol.Chem. / Year: 1993
Title: Genetic Engineering of Snake Toxins. Role of Invariant Residues in the Structural and Functional Properties of a Curaremimetic Toxin, as Probed by Site-Directed Mutagenesis
Authors: Pillet, L. / Tremeau, O. / Ducancel, F. / Drevet, P. / Zinn-Justin, S. / Pinkasfeld, S. / Boulain, J.C. / Menez, A.
#4: Journal: J.Biol.Chem. / Year: 1989
Title: The Crystal Structure of Erabutoxin a at 2.0-A Resolution
Authors: Corfield, P.W. / Lee, T.J. / Low, B.W.
#5: Journal: Acta Crystallogr.,Sect.A / Year: 1988
Title: Refinement at 1.4 A Resolution of a Model of Erabutoxin B: Treatment of Ordered Solvent and Discrete Disorder
Authors: Smith, J.L. / Corfield, P.W.R. / Hendrickson, W.A. / Low, B.W.
History
DepositionJun 25, 1997Processing site: BNL
Revision 1.0Dec 31, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Refinement description / Category: database_2 / software / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _software.name / _struct_ref_seq_dif.details
Revision 1.4Apr 3, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ERABUTOXIN A


Theoretical massNumber of molelcules
Total (without water)6,8241
Polymers6,8241
Non-polymers00
Water1,09961
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)49.650, 46.590, 21.740
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 ERABUTOXIN A


Mass: 6823.689 Da / Num. of mol.: 1 / Mutation: S8G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Laticauda semifasciata (broad-banded blue sea krait)
Variant: TYPE A (N26 AND K51) / Plasmid: PRIT5 / Production host: Escherichia coli (E. coli) / Strain (production host): MC1061 / References: UniProt: P60775
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 61 / 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: 1.8 Å3/Da / Density % sol: 35 %
Crystal growMethod: vapor diffusion, hanging drop / pH: 4.5
Details: CRYSTALLIZATION WERE PERFORMED AT 291K BY THE HANGING DROP METHOD. DROPS OF 2 MICROLITRE OF 0.007M PROTEIN AND 2 MICROLITRE OF RESERVOIR WERE EQUILIBRATED AGAINST 3M NACL, 0.05M NAOAC BUFFER ...Details: CRYSTALLIZATION WERE PERFORMED AT 291K BY THE HANGING DROP METHOD. DROPS OF 2 MICROLITRE OF 0.007M PROTEIN AND 2 MICROLITRE OF RESERVOIR WERE EQUILIBRATED AGAINST 3M NACL, 0.05M NAOAC BUFFER SOLUTION (PH 4.5)., vapor diffusion - hanging drop
Crystal grow
*PLUS
Temperature: 18 ℃ / Method: vapor diffusion
Details: drop solution was mixed with an equal volume of reservoir solution
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
17 mMtoxin1drop
23 M1reservoirNaCl
3250 mM1reservoirNaSCN

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Data collection

DiffractionMean temperature: 278 K
Diffraction sourceSource: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.901
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1993 / Details: MIRRORS
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.901 Å / Relative weight: 1
ReflectionResolution: 1.81→15 Å / Num. obs: 4889 / % possible obs: 99.8 % / Observed criterion σ(I): 3 / Redundancy: 8.4 % / Biso Wilson estimate: 10.8 Å2 / Rsym value: 0.047 / Net I/σ(I): 13
Reflection shellResolution: 1.814→1.86 Å / Redundancy: 5.8 % / Mean I/σ(I) obs: 6.3 / Rsym value: 0.116 / % possible all: 97.6
Reflection
*PLUS
Lowest resolution: 17 Å / Num. obs: 4924 / % possible obs: 99 % / Num. measured all: 41373 / Rmerge(I) obs: 0.047
Reflection shell
*PLUS
% possible obs: 97 % / Rmerge(I) obs: 0.116

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
ROTAVATAAGROVATAdata reduction
AMoREphasing
X-PLOR3.1refinement
CCP4(AGROVATAdata scaling
ROTAVATAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: STRUCTURE OF RECOMBINANT ERABUTOXIN A PROVIDED BY DR.B.ARNOUX

Resolution: 1.81→10 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 100000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
Details: AT THE END OF REFINEMENT THE WHOLE SET OF DATA WAS USED FOR THE LAST STEPS OF REFINEMENT.
RfactorNum. reflection% reflectionSelection details
Rfree0.236 500 10.5 %RANDOM
Rwork0.18 ---
obs0.18 4775 98 %-
Displacement parametersBiso mean: 12.1 Å2
Refine analyzeLuzzati coordinate error obs: 0.18 Å / Luzzati d res low obs: 10 Å / Luzzati sigma a obs: 0.08 Å
Refinement stepCycle: LAST / Resolution: 1.81→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms471 0 0 61 532
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.008
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_deg1.64
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d26.9
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.34
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it1.5
X-RAY DIFFRACTIONx_mcangle_it2
X-RAY DIFFRACTIONx_scbond_it2
X-RAY DIFFRACTIONx_scangle_it2.5
LS refinement shellResolution: 1.81→1.88 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.209 43 9.3 %
Rwork0.193 419 -
obs--95.8 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM11.WATTOPH11.WAT
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg26.9
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.34
LS refinement shell
*PLUS
Rfactor obs: 0.193

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