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- PDB-2wnc: Crystal structure of Aplysia ACHBP in complex with tropisetron -

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Basic information

Entry
Database: PDB / ID: 2wnc
TitleCrystal structure of Aplysia ACHBP in complex with tropisetron
ComponentsSoluble acetylcholine receptor
KeywordsRECEPTOR / CHOLINE-BINDING PROTEIN / ACETYLCHOLINE BINDING PROTEIN
Function / homology
Function and homology information


extracellular ligand-gated monoatomic ion channel activity / transmembrane signaling receptor activity / membrane / identical protein binding / metal ion binding
Similarity search - Function
Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Distorted Sandwich / Mainly Beta
Similarity search - Domain/homology
Chem-TKT / Soluble acetylcholine receptor
Similarity search - Component
Biological speciesAplysia californica (California sea hare)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsSulzenbacher, G. / Hibbs, R. / Shi, J. / Talley, T. / Conrod, S. / Kem, W. / Taylor, P. / Marchot, P. / Bourne, Y.
CitationJournal: EMBO J. / Year: 2009
Title: Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor.
Authors: Hibbs, R.E. / Sulzenbacher, G. / Shi, J. / Talley, T.T. / Conrod, S. / Kem, W.R. / Taylor, P. / Marchot, P. / Bourne, Y.
History
DepositionJul 8, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 1, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Refinement description / Version format compliance
Revision 1.2Jun 13, 2018Group: Data collection / Database references ...Data collection / Database references / Source and taxonomy / Structure summary
Category: citation / entity ...citation / entity / entity_src_gen / struct_ref / struct_ref_seq_dif
Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _entity.pdbx_description / _entity_src_gen.gene_src_common_name / _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_seq_type / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code
Revision 1.3Apr 3, 2019Group: Data collection / Source and taxonomy / Category: entity_src_gen / Item: _entity_src_gen.pdbx_host_org_cell_line
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / 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 / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Soluble acetylcholine receptor
B: Soluble acetylcholine receptor
C: Soluble acetylcholine receptor
D: Soluble acetylcholine receptor
E: Soluble acetylcholine receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)130,68510
Polymers129,2645
Non-polymers1,4225
Water11,007611
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14420 Å2
ΔGint-62.8 kcal/mol
Surface area44600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)212.584, 212.584, 212.584
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number197
Space group name H-MI23

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Components

#1: Protein
Soluble acetylcholine receptor / ACETYLCHOLINE BINDING PROTEIN


Mass: 25852.744 Da / Num. of mol.: 5 / Fragment: RESIDUES 18-236
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aplysia californica (California sea hare)
Cell: SENSORY CELL / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q8WSF8
#2: Chemical
ChemComp-TKT / (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-INDOLE-3-CARBOXYLATE / TROPISETRON / Tropisetron


Mass: 284.353 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C17H20N2O2 / Comment: chemotherapy, antagonist*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 611 / 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: 3.2 Å3/Da / Density % sol: 61 % / Description: NONE
Crystal growDetails: 22% PEG4000, 0.1 M TRIS-HCL PH 7.5, 0.2 M LI2SO4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97915
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 8, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97915 Å / Relative weight: 1
ReflectionResolution: 2.2→87 Å / Num. obs: 80567 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 5.8 % / Biso Wilson estimate: 35.7 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 13.9
Reflection shellResolution: 2.2→2.32 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.4 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BYN

2byn


Resolution: 2.2→75.16 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.933 / SU B: 8.071 / SU ML: 0.112 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.189 / ESU R Free: 0.163 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. GLOBAL B-FACTORS, CONTAINING RESIDUAL AND TLS COMPONENT HAVE BEEN DEPOSITED.
RfactorNum. reflection% reflectionSelection details
Rfree0.21171 2420 3 %RANDOM
Rwork0.17732 ---
obs0.17837 78146 99.95 %-
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: 37.5237 Å2
Refinement stepCycle: LAST / Resolution: 2.2→75.16 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8491 0 105 611 9207
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0229005
X-RAY DIFFRACTIONr_bond_other_d0.0020.026061
X-RAY DIFFRACTIONr_angle_refined_deg1.4641.96612320
X-RAY DIFFRACTIONr_angle_other_deg0.8693.00214765
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.20151110
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.02724.286434
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.935151474
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.4461559
X-RAY DIFFRACTIONr_chiral_restr0.080.21361
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0210037
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021842
X-RAY DIFFRACTIONr_nbd_refined0.1870.21454
X-RAY DIFFRACTIONr_nbd_other0.2050.26330
X-RAY DIFFRACTIONr_nbtor_refined0.1780.24253
X-RAY DIFFRACTIONr_nbtor_other0.0870.24926
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1530.2566
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1830.210
X-RAY DIFFRACTIONr_symmetry_vdw_other0.250.220
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.180.27
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9851.56982
X-RAY DIFFRACTIONr_mcbond_other0.1611.52137
X-RAY DIFFRACTIONr_mcangle_it1.17528874
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.95134277
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.7784.53421
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.2→2.257 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.268 184 -
Rwork0.218 5778 -
obs--100 %
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)
11.6188-0.1633-0.03361.9862-0.16712.08980.05910.17540.1557-0.2006-0.03870.0399-0.155-0.0388-0.0204-0.1728-0.01310.0432-0.20450.0266-0.1492-73.335-28.91-75.285
21.8406-0.30230.03321.3491-0.31711.85060.10830.15560.2012-0.03820.00370.2336-0.2266-0.1049-0.112-0.0158-0.01240.0675-0.22460.02170.0102-92.275-12.087-67.651
32.59270.3250.35691.97820.13582.05210.01160.15920.1989-0.09190.0250.3744-0.1727-0.2189-0.0366-0.10720.04970.1031-0.18930.0472-0.0016-111.342-25.929-55.349
42.08930.01360.05141.54280.18271.38540.02580.1533-0.1781-0.0670.00640.18580.1335-0.1498-0.0322-0.15470.00640.0481-0.18440.031-0.1013-104.324-51.684-55.47
51.2983-0.0384-0.11821.2576-0.07762.80610.00360.1699-0.1173-0.1263-0.02040.04910.0773-0.08240.0169-0.20290.02050.0086-0.21540.0056-0.1512-80.837-53.518-68.095
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-4 - 209
2X-RAY DIFFRACTION2B-4 - 208
3X-RAY DIFFRACTION3C-2 - 209
4X-RAY DIFFRACTION4D-2 - 210
5X-RAY DIFFRACTION5E-4 - 208

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