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- PDB-5o8f: Structure of a chimaeric beta3-alpha5 GABAA receptor in complex w... -

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Basic information

Entry
Database: PDB / ID: 5o8f
TitleStructure of a chimaeric beta3-alpha5 GABAA receptor in complex with nanobody Nb25 and pregnanolone
Components
  • (Nanobody Nb25) x 2
  • Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
KeywordsMEMBRANE PROTEIN / GABAA receptor / Pregnanolone / Nanobody complex / Neurosteroid / Ion channel
Function / homology
Function and homology information


inhibitory extracellular ligand-gated monoatomic ion channel activity / GABA receptor activation / inner ear receptor cell development / GABA-gated chloride ion channel activity / cellular response to histamine / inhibitory synapse assembly / GABA-A receptor activity / GABA-A receptor complex / GABA receptor binding / innervation ...inhibitory extracellular ligand-gated monoatomic ion channel activity / GABA receptor activation / inner ear receptor cell development / GABA-gated chloride ion channel activity / cellular response to histamine / inhibitory synapse assembly / GABA-A receptor activity / GABA-A receptor complex / GABA receptor binding / innervation / postsynaptic specialization membrane / neurotransmitter receptor activity / synaptic transmission, GABAergic / gamma-aminobutyric acid signaling pathway / neuronal cell body membrane / cochlea development / roof of mouth development / Signaling by ERBB4 / associative learning / chloride channel complex / GABA-ergic synapse / regulation of postsynaptic membrane potential / behavioral fear response / chloride transmembrane transport / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cytoplasmic vesicle membrane / signaling receptor activity / presynaptic membrane / postsynapse / postsynaptic membrane / neuron projection / synapse / signal transduction / nucleoplasm / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Gamma-aminobutyric-acid A receptor, alpha 5 subunit / Gamma-aminobutyric-acid A receptor, beta subunit / : / Gamma-aminobutyric-acid A receptor, alpha subunit / Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. ...Gamma-aminobutyric-acid A receptor, alpha 5 subunit / Gamma-aminobutyric-acid A receptor, beta subunit / : / Gamma-aminobutyric-acid A receptor, alpha subunit / Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / 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 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Distorted Sandwich / Up-down Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Pregnanolone / Gamma-aminobutyric acid receptor subunit beta-3 / Gamma-aminobutyric acid receptor subunit alpha-5
Similarity search - Component
Biological speciesHomo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsMiller, P.S. / Scott, S. / Masiulis, S. / De Colibus, L. / Pardon, E. / Steyaert, J. / Aricescu, A.R.
Funding support United Kingdom, France, 6items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research CouncilBB/M024709/1 United Kingdom
Medical Research Council (United Kingdom)MR/L009609/1 United Kingdom
Medical Research Council (United Kingdom)MC_UP_1201/15 United Kingdom
Wellcome Trust105247/Z/14/Z United Kingdom
Human Frontier Science ProgramRGP0065/2014 France
Wellcome Trust090532/Z/09/Z United Kingdom
CitationJournal: Nat. Struct. Mol. Biol. / Year: 2017
Title: Structural basis for GABAA receptor potentiation by neurosteroids.
Authors: Miller, P.S. / Scott, S. / Masiulis, S. / De Colibus, L. / Pardon, E. / Steyaert, J. / Aricescu, A.R.
History
DepositionJun 13, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 1, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
B: Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
C: Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
D: Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
E: Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5
K: Nanobody Nb25
L: Nanobody Nb25
M: Nanobody Nb25
N: Nanobody Nb25
O: Nanobody Nb25
hetero molecules


Theoretical massNumber of molelcules
Total (without water)285,31725
Polymers276,44310
Non-polymers8,87415
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area47110 Å2
ΔGint-92 kcal/mol
Surface area84190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)290.102, 290.102, 290.102
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number197
Space group name H-MI23
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15B
25C
16B
26D
17B
27E
18C
28D
19C
29E
110D
210E
111O
211N
112O
212M
113O
213L
114O
214K
115N
215M
116N
216L
117N
217K
118M
218L
119M
219K
120L
220K

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11METMETLEULEUAA9 - 41812 - 343
21METMETLEULEUBB9 - 41812 - 343
12METMETLEULEUAA9 - 41812 - 343
22METMETLEULEUCC9 - 41812 - 343
13METMETLEULEUAA9 - 41812 - 343
23METMETLEULEUDD9 - 41812 - 343
14METMETLEULEUAA9 - 41812 - 343
24METMETLEULEUEE9 - 41812 - 343
15METMETLEULEUBB9 - 41812 - 343
25METMETLEULEUCC9 - 41812 - 343
16METMETLEULEUBB9 - 41812 - 343
26METMETLEULEUDD9 - 41812 - 343
17METMETLEULEUBB9 - 41812 - 343
27METMETLEULEUEE9 - 41812 - 343
18METMETLEULEUCC9 - 41812 - 343
28METMETLEULEUDD9 - 41812 - 343
19METMETLEULEUCC9 - 41812 - 343
29METMETLEULEUEE9 - 41812 - 343
110METMETLEULEUDD9 - 41812 - 343
210METMETLEULEUEE9 - 41812 - 343
111GLNGLNVALVALOJ1 - 1231 - 123
211GLNGLNVALVALNI1 - 1231 - 123
112GLNGLNVALVALOJ1 - 1231 - 123
212GLNGLNVALVALMH1 - 1231 - 123
113GLNGLNVALVALOJ1 - 1231 - 123
213GLNGLNVALVALLG1 - 1231 - 123
114GLNGLNSERSEROJ1 - 1251 - 125
214GLNGLNSERSERKF1 - 1251 - 125
115GLNGLNSERSERNI1 - 1241 - 124
215GLNGLNSERSERMH1 - 1241 - 124
116GLNGLNSERSERNI1 - 1241 - 124
216GLNGLNSERSERLG1 - 1241 - 124
117GLNGLNVALVALNI1 - 1231 - 123
217GLNGLNVALVALKF1 - 1231 - 123
118GLNGLNSERSERMH1 - 1241 - 124
218GLNGLNSERSERLG1 - 1241 - 124
119GLNGLNVALVALMH1 - 1231 - 123
219GLNGLNVALVALKF1 - 1231 - 123
120GLNGLNVALVALLG1 - 1231 - 123
220GLNGLNVALVALKF1 - 1231 - 123

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20

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Components

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Antibody , 2 types, 5 molecules KOLMN

#2: Antibody Nanobody Nb25


Mass: 13673.024 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Plasmid: pMESy4 / Production host: Escherichia coli (E. coli)
#3: Antibody Nanobody Nb25


Mass: 13585.947 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Plasmid: pMESy4 / Production host: Escherichia coli (E. coli)

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Protein / Non-polymers , 2 types, 10 molecules ABCDE

#1: Protein
Gamma-aminobutyric acid receptor subunit beta-3,Gamma-aminobutyric acid receptor subunit alpha-5,Gamma-aminobutyric acid receptor subunit alpha-5 / GABA(A) receptor subunit beta-3 / GABA(A) receptor subunit alpha-5 / GABA(A) receptor subunit alpha-5


Mass: 41667.887 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Details: This is a chimaeric construct, containing the secretion signal sequence from pHLsec vector (PMID: 17001101), the extracellular region of human GBRB3 (mature polypeptide residues 1-217 from ...Details: This is a chimaeric construct, containing the secretion signal sequence from pHLsec vector (PMID: 17001101), the extracellular region of human GBRB3 (mature polypeptide residues 1-217 from Uniprot P28472), the transmembrane region from human GBRA5 (mature polypeptide residues 226-431 from Uniprot P31644 with the exception of the M3-M4 loop, residues 316-392, which were substituted by SQPARAA) and a C-terminal Rho-1D4 purification tag (TETSQVAPA).
Source: (gene. exp.) Homo sapiens (human) / Gene: GABRB3, GABRA5 / Plasmid: pHLsec / Cell line (production host): HEK-293S GnTI- / Production host: Homo sapiens (human) / References: UniProt: P28472, UniProt: P31644
#6: Chemical
ChemComp-P9N / Pregnanolone / (3alpha,5beta)-3-Hydroxypregnan-20-one / Pregnanolone


Mass: 318.493 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C21H34O2 / Comment: inhibitor*YM

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Sugars , 2 types, 10 molecules

#4: Polysaccharide
alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_f2-g1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}}}}}LINUCSPDB-CARE
#5: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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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: 3.5 Å3/Da / Density % sol: 64.9 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 14% PEG 6000, 0.1M N-(2-Acetamido)iminodiacetic acid (ADA), 7.6 mM 4-Cyclohexyl-1-Butyl-beta-D-Maltoside (CYMAL-4)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jul 26, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 3.19→49.752 Å / Num. obs: 66928 / % possible obs: 100 % / Redundancy: 30.4 % / Biso Wilson estimate: 68.2 Å2 / CC1/2: 0.986 / Rmerge(I) obs: 0.621 / Rpim(I) all: 0.131 / Net I/σ(I): 6.8
Reflection shellResolution: 3.19→3.31 Å / Redundancy: 25.5 % / Rmerge(I) obs: 3.131 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 6677 / CC1/2: 0.215 / Rpim(I) all: 0.609 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
HKL-2000data reduction
Aimless0.5.25data scaling
PHASER2.5.7phasing
Coot0.8.8model building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4COF

4cof


Resolution: 3.2→205.13 Å / Cor.coef. Fo:Fc: 0.896 / Cor.coef. Fo:Fc free: 0.884 / SU B: 60.029 / SU ML: 0.414 / Cross valid method: THROUGHOUT / ESU R Free: 0.428 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2424 3304 4.9 %RANDOM
Rwork0.23246 ---
obs0.23296 63621 99.96 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 70.752 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: 1 / Resolution: 3.2→205.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18217 0 600 0 18817
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01919337
X-RAY DIFFRACTIONr_bond_other_d0.0020.0217713
X-RAY DIFFRACTIONr_angle_refined_deg1.1211.93126301
X-RAY DIFFRACTIONr_angle_other_deg0.895340890
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.45252272
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.3322.738840
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.369153032
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.66415140
X-RAY DIFFRACTIONr_chiral_restr0.0610.23022
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0220869
X-RAY DIFFRACTIONr_gen_planes_other0.0020.024267
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_it1.0955.2129118
X-RAY DIFFRACTIONr_mcbond_other1.0955.2129117
X-RAY DIFFRACTIONr_mcangle_it1.9157.81811380
X-RAY DIFFRACTIONr_mcangle_other1.9157.81811381
X-RAY DIFFRACTIONr_scbond_it1.1645.43110218
X-RAY DIFFRACTIONr_scbond_other1.1645.43110219
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.0028.09114922
X-RAY DIFFRACTIONr_long_range_B_refined5.23798.99676095
X-RAY DIFFRACTIONr_long_range_B_other5.23798.99676096
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A219360.05
12B219360.05
21A219300.05
22C219300.05
31A218660.05
32D218660.05
41A219360.05
42E219360.05
51B219560.04
52C219560.04
61B219000.05
62D219000.05
71B219880.05
72E219880.05
81C220420.04
82D220420.04
91C218580.05
92E218580.05
101D218640.05
102E218640.05
111O73140.07
112N73140.07
121O72660.07
122M72660.07
131O72740.06
132L72740.06
141O73800.07
142K73800.07
151N72780.08
152M72780.08
161N72680.08
162L72680.08
171N72560.08
172K72560.08
181M72400.08
182L72400.08
191M72520.07
192K72520.07
201L71860.07
202K71860.07
LS refinement shellResolution: 3.195→3.278 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.36 214 -
Rwork0.372 4695 -
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)
11.87970.13681.42060.39890.20972.25040.0389-0.0077-0.01620.0413-0.09040.14220.2989-0.10610.05150.1226-0.01980.02730.0264-0.03380.054635.9123278.7602382.2627
21.4058-0.36051.1420.7817-0.50881.7413-0.0871-0.14070.26690.0569-0.10820.150.0428-0.20570.19520.08810.00120.03480.1093-0.05670.144937.4752303.9261381.2973
30.991-0.23690.70260.5092-0.50452.7765-0.01460.07670.26350.0162-0.08370.0295-0.11040.09250.09830.1225-0.02580.01510.03270.00070.092158.2877309.9506368.276
41.00440.03580.85320.59220.20312.94950.01520.1460.1472-0.1254-0.0884-0.0710.08440.25150.07310.0948-0.01440.03710.08730.0180.038369.5982288.4662361.2634
51.45520.44871.34930.72530.63682.69750.03560.0824-0.0668-0.0639-0.0397-0.02620.28190.09330.00410.11690.02980.04140.0427-0.00930.030455.7599269.1941369.9225
64.12452.5276-1.45734.1441-0.4693.74920.0229-0.1549-0.0260.4141-0.04210.13310.0884-0.07270.01920.30140.0313-0.0660.0346-0.01560.047733.6776249.9818380.6329
72.1277-1.3359-0.95565.0849-0.27882.9613-0.1193-0.1056-0.29620.3192-0.0465-0.02190.22150.2010.16580.13290.06130.01050.2930.00240.053777.2709259.5546353.4804
84.6405-0.156-1.84113.1541-0.68943.7-0.1426-0.1703-0.08010.088-0.0256-0.53220.05150.22170.16820.0998-0.039-0.05990.18930.04810.11982.9362311.3759349.8029
94.40120.3219-0.05075.231-1.00211.8980.113-0.29760.34820.1843-0.0301-0.5138-0.21440.2577-0.08280.16210.0269-0.0550.1293-0.070.136142.9615333.5988374.7114
105.4952-0.6591-1.20473.98041.31772.67260.042-0.30930.33740.32620.00840.054-0.12250.0163-0.05040.1095-0.057-0.01690.1803-0.02220.044412.3127295.8199393.7183
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 508
2X-RAY DIFFRACTION2B9 - 508
3X-RAY DIFFRACTION3C9 - 508
4X-RAY DIFFRACTION4D9 - 508
5X-RAY DIFFRACTION5E9 - 508
6X-RAY DIFFRACTION6O1 - 125
7X-RAY DIFFRACTION7N1 - 124
8X-RAY DIFFRACTION8M1 - 124
9X-RAY DIFFRACTION9L1 - 124
10X-RAY DIFFRACTION10K1 - 125

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