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- PDB-5oew: Crystal structure of the GluA2 ligand-binding domain (S1S2J) in c... -

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Basic information

Entry
Database: PDB / ID: 5oew
TitleCrystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538
ComponentsGlutamate receptor 2
KeywordsMEMBRANE PROTEIN / Ionotropic glutamate receptor GluA2. ligand-binding domain / positive allosteric modulator
Function / homology
Function and homology information


spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / perisynaptic space / AMPA glutamate receptor activity / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / immunoglobulin binding ...spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / perisynaptic space / AMPA glutamate receptor activity / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / immunoglobulin binding / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / cellular response to glycine / extracellularly glutamate-gated ion channel activity / asymmetric synapse / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of synaptic transmission / glutamate receptor binding / glutamate-gated receptor activity / regulation of synaptic transmission, glutamatergic / response to fungicide / cytoskeletal protein binding / ionotropic glutamate receptor binding / presynaptic active zone membrane / extracellular ligand-gated monoatomic ion channel activity / somatodendritic compartment / glutamate-gated calcium ion channel activity / cellular response to brain-derived neurotrophic factor stimulus / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / dendrite membrane / dendrite cytoplasm / ionotropic glutamate receptor signaling pathway / SNARE binding / dendritic shaft / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / PDZ domain binding / protein tetramerization / establishment of protein localization / synaptic membrane / modulation of chemical synaptic transmission / postsynaptic density membrane / terminal bouton / Schaffer collateral - CA1 synapse / cerebral cortex development / receptor internalization / synaptic vesicle membrane / synaptic vesicle / presynapse / signaling receptor activity / amyloid-beta binding / presynaptic membrane / growth cone / scaffold protein binding / chemical synaptic transmission / dendritic spine / perikaryon / postsynaptic membrane / neuron projection / postsynaptic density / axon / neuronal cell body / synapse / dendrite / protein-containing complex binding / protein kinase binding / glutamatergic synapse / cell surface / endoplasmic reticulum / protein-containing complex / identical protein binding / membrane / plasma membrane
Similarity search - Function
Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region ...Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like II / Periplasmic binding protein-like I / D-Maltodextrin-Binding Protein; domain 2 / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-9TE / ACETATE ION / GLUTAMIC ACID / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsLarsen, A.P. / Frydenvang, K.A. / Kastrup, J.S.
Citation
Journal: J. Med. Chem. / Year: 2018
Title: 7-Phenoxy-Substituted 3,4-Dihydro-2H-1,2,4-benzothiadiazine 1,1-Dioxides as Positive Allosteric Modulators of alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors with Nanomolar Potency.
Authors: Goffin, E. / Drapier, T. / Larsen, A.P. / Geubelle, P. / Ptak, C.P. / Laulumaa, S. / Rovinskaja, K. / Gilissen, J. / Tullio, P. / Olsen, L. / Frydenvang, K. / Pirotte, B. / Hanson, J. / ...Authors: Goffin, E. / Drapier, T. / Larsen, A.P. / Geubelle, P. / Ptak, C.P. / Laulumaa, S. / Rovinskaja, K. / Gilissen, J. / Tullio, P. / Olsen, L. / Frydenvang, K. / Pirotte, B. / Hanson, J. / Oswald, R.E. / Kastrup, J.S. / Francotte, P.
#1: Journal: J. Med. Chem. / Year: 2013
Title: Synthesis, pharmacological and structural characterization, and thermodynamic aspects of GluA2-positive allosteric modulators with a 3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide scaffold.
Authors: Norholm, A.B. / Francotte, P. / Olsen, L. / Krintel, C. / Frydenvang, K. / Goffin, E. / Challal, S. / Danober, L. / Botez-Pop, I. / Lestage, P. / Pirotte, B. / Kastrup, J.S.
History
DepositionJul 10, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 3, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2Jan 17, 2024Group: 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 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_alt_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _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
Revision 1.3Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glutamate receptor 2
B: Glutamate receptor 2
C: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,31929
Polymers87,8363
Non-polymers2,48226
Water9,386521
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A: Glutamate receptor 2
B: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,90516
Polymers58,5572
Non-polymers1,34714
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3190 Å2
ΔGint-203 kcal/mol
Surface area23460 Å2
MethodPISA
2
C: Glutamate receptor 2
hetero molecules

C: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,82726
Polymers58,5572
Non-polymers2,27024
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_765-x+2,-y+1,z1
Buried area4090 Å2
ΔGint-337 kcal/mol
Surface area23720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)114.702, 164.374, 47.328
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid 3 and (name O or name...
21(chain B and (resseq 3:18 or resseq 20 or resseq...
31(chain C and ((resid 3 and (name O or name...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNASNASN(chain A and ((resid 3 and (name O or name...AA33
12GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
13GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
14GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
15GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
16GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
17GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
18GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
19GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
110GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
111GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
112GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
113GLYGLYCYSCYS(chain A and ((resid 3 and (name O or name...AA1 - 2611 - 261
21ASNASNMETMET(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 183 - 18
22LYSLYSLYSLYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB2020
23LEULEUASNASN(chain B and (resseq 3:18 or resseq 20 or resseq...BB26 - 2926 - 29
24ARGARGGLUGLU(chain B and (resseq 3:18 or resseq 20 or resseq...BB31 - 4231 - 42
25ALAALAALAALA(chain B and (resseq 3:18 or resseq 20 or resseq...BB4444
26HISHISHISHIS(chain B and (resseq 3:18 or resseq 20 or resseq...BB4646
27ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
28ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
29ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
210ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
211ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
212ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
213ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
214ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
215ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
216ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
217ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
218ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
219ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
220ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
221ASNASNCYSCYS(chain B and (resseq 3:18 or resseq 20 or resseq...BB3 - 2613 - 261
31ASNASNASNASN(chain C and ((resid 3 and (name O or name...CC33
32GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
33GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
34GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
35GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
36GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
37GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
38GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
39GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
310GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
311GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
312GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261
313GLYGLYCYSCYS(chain C and ((resid 3 and (name O or name...CC1 - 2611 - 261

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein Glutamate receptor 2 / GluR-2 / AMPA-selective glutamate receptor 2 / GluR-B / GluR-K2 / Glutamate receptor ionotropic / ...GluR-2 / AMPA-selective glutamate receptor 2 / GluR-B / GluR-K2 / Glutamate receptor ionotropic / AMPA 2 / GluA2


Mass: 29278.732 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: Ligand-binding domain, UNP residues 413-527 and 653-797 connected by a GT linker (numbering including signal peptide)
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Production host: Escherichia coli (E. coli) / References: UniProt: P19491

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Non-polymers , 5 types, 547 molecules

#2: Chemical ChemComp-GLU / GLUTAMIC ACID


Type: L-peptide linking / Mass: 147.129 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C5H9NO4
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: Zn
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#5: Chemical ChemComp-9TE / 4-cyclopropyl-7-(3-methoxyphenoxy)-2,3-dihydro-1$l^{6},2,4-benzothiadiazine 1,1-dioxide


Mass: 346.401 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H18N2O4S / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 521 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.54 Å3/Da / Density % sol: 51.57 %
Crystal growTemperature: 279 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 18% PEG4000, 0.23M lithium-sulfate, 0.1M phosphate-citrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 14, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→29.27 Å / Num. all: 61361 / Num. obs: 61361 / % possible obs: 99.8 % / Redundancy: 4.1 % / Biso Wilson estimate: 20.77 Å2 / Rpim(I) all: 0.046 / Rrim(I) all: 0.099 / Rsym value: 0.087 / Net I/av σ(I): 6.5 / Net I/σ(I): 10.3 / Num. measured all: 253105
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsRpim(I) allRrim(I) allRsym value% possible all
2-2.114.10.31320.1720.3590.313100
2.11-2.244.20.2183.20.1180.2490.218100
2.24-2.394.10.1753.90.0950.20.175100
2.39-2.584.20.13850.0750.1580.138100
2.58-2.834.10.1076.30.0570.1230.107100
2.83-3.164.10.0837.70.0430.0950.083100
3.16-3.654.10.0688.90.0350.0780.06899.9
3.65-4.474.10.05610.50.0290.0640.05699.7
4.47-6.324.10.05110.70.0260.0580.05199.2
6.32-28.5213.90.04513.20.0240.0510.04597.2

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation4.63 Å28.52 Å
Translation4.63 Å28.52 Å

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Processing

Software
NameVersionClassification
SCALA3.3.20data scaling
PHASER2.5.1phasing
PHENIX1.1refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3TDJ

3tdj


Resolution: 2→28.521 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 16.95
RfactorNum. reflection% reflection
Rfree0.1889 3110 5.07 %
Rwork0.1673 --
obs0.1684 61325 99.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 113.83 Å2 / Biso mean: 26.8321 Å2 / Biso min: 7.13 Å2
Refinement stepCycle: final / Resolution: 2→28.521 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6096 0 136 522 6754
Biso mean--29.97 34.43 -
Num. residues----781
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0036391
X-RAY DIFFRACTIONf_angle_d0.6068619
X-RAY DIFFRACTIONf_chiral_restr0.043944
X-RAY DIFFRACTIONf_plane_restr0.0031075
X-RAY DIFFRACTIONf_dihedral_angle_d13.133874
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3788X-RAY DIFFRACTION4.356TORSIONAL
12B3788X-RAY DIFFRACTION4.356TORSIONAL
13C3788X-RAY DIFFRACTION4.356TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 22

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2-2.03130.20861430.197526002743100
2.0313-2.06450.23291360.189826332769100
2.0645-2.10010.19181240.186225992723100
2.1001-2.13830.25051360.182526402776100
2.1383-2.17940.20631390.181125942733100
2.1794-2.22390.18941400.179126212761100
2.2239-2.27220.20871550.173226002755100
2.2722-2.32510.20871350.171326292764100
2.3251-2.38320.2071610.174726312792100
2.3832-2.44760.2211440.17825932737100
2.4476-2.51960.2161540.170226412795100
2.5196-2.60080.17281440.168726272771100
2.6008-2.69370.19111450.161526212766100
2.6937-2.80150.16991210.159326832804100
2.8015-2.92890.19291350.165526322767100
2.9289-3.08310.13631380.168426582796100
3.0831-3.2760.20171530.161826512804100
3.276-3.52850.19341320.158726602792100
3.5285-3.88280.16741470.154726912838100
3.8828-4.44290.17031430.13712686282999
4.4429-5.59060.15441350.1482713284899
5.5906-28.52420.21371500.20772812296297
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)
13.47920.06650.40083.3341-0.06223.16060.07620.00470.28370.09210.0001-0.0691-0.3350.2747-0.18220.1701-0.03360.01180.09070.02520.1587135.662142.180472.6076
28.53053.1631-2.39093.2158-1.94122.60390.2624-0.30230.4920.023-0.1253-0.114-0.51410.2986-0.08970.2153-0.05850.0110.13080.01390.1835132.500946.777571.6897
35.8568-2.1507-0.74416.01210.96453.48620.0876-0.07730.17240.2092-0.013-0.55550.02990.4097-0.10220.1065-0.0329-0.0290.19710.02610.0736137.361535.150476.6982
40.8187-0.2767-0.37950.90280.53973.4293-0.0468-0.0006-0.06780.05920.0122-0.06510.2610.22010.01360.13820.0051-0.0020.08140.01910.1526133.24725.996870.4333
54.50410.5306-0.78745.8047-0.83754.4261-0.3066-0.2549-0.60540.0676-0.0407-0.09170.47370.26870.28450.19770.0940.05590.15560.08240.3162137.40715.216459.0231
63.5837-3.4297-0.04543.39130.19182.1996-0.0744-0.0977-0.57880.0777-0.0617-0.14690.37360.32450.07480.22630.09850.05990.22260.08530.3014142.708514.333959.9412
75.6702-1.2945-1.31648.34522.29857.2164-0.20050.0432-0.0906-0.42050.0246-0.70140.02710.80680.11870.1640.01140.03030.21030.06310.2747145.288427.291351.8167
85.1843-0.3071-4.13787.19510.74894.2208-0.0142-0.1103-0.10530.01650.07620.29830.04130.1056-0.07670.13820.0328-0.04160.16070.01070.0979134.510829.223655.9197
95.73433.1118-3.47035.6096-2.98814.6719-0.15090.54050.093-0.31810.0580.01940.09870.06560.08130.20050.0322-0.05630.28530.01580.1584132.342828.375151.8838
104.1133-0.1425-0.37982.42940.01767.4759-0.1768-0.3110.02340.20420.09220.2691-0.1386-0.01030.06510.1035-0.01860.01190.06760.0220.1796121.81533.689176.6802
115.9892-1.8923-3.90893.49751.09032.62550.36920.71240.2097-0.33-0.2315-0.0626-0.407-0.3397-0.15050.22870.0028-0.03490.20280.06580.1839125.074641.435558.5515
123.04651.2385-0.39453.55910.07824.34630.10380.008-0.5139-0.0282-0.05570.15820.3787-0.1616-0.04750.1778-0.0194-0.02180.096-0.02990.2549104.34078.378670.9881
135.6582-3.9060.83967.3023-1.3922.3010.0203-0.1066-0.26970.16180.04980.4010.0338-0.2411-0.0940.113-0.0346-0.00940.1465-0.01250.0762100.971518.919376.57
141.4665-0.34770.02910.5581-0.18553.7954-0.00610.01190.0515-0.02320.00980-0.1594-0.139-0.00490.1352-0.0255-0.00620.0654-0.01330.1397105.271727.086770.2563
152.8411-0.0561-0.23035.1933-0.34253.75740.26340.04590.693-0.00040.01640.1942-0.7722-0.328-0.16340.31910.07930.10590.1937-0.00340.326298.937438.181959.4963
163.7872-1.31671.00239.4763-3.44477.77850.1370.46540.1927-0.53940.18230.6560.1093-1.02-0.27220.14520.0113-0.01830.390900.200593.216725.864751.7337
175.6989-0.70773.92836.8611-0.03663.4815-0.00970.0908-0.0099-0.19590.1771-0.242-0.03610.0725-0.18240.1756-0.02110.03320.21460.01250.1156104.073123.918455.4681
186.40843.88134.32965.03612.63895.8084-0.10850.6409-0.1493-0.29230.1299-0.02270.08770.0205-0.0270.17340.01830.03990.341-0.02010.1975105.939824.419351.4582
195.0432-0.2719-1.35773.1569-0.93257.1208-0.1452-0.4326-0.25280.30710.0229-0.41430.02250.18950.0580.1246-0.0388-0.05650.098-0.02070.2098116.583419.247376.6571
209.1335-0.80356.26974.3055-0.6266.30670.33590.9022-0.4176-0.6947-0.1262-0.250.46560.4104-0.27880.3125-0.01950.08130.2583-0.12570.2901113.503611.55458.4848
212.34080.4133-0.35341.904-0.05181.7389-0.0181-0.0845-0.14230.0816-0.0204-0.19230.17790.2260.01110.11110.0304-0.01110.1350.00530.1054131.701271.914484.4119
220.91760.1290.09291.92711.08561.5335-0.06510.0245-0.0382-0.0432-0.00810.11870.14140.04960.06810.11840.02080.02210.08340.03460.1404119.807669.257370.497
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 22 )A1 - 22
2X-RAY DIFFRACTION2chain 'A' and (resid 23 through 47 )A23 - 47
3X-RAY DIFFRACTION3chain 'A' and (resid 48 through 65 )A48 - 65
4X-RAY DIFFRACTION4chain 'A' and (resid 66 through 123 )A66 - 123
5X-RAY DIFFRACTION5chain 'A' and (resid 124 through 152 )A124 - 152
6X-RAY DIFFRACTION6chain 'A' and (resid 153 through 173 )A153 - 173
7X-RAY DIFFRACTION7chain 'A' and (resid 174 through 187 )A174 - 187
8X-RAY DIFFRACTION8chain 'A' and (resid 188 through 202 )A188 - 202
9X-RAY DIFFRACTION9chain 'A' and (resid 203 through 217 )A203 - 217
10X-RAY DIFFRACTION10chain 'A' and (resid 218 through 243 )A218 - 243
11X-RAY DIFFRACTION11chain 'A' and (resid 244 through 261 )A244 - 261
12X-RAY DIFFRACTION12chain 'B' and (resid 3 through 47 )B3 - 47
13X-RAY DIFFRACTION13chain 'B' and (resid 48 through 65 )B48 - 65
14X-RAY DIFFRACTION14chain 'B' and (resid 66 through 123 )B66 - 123
15X-RAY DIFFRACTION15chain 'B' and (resid 124 through 173 )B124 - 173
16X-RAY DIFFRACTION16chain 'B' and (resid 174 through 187 )B174 - 187
17X-RAY DIFFRACTION17chain 'B' and (resid 188 through 202 )B188 - 202
18X-RAY DIFFRACTION18chain 'B' and (resid 203 through 217 )B203 - 217
19X-RAY DIFFRACTION19chain 'B' and (resid 218 through 243 )B218 - 243
20X-RAY DIFFRACTION20chain 'B' and (resid 244 through 261 )B244 - 261
21X-RAY DIFFRACTION21chain 'C' and (resid 1 through 93 )C1 - 93
22X-RAY DIFFRACTION22chain 'C' and (resid 94 through 261 )C94 - 261

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