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- PDB-5o9a: Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504Y... -

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Basic information

Entry
Database: PDB / ID: 5o9a
TitleCrystal structure of the GluA2 ligand-binding domain (S1S2J-L504Y-N775S) in complex with glutamate and BPAM121 at 1.78 A resolution
ComponentsGlutamate receptor 2,Glutamate receptor 2
KeywordsMEMBRANE PROTEIN / AMPA receptor / Ligand-binding domain / positive allosteric modulator / signaling protein / Ionotropic glutamate receptor / GLUA2 / GLUR2 / L504Y-N775S
Function / homology
Function and homology information


spine synapse / dendritic spine neck / dendritic spine cytoplasm / cellular response to amine stimulus / dendritic spine head / perisynaptic space / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors ...spine synapse / dendritic spine neck / dendritic spine cytoplasm / cellular response to amine stimulus / dendritic spine head / perisynaptic space / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / AMPA glutamate receptor clustering / cellular response to glycine / kainate selective glutamate receptor activity / AMPA glutamate receptor complex / immunoglobulin binding / asymmetric synapse / regulation of receptor recycling / extracellularly glutamate-gated ion channel activity / ionotropic glutamate receptor complex / conditioned place preference / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / positive regulation of synaptic transmission / regulation of synaptic transmission, glutamatergic / response to fungicide / cytoskeletal protein binding / extracellular ligand-gated monoatomic ion channel activity / cellular response to brain-derived neurotrophic factor stimulus / glutamate-gated receptor activity / regulation of long-term synaptic depression / somatodendritic compartment / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / dendrite membrane / excitatory synapse / ionotropic glutamate receptor binding / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / synaptic membrane / positive regulation of excitatory postsynaptic potential / dendritic shaft / SNARE binding / PDZ domain binding / synaptic transmission, glutamatergic / protein tetramerization / establishment of protein localization / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cerebral cortex development / postsynaptic density membrane / receptor internalization / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / terminal bouton / synaptic vesicle / long-term synaptic potentiation / synaptic vesicle membrane / signaling receptor activity / amyloid-beta binding / presynapse / growth cone / presynaptic membrane / scaffold protein binding / dendritic spine / chemical synaptic transmission / perikaryon / postsynaptic membrane / neuron projection / postsynaptic density / axon / external side of plasma membrane / neuronal cell body / synapse / dendrite / protein kinase binding / protein-containing complex 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. / Periplasmic binding protein-like II / Receptor, 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. / Periplasmic binding protein-like II / Receptor, ligand binding region / Receptor family ligand binding region / D-Maltodextrin-Binding Protein; domain 2 / Periplasmic binding protein-like I / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-7M6 / CITRIC ACID / GLUTAMIC ACID / DI(HYDROXYETHYL)ETHER / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.78 Å
AuthorsLaulumaa, S. / Rovinskaja, K. / Frydenvang, K.A. / Kastrup, J.S.
CitationJournal: 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.
History
DepositionJun 16, 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 / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 1.3Oct 16, 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,Glutamate receptor 2
B: Glutamate receptor 2,Glutamate receptor 2
C: Glutamate receptor 2,Glutamate receptor 2
D: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,36842
Polymers117,2074
Non-polymers4,16138
Water20,8971160
1
A: Glutamate receptor 2,Glutamate receptor 2
B: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,48420
Polymers58,6032
Non-polymers1,88018
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4480 Å2
ΔGint-112 kcal/mol
Surface area24850 Å2
MethodPISA
2
C: Glutamate receptor 2,Glutamate receptor 2
D: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,88422
Polymers58,6032
Non-polymers2,28120
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4790 Å2
ΔGint-146 kcal/mol
Surface area24320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.308, 98.408, 121.787
Angle α, β, γ (deg.)90.000, 90.530, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resseq 5:15 or resseq 17:20 or (resid...
21(chain B and (resseq 5:15 or resseq 17:20 or (resid...
31(chain D and (resseq 5:15 or resseq 17:20 or (resid...

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
11THRTHRPROPRO(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA5 - 155 - 15
12VALVALLYSLYS(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA17 - 2017 - 20
13HISHISHISHIS(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA2323
14GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
15GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
16GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
17GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
18GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
19GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
110GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
111GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
112GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
113GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
114GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
115GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
116GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
117GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
118GLYGLYSERSER(chain A and (resseq 5:15 or resseq 17:20 or (resid...AA1 - 2631 - 263
21THRTHRPROPRO(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB5 - 155 - 15
22VALVALLYSLYS(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB17 - 2017 - 20
23HISHISHISHIS(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB2323
24GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
25GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
26GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
27GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
28GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
29GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
210GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
211GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
212GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
213GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
214GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
215GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
216GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
217GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
218GLYGLYGLYGLY(chain B and (resseq 5:15 or resseq 17:20 or (resid...BB1 - 2641 - 264
31THRTHRPROPRO(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD5 - 155 - 15
32VALVALLYSLYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD17 - 2017 - 20
33HISHISHISHIS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2323
34ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
35ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
36ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
37ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
38ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
39ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
310ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
311ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
312ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
313ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
314ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
315ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
316ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
317ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261
318ALAALACYSCYS(chain D and (resseq 5:15 or resseq 17:20 or (resid...DD2 - 2612 - 261

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Glutamate receptor 2,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: 29301.729 Da / Num. of mol.: 4 / Mutation: L504Y,N775S
Source method: isolated from a genetically manipulated source
Details: Native GluA2 is a membrane protein. The crystallized protein is a double mutant (L540Y, N775S) of the ligand-binding domain of GluA2. Transmembrane regions were replaced with a Gly-Thr ...Details: Native GluA2 is a membrane protein. The crystallized protein is a double mutant (L540Y, N775S) of the ligand-binding domain of GluA2. Transmembrane regions were replaced with a Gly-Thr linker (residues 117-118). Gly1 is a cloning remnant. The sequence matches discontinuously with reference database (413-527, 653-797).
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 , 9 types, 1198 molecules

#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Formula: SO4
#3: Chemical
ChemComp-7M6 / 7-chloro-4-(2-fluoroethyl)-2,3-dihydro-1,2,4-benzothiadiazine 1,1-dioxide


Mass: 264.704 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C9H10ClFN2O2S
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Cl
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-GLU / GLUTAMIC ACID


Type: L-peptide linking / Mass: 147.129 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H9NO4
#7: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#9: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1160 / 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: 2.42 Å3/Da / Density % sol: 49.14 %
Crystal growTemperature: 279 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 18% PEG4000, 0.23 M lithium sulfate, 0.1 M phosphate citrate pH 4.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 0.979 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 19, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 1.78→121.782 Å / Num. all: 106755 / Num. obs: 106755 / % possible obs: 100 % / Redundancy: 3.7 % / Biso Wilson estimate: 15.47 Å2 / Rpim(I) all: 0.038 / Rrim(I) all: 0.074 / Rsym value: 0.063 / Net I/av σ(I): 10.4 / Net I/σ(I): 14.7 / Num. measured all: 395853
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) allRsym valueNet I/σ(I) obs% possible all
1.78-1.883.60.377256042155820.2330.4450.3773.5100
1.88-1.993.70.249354342146820.1510.2920.2495.3100
1.99-2.133.70.1554.851284138090.0940.1820.1558100
2.13-2.33.70.1057.148006128750.0630.1230.10511.3100
2.3-2.523.70.082944383118740.050.0960.08213.7100
2.52-2.813.70.061240212107280.0360.070.0617.9100
2.81-3.253.80.04315.93553394560.0260.0510.04323.9100
3.25-3.983.70.03219.93016380580.0190.0380.03232.4100
3.98-5.633.70.02620.92323562100.0160.0310.02636.8100
5.63-49.2043.60.026201265334810.0160.0310.0263499.8

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Processing

Software
NameClassification
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3TKD

3tkd


Resolution: 1.78→49.204 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 17.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1789 5325 4.99 %
Rwork0.1534 101384 -
obs0.1547 106709 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 112.84 Å2 / Biso mean: 22.4654 Å2 / Biso min: 5.63 Å2
Refinement stepCycle: final / Resolution: 1.78→49.204 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8178 0 199 1186 9563
Biso mean--41.23 29.23 -
Num. residues----1054
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0058868
X-RAY DIFFRACTIONf_angle_d0.78612010
X-RAY DIFFRACTIONf_chiral_restr0.0491304
X-RAY DIFFRACTIONf_plane_restr0.0051490
X-RAY DIFFRACTIONf_dihedral_angle_d15.8165450
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3712X-RAY DIFFRACTION4.403TORSIONAL
12B3712X-RAY DIFFRACTION4.403TORSIONAL
13D3712X-RAY DIFFRACTION4.403TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.78-1.80020.27311470.22634323579100
1.8002-1.82140.25011840.217834243608100
1.8214-1.84360.22281320.197833563488100
1.8436-1.8670.23641910.191633213512100
1.867-1.89150.20971820.190234223604100
1.8915-1.91740.19821520.186633313483100
1.9174-1.94480.19971730.189733873560100
1.9448-1.97390.21731780.184234063584100
1.9739-2.00470.20191760.176933293505100
2.0047-2.03760.21391860.169733603546100
2.0376-2.07270.18431720.157533673539100
2.0727-2.11040.19022030.154333223525100
2.1104-2.1510.18342250.1533793604100
2.151-2.19490.14971690.145233163485100
2.1949-2.24260.17691620.144934463608100
2.2426-2.29480.19021890.147433103499100
2.2948-2.35220.18041780.146933983576100
2.3522-2.41580.1751790.145733493528100
2.4158-2.48690.17621790.147834353614100
2.4869-2.56710.17241760.14833153491100
2.5671-2.65890.17621940.146833983592100
2.6589-2.76530.1931750.144733663541100
2.7653-2.89120.16141610.148433783539100
2.8912-3.04360.18192050.155633633568100
3.0436-3.23420.18361890.14533733562100
3.2342-3.48390.15371600.138634153575100
3.4839-3.83440.15311830.134433913574100
3.8344-4.38890.13471780.121234143592100
4.3889-5.52840.14661740.132534113585100
5.5284-49.22280.22391730.18923470364399
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)
12.1731-0.22920.0982.02630.27551.9456-0.05710.32230.1682-0.15370.04950.0294-0.05610.06760.02280.1313-0.0175-0.01730.10170.0130.06728.930926.540324.6711
22.3426-0.10210.59490.9970.46213.5005-0.11660.27290.1778-0.25460.16810.0268-0.3670.1871-0.01720.1849-0.0651-0.02140.14530.04430.11958.131931.686522.4919
32.88960.84580.01233.09270.55552.1461-0.0980.0193-0.3412-0.10910.0675-0.17360.27550.12940.0630.0897-0.00180.01930.1127-0.02340.088314.682616.850831.763
42.72390.63750.24510.68630.19480.6443-0.0261-0.074-0.03650.0154-0.0035-0.01540.01510.0540.03330.09720.012-0.00790.06520.00610.0463.909320.380639.4679
53.24210.5937-0.04872.8361-0.72433.87360.0463-0.285-0.22250.2671-0.0738-0.13340.2543-0.05190.02050.19970.0019-0.01250.06050.02570.1003-4.30188.240144.0692
62.03010.29450.50393.77750.81271.84270.0812-0.199-0.29310.019-0.0011-0.01480.6332-0.12480.00220.20840.001-0.00410.08050.02170.1254-3.27373.788641.5509
73.45530.60270.48543.7191-0.24552.776-0.03670.0882-0.0898-0.13770.0481-0.03490.1299-0.15060.00160.0964-0.007-0.00230.0787-0.010.0416-9.267915.953132.7976
86.06121.17934.61780.41961.20667.4588-0.0371-0.27880.2302-0.0165-0.11990.1173-0.2569-0.52810.09340.14990.0244-0.00650.0851-0.01530.1452-11.617120.528436.8308
93.51990.2456-0.14132.54110.32181.7461-0.00140.0070.18360.0509-0.0227-0.1453-0.16310.14650.02870.1109-0.0117-0.02080.0975-0.01210.047913.705832.428739.5142
106.0994.44651.72964.13311.26941.8442-0.19440.01480.5971-0.11160.0050.4834-0.1503-0.16640.19650.16960.0223-0.03690.1025-0.00830.1761-5.217534.780831.4429
111.9762-0.33740.14881.89020.0371.57880.0306-0.123-0.02890.1144-0.0402-0.06090.03040.23960.0030.0927-0.01270.00390.1871-0.00510.08098.910830.092970.5916
121.9016-0.3162-0.14711.809-0.40961.80310.0011-0.09530.25310.0396-0.018-0.0151-0.22490.11680.03170.1179-0.0317-0.01010.1297-0.02530.1098.795440.339157.1352
131.3679-0.351-0.52813.69760.50772.31380.2830.05710.4976-0.11620.00520.7486-0.4083-0.2505-0.22520.36940.02290.09570.1572-0.01680.4317-5.167652.155853.5174
144.0454-1.3164-1.22512.37260.15512.15170.0582-0.19560.2082-0.0027-0.04550.4935-0.0488-0.23730.00150.1468-0.0432-0.00910.1272-0.04640.2363-2.651837.678156.9725
154.9584-0.8075-1.64522.42930.18022.7186-0.092-0.1565-0.08430.05890.01480.3220.1567-0.25640.1030.1004-0.0117-0.00770.15380.00520.08570.603623.665559.111
162.1767-0.02320.39641.8329-0.02691.4685-0.10850.22-0.2024-0.18880.0728-0.0070.1736-0.15840.04840.1331-0.03380.0250.1257-0.01730.1012-9.570419.962484.6026
172.95240.72320.03993.5047-0.55592.4338-0.08760.0080.2912-0.09880.10520.1409-0.2729-0.14020.01740.06440.0179-0.01840.11270.03640.0857-15.840732.367592.4356
181.99470.8003-0.2270.81050.05860.98650.0318-0.09620.08120.053-0.02880.0163-0.05070.05590.00320.07860.0199-0.00210.07720.01150.057-2.025733.7527102.2695
191.75080.3499-0.90724.22850.09843.02610.0501-0.17970.2729-0.0560.01710.03-0.70840.1085-0.02170.13980.00340.01090.1031-0.02140.10631.888945.4827102.2621
203.08360.6237-0.45133.96980.24653.1232-0.05940.07040.0568-0.16480.08690.0201-0.08310.1373-0.01450.0567-0.0019-0.0050.10520.00850.04597.962533.480993.416
217.40850.8186-6.39940.1088-0.93258.3417-0.0142-0.2876-0.1844-0.0283-0.09-0.06420.1510.53680.07430.10910.0322-0.00350.09310.02090.143410.351628.613497.7008
223.2477-0.32630.99143.5911-0.72212.4886-0.0252-0.1226-0.3175-0.1520.03040.20790.256-0.2069-0.00590.1113-0.01510.02910.10240.01460.0733-14.699717.1572100.3095
234.44092.4896-1.30762.1311-0.56111.9774-0.3532-0.1688-0.8447-0.12370.025-0.56420.29260.23570.30450.19050.04970.07570.14410.02290.24724.073314.557592.28
242.00680.1572-0.33892.33820.36531.82730.0492-0.13190.04960.2085-0.02490.09910.0468-0.2363-0.00390.1076-0.01220.01330.17260.03380.0933-10.855916.0813131.105
253.8732-0.96011.74072.5041-1.86347.2532-0.0299-0.08080.08220.21610.04380.0555-0.2762-0.1825-0.00890.0937-0.0082-0.00220.0829-0.02370.0868-10.701921.7356131.3769
263.5876-0.59510.00534.86720.09672.3461-0.0654-0.0805-0.4271-0.01690.05670.22370.4935-0.28080.02920.13-0.06980.02620.16890.06620.1396-17.06986.9232122.1429
271.9463-0.44590.44782.76980.99510.6627-0.0353-0.2618-0.08380.0829-0.13530.27420.2197-0.31950.11830.102-0.04790.00740.17390.02560.1183-16.158711.8389119.5395
281.6903-0.61460.7011.0112-0.38431.2026-0.0431-0.0273-0.1375-0.2385-0.1038-0.19830.3350.13370.04230.17420.02330.06550.14310.06320.1641-1.78039.4835113.7569
291.417-0.28930.13741.28140.1580.35140.48820.2342-0.5633-1.0319-0.2603-0.15210.63930.15940.14720.74460.2523-0.0530.12260.10210.31862.1818-3.8374112.3432
307.7987-3.1817-0.47367.01712.53725.5346-0.0682-0.9925-0.40730.0414-0.002-0.43680.23790.17930.1060.1909-0.00840.00540.25340.11510.22918.0438-0.9217126.5183
312.2481-1.4065-0.12922.6612-0.92741.20210.0798-0.16060.1089-0.1201-0.1987-0.51410.10750.37630.090.16360.03520.06020.23680.0980.28167.42469.5175120.3405
323.05660.2251-0.2283.2886-0.55531.4711-0.0361-0.00330.031-0.13840.06530.3373-0.015-0.31920.00170.0884-0.0031-0.01850.14090.01360.0548-15.335122.0464114.5471
337.0824-2.25022.41563.2592-0.34272.8217-0.2217-0.18750.25720.07770.1043-0.5199-0.21140.50.20260.1066-0.0284-0.01420.2170.00590.15093.239824.3856123.7666
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 79 )A48 - 79
4X-RAY DIFFRACTION4chain 'A' and (resid 80 through 123 )A80 - 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 202 )A174 - 202
8X-RAY DIFFRACTION8chain 'A' and (resid 203 through 217 )A203 - 217
9X-RAY DIFFRACTION9chain 'A' and (resid 218 through 243 )A218 - 243
10X-RAY DIFFRACTION10chain 'A' and (resid 244 through 263 )A244 - 263
11X-RAY DIFFRACTION11chain 'B' and (resid 1 through 47 )B1 - 47
12X-RAY DIFFRACTION12chain 'B' and (resid 48 through 123 )B48 - 123
13X-RAY DIFFRACTION13chain 'B' and (resid 124 through 187 )B124 - 187
14X-RAY DIFFRACTION14chain 'B' and (resid 188 through 230 )B188 - 230
15X-RAY DIFFRACTION15chain 'B' and (resid 231 through 264 )B231 - 264
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 47 )C1 - 47
17X-RAY DIFFRACTION17chain 'C' and (resid 48 through 79 )C48 - 79
18X-RAY DIFFRACTION18chain 'C' and (resid 80 through 152 )C80 - 152
19X-RAY DIFFRACTION19chain 'C' and (resid 153 through 173 )C153 - 173
20X-RAY DIFFRACTION20chain 'C' and (resid 174 through 202 )C174 - 202
21X-RAY DIFFRACTION21chain 'C' and (resid 203 through 217 )C203 - 217
22X-RAY DIFFRACTION22chain 'C' and (resid 218 through 243 )C218 - 243
23X-RAY DIFFRACTION23chain 'C' and (resid 244 through 263 )C244 - 263
24X-RAY DIFFRACTION24chain 'D' and (resid 2 through 22 )D2 - 22
25X-RAY DIFFRACTION25chain 'D' and (resid 23 through 47 )D23 - 47
26X-RAY DIFFRACTION26chain 'D' and (resid 48 through 79 )D48 - 79
27X-RAY DIFFRACTION27chain 'D' and (resid 80 through 93 )D80 - 93
28X-RAY DIFFRACTION28chain 'D' and (resid 94 through 123 )D94 - 123
29X-RAY DIFFRACTION29chain 'D' and (resid 124 through 173 )D124 - 173
30X-RAY DIFFRACTION30chain 'D' and (resid 174 through 187 )D174 - 187
31X-RAY DIFFRACTION31chain 'D' and (resid 188 through 217 )D188 - 217
32X-RAY DIFFRACTION32chain 'D' and (resid 218 through 243 )D218 - 243
33X-RAY DIFFRACTION33chain 'D' and (resid 244 through 261 )D244 - 261

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