PDB-8qez: Crystal structure of the AMPA receptor GluA2-L504Y-N775S ligand b...

ID or keywords:

Entry

Database: PDB / ID: 8qez

Title

Crystal structure of the AMPA receptor GluA2-L504Y-N775S ligand binding domain in complex with L-glutamate and positive allosteric modulator BPAM395 at 1.55A resolution

Components

Glutamate receptor 2

Keywords

MEMBRANE PROTEIN / AMPA RECEPTOR LIGAND-BINDING DOMAIN / GLUA2 S1S2J-L504Y-N775S / BPAM395 / POSITIVE ALLOSTERIC MODULATION

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

Biological species

Rattus norvegicus (Norway rat)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.55 Å

Authors

Dorosz, J. / Laulumaa, S. / Frydenvang, K. / Kastrup, J.S.

Funding support

1items

Citation

Journal: Eur.J.Med.Chem. / Year: 2023
Title: Exploring thienothiadiazine dioxides as isosteric analogues of benzo- and pyridothiadiazine dioxides in the search of new AMPA and kainate receptor positive allosteric modulators.
Authors: Francotte, P. / Bay, Y. / Goffin, E. / Colson, T. / Lesenfants, C. / Dorosz, J. / Laulumaa, S. / Fraikin, P. / de Tullio, P. / Beaufour, C. / Botez, I. / Pickering, D.S. / Frydenvang, K. / ...

History

Deposition	Sep 1, 2023	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Dec 27, 2023	Provider: repository / Type: Initial release
Revision 1.1	Oct 16, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	8qez.cif.gz	485.3 KB	Display	PDBx/mmCIF format
PDB format	pdb8qez.ent.gz	409.8 KB	Display	PDB format
PDBx/mmJSON format	8qez.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qe/8qez ftp://data.pdbj.org/pub/pdb/validation_reports/qe/8qez	HTTPS FTP

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Related structure data

Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#235 - Jul 2019 AMPA Receptor similarity (14) #196 - Apr 2016 Lead Poisoning similarity (1) #199 - Jul 2016 Monellin similarity (2) #88 - Apr 2007 Clathrin similarity (1) #133 - Jan 2011 Nitric Oxide Synthase similarity (1) #203 - Nov 2016 Aminopeptidase 1 and Autophagy similarity (1) #75 - Mar 2006 Tissue Factor similarity (1) #90 - Jun 2007 Fatty Acid Synthase similarity (1) #191 - Nov 2015 Glutamate-gated Chloride Receptors similarity (1) #44 - Aug 2003 Calmodulin similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#235 - Jul 2019
AMPA Receptor
similarity (14)
#196 - Apr 2016
Lead Poisoning
similarity (1)
#199 - Jul 2016
Monellin
similarity (2)
#88 - Apr 2007
Clathrin
similarity (1)
#133 - Jan 2011
Nitric Oxide Synthase
similarity (1)
#203 - Nov 2016
Aminopeptidase 1 and Autophagy
similarity (1)
#75 - Mar 2006
Tissue Factor
similarity (1)
#90 - Jun 2007
Fatty Acid Synthase
similarity (1)
#191 - Nov 2015
Glutamate-gated Chloride Receptors
similarity (1)
#44 - Aug 2003
Calmodulin
similarity (1)

Deposited unit

A: Glutamate receptor 2

B: Glutamate receptor 2

C: Glutamate receptor 2

hetero molecules

90.7 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Glutamate receptor 2

B: Glutamate receptor 2

hetero molecules

defined by author
60.3 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Glutamate receptor 2

hetero molecules

C: Glutamate receptor 2

hetero molecules

defined by author
Evidence: Chain C forms a dimer with a symmetry related chain C
60.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	114.316, 163.416, 47.466
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	18
Space group name H-M	P2₁2₁2

Components on special symmetry positions

ID	Model	Components
1	1	C-436- HOH

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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: 29301.729 Da / Num. of mol.: 3 / Mutation: L504Y,N775S Source method: isolated from a genetically manipulated source Details: NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND-BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR ...Details: NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND-BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR LINKER (RESIDUES 118-119). THEREFORE THE SEQUENCE MATCHES DISCONTINUOUSLY WITH THE REFERENCE DATABASE (UNP RESIDUES 413- 527 AND 653-796, NUMBERING WITH SIGNAL PEPTIDE OF 21 AMINO ACIDS) THE TWO FIRST RESIDUES (GLY, ALA) ARE CLONING REMNANTS. Engineered mutations: L504Y, N775S.,NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND-BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR LINKER (RESIDUES 118-119). THEREFORE THE SEQUENCE MATCHES DISCONTINUOUSLY WITH THE REFERENCE DATABASE (UNP RESIDUES 413- 527 AND 653-796, NUMBERING WITH SIGNAL PEPTIDE OF 21 AMINO ACIDS) THE TWO FIRST RESIDUES (GLY, ALA) ARE CLONING REMNANTS. Engineered mutations: L504Y, N775S. Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Plasmid: PET-22B(+) / Production host: Escherichia coli (E. coli) / Strain (production host): Origami B (DE3) / References: UniProt: P19491

#1: Protein

Glutamate receptor 2 / GluR-2 / AMPA-selective glutamate receptor 2 / GluR-B / GluR-K2 / Glutamate receptor ionotropic / ...

Mass: 29301.729 Da / Num. of mol.: 3 / Mutation: L504Y,N775S
Source method: isolated from a genetically manipulated source
Details: NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND-BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR ...
Source: (gene. exp.)

Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Plasmid: PET-22B(+) / Production host:

Escherichia coli (E. coli) / Strain (production host): Origami B (DE3) / References: UniProt: P19491

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Non-polymers , 8 types, 818 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 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Zn
#4: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₂H₃O₂
#5: Chemical	ChemComp-UF5 / 6-chloranyl-4-cyclopropyl-2,3-dihydrothieno[3,2-e][1,2,4]thiadiazine 1,1-dioxide Mass: 264.752 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₈H₉ClN₂O₂S₂ / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#7: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃H₈O₃
#8: Chemical	ChemComp-CAC / CACODYLATE ION / dimethylarsinate Mass: 136.989 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₆AsO₂
#9: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 789 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
Has protein modification	Y

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.52 Å³/Da / Density % sol: 51.23 %
Crystal grow	Temperature: 279 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 15.2% PEG4000, 0.1M Zn Acetate, 0.1M Cacodylate pH 6.5

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å
Detector	Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Mar 6, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97625 Å / Relative weight: 1
Reflection	Resolution: 1.55→49.17 Å / Num. obs: 129920 / % possible obs: 100 % / Redundancy: 6.7 % / R_merge(I) obs: 0.071 / R_pim(I) all: 0.029 / R_rim(I) all: 0.077 / Net I/σ(I): 13.1 / Num. measured all: 864426
Reflection shell	Resolution: 1.55→1.63 Å / % possible obs: 100 % / Redundancy: 6.6 % / R_merge(I) obs: 0.879 / Num. measured all: 124663 / Num. unique obs: 18786 / R_pim(I) all: 0.367 / R_rim(I) all: 0.953 / Net I/σ(I) obs: 2

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Processing

Software

Name	Version	Classification
PHENIX	(1.20_4459: ???)	refinement
SCALA		data scaling
XDS		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.55→49.17 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 18.04 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1952	6588	5.07 %
R_work	0.1676	-	-
obs	0.169	129822	99.98 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 1.55→49.17 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6156	0	146	789	7091

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	6603
X-RAY DIFFRACTION	f_angle_d	0.885	8922
X-RAY DIFFRACTION	f_dihedral_angle_d	13.084	2539
X-RAY DIFFRACTION	f_chiral_restr	0.052	966
X-RAY DIFFRACTION	f_plane_restr	0.006	1127

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
1.55-1.57	0.2677	231	0.2615	4035	X-RAY DIFFRACTION	100
1.57-1.59	0.2819	257	0.2547	4037	X-RAY DIFFRACTION	100
1.59-1.61	0.2702	235	0.2416	4012	X-RAY DIFFRACTION	100
1.61-1.63	0.2681	223	0.2311	4062	X-RAY DIFFRACTION	100
1.63-1.65	0.2555	241	0.2349	4050	X-RAY DIFFRACTION	100
1.65-1.67	0.2532	191	0.2338	4061	X-RAY DIFFRACTION	100
1.67-1.69	0.2864	213	0.2577	4133	X-RAY DIFFRACTION	100
1.69-1.72	0.2805	189	0.2438	4041	X-RAY DIFFRACTION	100
1.72-1.75	0.2603	230	0.2307	4038	X-RAY DIFFRACTION	100
1.75-1.77	0.2489	207	0.2213	4083	X-RAY DIFFRACTION	100
1.77-1.8	0.2625	207	0.2034	4056	X-RAY DIFFRACTION	100
1.8-1.84	0.216	218	0.1904	4095	X-RAY DIFFRACTION	100
1.84-1.87	0.2086	233	0.1698	4075	X-RAY DIFFRACTION	100
1.87-1.91	0.1956	212	0.167	4110	X-RAY DIFFRACTION	100
1.91-1.95	0.1987	198	0.1674	4080	X-RAY DIFFRACTION	100
1.95-2	0.2022	225	0.1725	4071	X-RAY DIFFRACTION	100
2-2.05	0.2109	246	0.1702	4059	X-RAY DIFFRACTION	100
2.05-2.1	0.2036	227	0.1792	4090	X-RAY DIFFRACTION	100
2.1-2.17	0.2	216	0.1599	4099	X-RAY DIFFRACTION	100
2.17-2.24	0.1562	192	0.1476	4107	X-RAY DIFFRACTION	100
2.24-2.32	0.1754	221	0.1456	4092	X-RAY DIFFRACTION	100
2.32-2.41	0.1902	205	0.1543	4142	X-RAY DIFFRACTION	100
2.41-2.52	0.1983	227	0.1531	4119	X-RAY DIFFRACTION	100
2.52-2.65	0.1807	210	0.155	4152	X-RAY DIFFRACTION	100
2.65-2.82	0.1912	203	0.1546	4148	X-RAY DIFFRACTION	100
2.82-3.03	0.1693	239	0.1607	4125	X-RAY DIFFRACTION	100
3.03-3.34	0.1866	229	0.1516	4162	X-RAY DIFFRACTION	100
3.34-3.82	0.1912	219	0.1489	4193	X-RAY DIFFRACTION	100
3.82-4.81	0.1431	217	0.1333	4268	X-RAY DIFFRACTION	100
4.81-49.17	0.2035	227	0.1904	4439	X-RAY DIFFRACTION	100

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°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)
1	3.2109	-0.3776	0.5444	3.0788	-0.1951	3.9887	0.0432	-0.0193	-0.3023	-0.0117	-0.0436	-0.1011	0.1081	0.1217	-0.0089	0.1523	0.0111	-0.0062	0.0959	0.0197	0.1745	-47.0923	8.443	-24.0267
2	4.9767	3.0279	0.5876	5.4327	-0.2019	2.9979	-0.0331	0.1669	0.2214	0.0025	-0.0695	-0.2918	-0.1738	0.3429	0.0651	0.0909	0.0159	-0.0049	0.1698	0.0176	0.159	-42.4064	22.5932	-30.4314
3	1.4017	0.5825	0.0527	0.5534	0.1501	2.9365	-0.0256	-0.0624	0.0902	0.0862	-0.0097	-0.0021	-0.0902	0.1254	0.0321	0.1395	0.0253	-0.0179	0.1046	0.0243	0.1374	-49.9683	26.4719	-19.9685
4	3.9029	0.9758	-0.0227	5.0849	-0.9363	5.1487	0.0208	-0.1192	0.5363	-0.0962	-0.1192	-0.1341	-0.5462	0.6258	0.0865	0.2156	-0.0691	0.0344	0.2525	0.0108	0.3176	-39.9268	35.0404	-10.5371
5	4.3075	-0.7425	2.9684	3.2043	-2.3594	5.6715	0.0035	-0.4431	-0.1347	-0.0413	0.0264	0.0566	0.1364	0.0001	-0.0319	0.1613	0.0292	0.0271	0.2001	0.0118	0.1289	-47.4374	23.5469	-6.2838
6	5.4419	-0.0075	-1.9713	1.9429	1.3697	6.0379	-0.1527	0.4429	-0.2098	-0.0772	0.0352	0.1892	0.0423	-0.2643	0.0977	0.1355	0.028	-0.0325	0.0968	0.0337	0.1504	-59.3322	18.968	-29.1752
7	7.3684	-1.0193	6.6329	3.3314	-1.704	7.6319	0.1869	-0.712	-0.2514	0.3747	-0.0296	0.1115	0.2939	-0.4583	-0.1935	0.3299	0.0231	0.0628	0.2756	0.0823	0.244	-55.8672	11.5989	-9.7461
8	2.1845	0.4449	-0.2632	2.4593	0.0005	2.2136	-0.0371	0.0493	0.0345	-0.0755	0.0121	0.2983	-0.0427	-0.2875	0.0146	0.1165	0.012	-0.0112	0.1444	-0.0057	0.1331	-77.8375	37.5476	-27.2767
9	1.4342	0.6864	-0.9265	1.1929	-0.4322	1.7994	-0.0275	-0.0574	-0.1062	0.0674	-0.0873	0.0251	0.0832	-0.1635	0.1102	0.1408	-0.0048	-0.0131	0.1484	-0.0177	0.154	-75.508	25.5119	-13.1964
10	2.202	-0.0127	-0.5144	2.4467	-0.1557	2.161	0.1035	0.094	-0.0863	-0.0873	0.0138	0.1115	0.1018	-0.3365	-0.0305	0.1025	-0.0112	0.011	0.1645	0.0009	0.1233	-76.378	73.1787	-35.5454
11	2.8415	0.3989	-0.5921	2.9508	-0.7918	2.2759	-0.048	0.0409	-0.0777	0.0105	0.1062	0.3809	0.119	-0.3566	-0.045	0.1002	0.0047	0.0043	0.2144	-0.0011	0.159	-81.5013	76.8094	-33.0909
12	2.7862	-1.5066	0.2198	6.4504	-0.932	3.7156	-0.0415	0.0823	-0.286	-0.0514	0.0326	-0.1831	0.4107	0.0639	-0.0071	0.1233	-0.0426	-0.0021	0.1092	-0.028	0.1149	-68.3024	65.5098	-40.404
13	0.1845	-0.188	0.2329	0.8287	-0.4098	2.3643	-0.0055	0.0194	-0.0005	-0.0032	-0.0184	-0.0649	0.0774	-0.022	0.0231	0.1113	-0.0172	0.0132	0.1409	-0.0038	0.1457	-61.7267	71.055	-30.1864
14	4.634	-0.7489	-0.8186	3.2299	-1.5427	7.5306	-0.095	0.083	-0.1229	-0.1796	-0.1191	-0.5628	0.3466	0.1113	0.1642	0.1637	0.0009	0.043	0.048	-0.0322	0.26	-54.1784	60.5142	-21.5447
15	3.7971	1.5481	0.8339	5.5854	0.545	2.9478	-0.0363	-0.0231	-0.1144	-0.158	-0.0164	-0.6331	0.2071	0.0606	0.0527	0.1657	0.01	0.0518	0.1133	-0.0195	0.2023	-55.6729	55.5047	-22.2869
16	7.2875	-1.738	3.9404	1.8682	-0.8265	7.6927	0.0334	-0.2852	-0.5153	0.1441	-0.0803	0.2438	0.5607	-0.4408	-0.0185	0.2143	-0.054	0.0521	0.1229	-0.0383	0.2294	-68.7087	58.3019	-14.1172
17	7.3211	-2.4197	-1.6118	6.4962	-4.6057	5.4463	0.062	0.0815	0.1219	-0.0129	0.068	-0.0281	0.0301	-0.1808	-0.1266	0.109	-0.0352	-0.0298	0.1142	-0.0273	0.0641	-65.9465	68.8519	-18.1406
18	7.2578	3.6445	-6.0229	1.94	-3.0416	7.0215	0.1742	-0.0928	0.1752	0.2579	-0.1238	0.0945	-0.2088	-0.0863	-0.0367	0.1727	0.0008	0.0095	0.1036	-0.0222	0.1525	-64.5073	70.3971	-13.9222
19	2.3789	0.1268	1.4737	4.8239	1.4049	3.9401	-0.0203	0.1533	0.1644	-0.4578	-0.0913	-0.0037	-0.184	0.0803	0.1014	0.0767	-0.0132	0.0274	0.1321	0.0195	0.1025	-64.6755	82.1314	-39.3886
20	4.7916	3.6622	-4.1475	6.2607	-4.8938	4.4066	0.0617	-0.3334	0.0678	0.7419	0.0395	0.1282	-0.4403	-0.0038	-0.0985	0.2346	0.0262	0.0174	0.2553	-0.0512	0.207	-73.0113	82.29	-19.766

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 1 through 47 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 48 through 79 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 80 through 123 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 124 through 187 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 188 through 217 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 218 through 243 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 244 through 264 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 1 through 93 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 94 through 264 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 1 through 20 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 21 through 47 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 48 through 79 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 80 through 123 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 124 through 152 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 153 through 173 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 174 through 187 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 188 through 202 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 203 through 217 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 218 through 243 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 244 through 264 )

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