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- PDB-4u4s: Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y... -

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Basic information

Entry
Database: PDB / ID: 4u4s
TitleCrystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM25 at 1.90 A resolution.
ComponentsGlutamate receptor 2,Glutamate receptor 2
KeywordsMEMBRANE PROTEIN / AMPA RECEPTOR LIGAND-BINDING DOMAIN / ALLOSTERIC MODULATION / BPAM25
Function / homology
Function and homology information


spine synapse / dendritic spine neck / dendritic spine head / cellular response to amine stimulus / perisynaptic space / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / AMPA glutamate receptor activity / response to lithium ion / Trafficking of GluR2-containing AMPA receptors ...spine synapse / dendritic spine neck / dendritic spine head / cellular response to amine stimulus / perisynaptic space / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / AMPA glutamate receptor activity / response to lithium ion / Trafficking of GluR2-containing AMPA receptors / kainate selective glutamate receptor activity / cellular response to glycine / AMPA glutamate receptor complex / extracellularly glutamate-gated ion channel activity / immunoglobulin binding / asymmetric synapse / ionotropic glutamate receptor complex / conditioned place preference / regulation of receptor recycling / glutamate receptor binding / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of synaptic transmission / regulation of synaptic transmission, glutamatergic / response to fungicide / cytoskeletal protein binding / glutamate-gated receptor activity / regulation of long-term synaptic depression / cellular response to brain-derived neurotrophic factor stimulus / extracellular ligand-gated monoatomic ion channel activity / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / somatodendritic compartment / dendrite membrane / ionotropic glutamate receptor binding / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / synaptic membrane / dendritic shaft / SNARE binding / 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 / postsynaptic density membrane / cerebral cortex development / modulation of chemical synaptic transmission / receptor internalization / Schaffer collateral - CA1 synapse / terminal bouton / synaptic vesicle / synaptic vesicle membrane / signaling receptor activity / presynapse / amyloid-beta binding / growth cone / presynaptic membrane / scaffold protein binding / perikaryon / dendritic spine / chemical synaptic transmission / 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. / 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-3C1 / ACETATE ION / GLUTAMIC ACID / DI(HYDROXYETHYL)ETHER / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsNoerholm, A.B. / Deva, T. / Frydenvang, K. / Kastrup, J.S.
Citation
Journal: J.Med.Chem. / Year: 2014
Title: Positive Allosteric Modulators of 2-Amino-3-(3-hydroxy-5-methylisoxazol-4-yl)propionic Acid Receptors Belonging to 4-Cyclopropyl-3,4-dihydro-2H-1,2,4-pyridothiadiazine Dioxides and Diversely ...Title: Positive Allosteric Modulators of 2-Amino-3-(3-hydroxy-5-methylisoxazol-4-yl)propionic Acid Receptors Belonging to 4-Cyclopropyl-3,4-dihydro-2H-1,2,4-pyridothiadiazine Dioxides and Diversely Chloro-Substituted 4-Cyclopropyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-Dioxides.
Authors: Francotte, P. / Nrholm, A.B. / Deva, T. / Olsen, L. / Frydenvang, K. / Goffin, E. / Fraikin, P. / de Tullio, P. / Challal, S. / Thomas, J.Y. / Iop, F. / Louis, C. / Botez-Pop, I. / Lestage, ...Authors: Francotte, P. / Nrholm, A.B. / Deva, T. / Olsen, L. / Frydenvang, K. / Goffin, E. / Fraikin, P. / de Tullio, P. / Challal, S. / Thomas, J.Y. / Iop, F. / Louis, C. / Botez-Pop, I. / Lestage, P. / Danober, L. / Kastrup, J.S. / Pirotte, B.
#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: Noerholm, A.B. / Francotte, P. / Olsen, L. / Krintel, C. / Frydenvang, K. / Goffin, E. / Challal, S. / Danober, L. / Botez-Pop, I. / Lestage, P. / Pirotte, B. / Kastup, J.S.
#2: Journal: Biochem. J. / Year: 2012
Title: Thermodynamics and structural analysis of positive allosteric modulation of the ionotropic glutamate receptor GluA2.
Authors: Krintel, C. / Frydenvang, K. / Olsen, L. / Kristensen, M.T. / de Barrios, O. / Naur, P. / Francotte, P. / Pirotte, B. / Gajhede, M. / Kastrup, J.S.
History
DepositionJul 24, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Nov 19, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 10, 2014Group: Database references
Revision 1.2Jan 17, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.3Jun 13, 2018Group: Data collection / Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.pdbx_pdb_strand_id
Revision 1.4Dec 20, 2023Group: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.5Nov 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,Glutamate receptor 2
B: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,51624
Polymers58,4892
Non-polymers2,02722
Water7,242402
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6030 Å2
ΔGint-62 kcal/mol
Surface area22990 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.830, 121.370, 47.330
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11B-947-

HOH

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Components

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Protein , 1 types, 2 molecules AB

#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: 29244.678 Da / Num. of mol.: 2 / Fragment: UNP residues 413-527, UNP residues 653-796 / Mutation: yes
Source method: isolated from a genetically manipulated source
Details: AMPA RECEPTOR LIGAND BINDING DOMAIN, GLUA2 S1S2J-L483Y-N754S, UNP RESIDUES 413-527 AND 653-796; CRYSTALLIZED WITH ALLOSTERIC MODULATOR BPAM-25. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED ...Details: AMPA RECEPTOR LIGAND BINDING DOMAIN, GLUA2 S1S2J-L483Y-N754S, UNP RESIDUES 413-527 AND 653-796; CRYSTALLIZED WITH ALLOSTERIC MODULATOR BPAM-25. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR LINKER (118-119). THE FIRST TWO RESIDUES (GLY, ALA) ARE CLONING REMNANTS.
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Plasmid: pET-22b(+) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): ORIGAMI 2 / References: UniProt: P19491

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Non-polymers , 8 types, 424 molecules

#2: Chemical ChemComp-3C1 / 4-ethyl-3,4-dihydro-2H-pyrido[4,3-e][1,2,4]thiadiazine 1,1-dioxide


Mass: 213.257 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H11N3O2S
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-GLU / GLUTAMIC ACID


Type: L-peptide linking / Mass: 147.129 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H9NO4
#8: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


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


Mass: 18.015 Da / Num. of mol.: 402 / 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: 2.4 Å3/Da / Density % sol: 48.79 %
Crystal growTemperature: 280 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 22% PEG4000, 0.2 M ammoniumsulfate, 0.1 M 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: Dec 15, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→34.87 Å / Num. all: 45062 / Num. obs: 45062 / % possible obs: 99.7 % / Redundancy: 4.7 % / Biso Wilson estimate: 16.1 Å2 / Rpim(I) all: 0.045 / Rrim(I) all: 0.1 / Rsym value: 0.089 / Net I/av σ(I): 5.736 / Net I/σ(I): 11.1 / Num. measured all: 210081
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRpim(I) allRsym valueNet I/σ(I) obs% possible all
1.9-24.70.3082.33020464910.1510.3084.7100
2-2.124.70.1973.62883161590.0960.1976.6100
2.12-2.274.70.1464.82729458420.0720.1468.3100
2.27-2.454.70.1235.52531354040.0610.1239.6100
2.45-2.694.70.0966.92341450130.0480.09611.1100
2.69-34.70.0768.32135045700.0380.07613.3100
3-3.474.70.0698.41884440500.0360.06916.5100
3.47-4.254.70.0697.71598734280.0360.06919.599.5
4.25-6.014.70.0599.21233626380.030.05919.998.2
6.01-34.0144.40.04113.3650814670.0220.04118.794.7

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Processing

Software
NameVersionClassification
SCALA3.3.20data scaling
PDB_EXTRACT3.14data extraction
PHENIX(phenix.refine: 1.8.4_1496)refinement
PHASERphasing
Cootmodel building
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1LB8, mol A

1lb8


Resolution: 1.9→34.014 Å / FOM work R set: 0.8634 / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.08 / Phase error: 19.82 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2082 4180 4.99 %
Rwork0.1586 79522 -
obs0.161 45017 97.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 95.31 Å2 / Biso mean: 21.28 Å2 / Biso min: 4.25 Å2
Refinement stepCycle: final / Resolution: 1.9→34.014 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4055 0 128 402 4585
Biso mean--34.32 29.26 -
Num. residues----519
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0074313
X-RAY DIFFRACTIONf_angle_d1.025803
X-RAY DIFFRACTIONf_chiral_restr0.043629
X-RAY DIFFRACTIONf_plane_restr0.004725
X-RAY DIFFRACTIONf_dihedral_angle_d13.9891646
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9-1.92160.2391250.1952593271897
1.9216-1.94420.24571300.20012679280997
1.9442-1.96790.27561120.20142669278197
1.9679-1.99280.24081400.19252621276197
1.9928-2.0190.21021450.18952604274997
2.019-2.04670.23191710.16542689286097
2.0467-2.07590.19181240.16622634275898
2.0759-2.10690.18221280.15672609273797
2.1069-2.13980.22181250.1552728285398
2.1398-2.17490.18341520.14932660281297
2.1749-2.21240.17091250.16022609273498
2.2124-2.25260.20731310.15692702283398
2.2526-2.29590.2391530.16552608276198
2.2959-2.34280.1851590.16262655281498
2.3428-2.39370.20551520.1682644279698
2.3937-2.44940.25321400.16012628276898
2.4494-2.51060.23731790.17222655283498
2.5106-2.57850.21341360.17382635277198
2.5785-2.65430.21361250.15642700282598
2.6543-2.740.18921130.15422671278498
2.74-2.83780.20351720.16732646281898
2.8378-2.95140.24291440.1662699284398
2.9514-3.08570.2281600.17262604276498
3.0857-3.24820.25251380.15792669280798
3.2482-3.45150.19661530.15412655280898
3.4515-3.71770.17491190.13922712283198
3.7177-4.09130.21171340.12982654278898
4.0913-4.6820.16671340.1252683281798
4.682-5.89390.16411280.14842647277597
5.8939-34.01930.21711330.18032560269394
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)
10.0784-0.0004-0.02470.00710.00950.0342-0.0088-0.0344-0.0887-0.0013-0.00760.00370.015-0.00410.0110.1770.02630.05010.01470.0626-0.011-15.263921.4215-7.5347
20.01960.01840.00530.01750.00860.006-0.0194-0.0117-0.0435-0.0902-0.01420.10290.0622-0.0237-0.02230.16860.00020.00070.04880.01140.0867-21.151120.1838-8.8767
30.00610.00520.00750.00460.00810.04430.02170.0468-0.0059-0.106-0.0562-0.06240.13450.0277-0.01620.18640.04290.0250.08280.01030.0965-10.370226.7109-14.0478
40.00170.00020.00080.00370.00490.00540.02150.02380.007-0.03350.0076-0.00350.04210.07270.00360.12140.03810.03890.13020.01610.0677-1.365633.5854-17.193
50.17070.0227-0.03890.0792-0.03380.0145-0.0149-0.05140.0322-0.0491-0.0616-0.00710.09440.1112-0.03260.08270.0186-0.00040.09290.02370.067-10.022237.3747-4.8019
60.0163-0.02550.02380.0808-0.06760.193-0.0574-0.10520.070.0039-0.1522-0.12530.01870.2438-0.1633-0.15380.1282-0.05980.22750.12630.1853.881640.58532.7536
70.1320.02220.02080.0271-0.04770.1119-0.0794-0.0737-0.035-0.013-0.1301-0.14240.05470.1858-0.19560.11950.0960.01980.19250.08340.0686-5.080130.49838.5032
80.0077-0.0010.00550.0031-0.00820.006-0.0843-0.0519-0.07740.0585-0.07220.04260.0501-0.0092-00.15060.03230.02030.17510.02410.1391-9.974634.531511.1599
90.01350.0165-0.00590.0839-0.02840.01040.0023-0.00340.0883-0.04090.06170.16220.06820.02860.02510.1066-0.001-0.0050.07170.01330.0904-22.251337.3202-13.8199
100.00840.0154-0.00120.0231-0.0044-0.00050.0115-0.0265-0.00480.0526-0.0278-0.00240.0418-0.0034-0.0130.1957-0.00040.09220.05790.04290.0911-23.854929.03074.5847
110.03840.01350.02010.0230.0030.00990.08350.0250.1039-0.02220.0380.0086-0.0850.06690.00590.1032-0.01080.02310.0831-0.01240.0816-22.349466.964-9.7877
120.06960.01650.06880.00410.01370.08030.1656-0.06070.13230.0032-0.0254-0.0507-0.17870.0590.06220.1252-0.02110.0570.0628-0.01720.1193-17.164468.5648-8.5898
130.00950.0039-0.01770.011-0.01020.03820.04710.03780.0239-0.0605-0.0010.0437-0.0661-0.05410.02080.08680.00650.00830.06470.00240.0709-28.435762.5214-13.649
140.0029-0.0017-0.00120.0031-0.00280.00370.01380.01970.0079-0.0296-0.00790.0344-0.0075-0.0901-0.01160.07390.0012-0.01930.09810.01450.0797-37.203155.6471-17.1844
150.0198-0.03060.00910.0261-0.00590.01230.0219-0.0223-0.0142-0.0336-0.01510.0421-0.04060.016900.05870.0127-0.00450.05340.00060.0547-27.28451.9689-8.7113
160.0479-0.0618-0.01110.3858-0.05210.0167-0.02330.0711-0.18960.08210.03160.04680.0147-0.00880.01230.0179-0.0250.01540.099-0.00530.0962-39.691947.63996.3387
170.00210.00410.00490.0040.01080.0357-0.0074-0.001-0.01760.0195-0.05430.0690.0029-0.1315-0.01210.0594-0.01260.01170.0989-0.01770.1672-45.180849.78482.6091
180.01150.00210.00920.0034-0.00110.0123-0.03290.02240.05030.05660.00590.0184-0.0146-0.0279-0.00070.07360.01790.0080.0558-0.01570.0873-38.825461.502610.7508
190.01820.01170.00620.01770.00580.00250.0281-0.0206-0.04840.06340.0303-0.0473-0.0035-0.02430.00110.05380.00570.01040.0716-0.01310.0469-29.438456.08076.7962
200.0072-0.0016-0.00930.00110.00440.0058-0.0463-0.07950.04690.0373-0.0174-0.03730.00540.0515-0.00160.1090.01590.00180.1126-0.01950.1188-28.399154.394111.1177
210-0.00410.00030.01770.01310.0169-0.01590.0327-0.0669-0.05080.0311-0.0325-0.0040.05770.00040.06160.00370.00860.0699-0.00260.0864-16.774951.6801-13.9999
220.01170.00860.00190.00820.00330.00050.0567-0.08960.03420.0487-0.013-0.0165-0.02010.04110.0030.0549-0.015-0.01120.1086-0.030.0929-14.547759.80865.1098
230.0040.0039-0.00040.02430.00630.0036-0.0010.0093-0.0198-0.01720.0068-0.03010.04880.0156-0.0050.12020.0625-0.00010.1258-0.00470.0477-19.283744.4139-4.011
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 4 through 22 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 23 through 47 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 48 through 65 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 66 through 79 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 80 through 123 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 124 through 173 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 174 through 202 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 203 through 217 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 218 through 244 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 245 through 261 )A0
11X-RAY DIFFRACTION11chain 'B' and (resid 1 through 22 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 23 through 47 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 48 through 65 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 66 through 79 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 80 through 116 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 117 through 152 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 153 through 173 )B0
18X-RAY DIFFRACTION18chain 'B' and (resid 174 through 187 )B0
19X-RAY DIFFRACTION19chain 'B' and (resid 188 through 202 )B0
20X-RAY DIFFRACTION20chain 'B' and (resid 203 through 217 )B0
21X-RAY DIFFRACTION21chain 'B' and (resid 218 through 243 )B0
22X-RAY DIFFRACTION22chain 'B' and (resid 244 through 263 )B0
23X-RAY DIFFRACTION23chain 'L' and (resid 3 through 4 )L0

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