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- PDB-6hch: STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-L504Y-N775S) IN C... -

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Basic information

Entry
Database: PDB / ID: 6hch
TitleSTRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-L504Y-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM01 AT 1.6 A RESOLUTION.
ComponentsGlutamate receptor 2GRIA2
KeywordsMEMBRANE PROTEIN / ampa receptor / gluA2 / ligand-binding domain / glua2-S1S2J-L504Y-N775S / signaling protein / positive allosteric modulator
Function / homology
Function and homology information


spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / response to lithium ion / perisynaptic space / cellular response to glycine / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / immunoglobulin binding ...spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / response to lithium ion / perisynaptic space / cellular response to glycine / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / immunoglobulin binding / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / asymmetric synapse / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / positive regulation of synaptic transmission / glutamate-gated receptor activity / presynaptic active zone membrane / response to fungicide / regulation of synaptic transmission, glutamatergic / cellular response to brain-derived neurotrophic factor stimulus / somatodendritic compartment / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor binding / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / cytoskeletal protein binding / SNARE binding / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / dendritic shaft / synaptic membrane / synaptic transmission, glutamatergic / PDZ domain binding / postsynaptic density membrane / protein tetramerization / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / establishment of protein localization / terminal bouton / receptor internalization / synaptic vesicle membrane / cerebral cortex development / synaptic vesicle / presynapse / signaling receptor activity / presynaptic membrane / amyloid-beta binding / growth cone / perikaryon / chemical synaptic transmission / scaffold protein binding / postsynaptic membrane / dendritic spine / postsynaptic density / neuron projection / axon / neuronal cell body / dendrite / synapse / glutamatergic synapse / protein-containing complex binding / endoplasmic reticulum membrane / protein kinase binding / cell surface / endoplasmic reticulum / protein-containing complex / membrane / identical protein binding / plasma membrane
Similarity search - Function
Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. ...Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / 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
ACETATE ION / Chem-D45 / GLUTAMIC ACID / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsLaulumaa, S. / Hansen, K.V. / Frydenvang, K. / Kastrup, J.S.
CitationJournal: Acs Med.Chem.Lett. / Year: 2019
Title: Crystal Structures of Potent Dimeric Positive Allosteric Modulators at the Ligand-Binding Domain of the GluA2 Receptor.
Authors: Laulumaa, S. / Hansen, K.V. / Masternak, M. / Drapier, T. / Francotte, P. / Pirotte, B. / Frydenvang, K. / Kastrup, J.S.
History
DepositionAug 15, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 3, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 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
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_alt_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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_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_alt_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.ptnr3_symmetry / _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.ptnr1_symmetry / _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

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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)91,55545
Polymers87,9053
Non-polymers3,65042
Water14,448802
1
A: Glutamate receptor 2
B: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,72427
Polymers58,6032
Non-polymers2,12125
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Glutamate receptor 2
hetero molecules

C: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,66236
Polymers58,6032
Non-polymers3,05834
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_465-x-1,-y+1,z1
Unit cell
Length a, b, c (Å)114.630, 163.580, 47.528
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 1 through 15 or resid 17...
21(chain B and (resid 1 through 15 or resid 17...
31(chain C and (resid 1 through 15 or resid 17...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 1 through 15 or resid 17...A1 - 15
121(chain A and (resid 1 through 15 or resid 17...A17
131(chain A and (resid 1 through 15 or resid 17...A20 - 23
141(chain A and (resid 1 through 15 or resid 17...A0
151(chain A and (resid 1 through 15 or resid 17...A1
161(chain A and (resid 1 through 15 or resid 17...A109 - 115
171(chain A and (resid 1 through 15 or resid 17...A165 - 175
181(chain A and (resid 1 through 15 or resid 17...A1 - 263
191(chain A and (resid 1 through 15 or resid 17...A1195
1101(chain A and (resid 1 through 15 or resid 17...A197
1111(chain A and (resid 1 through 15 or resid 17...A197
1121(chain A and (resid 1 through 15 or resid 17...A2
1131(chain A and (resid 1 through 15 or resid 17...A218 - 2221
1141(chain A and (resid 1 through 15 or resid 17...A223 - 23
1151(chain A and (resid 1 through 15 or resid 17...A233 - 239
1161(chain A and (resid 1 through 15 or resid 17...A241 - 245
1171(chain A and (resid 1 through 15 or resid 17...A247 - 262
211(chain B and (resid 1 through 15 or resid 17...B1 - 15
221(chain B and (resid 1 through 15 or resid 17...B17
231(chain B and (resid 1 through 15 or resid 17...B20 - 23
241(chain B and (resid 1 through 15 or resid 17...B2
251(chain B and (resid 1 through 15 or resid 17...B0
261(chain B and (resid 1 through 15 or resid 17...B78 - 106
271(chain B and (resid 1 through 15 or resid 17...B1 - 262
281(chain B and (resid 1 through 15 or resid 17...B165 - 175
291(chain B and (resid 1 through 15 or resid 17...B197
2101(chain B and (resid 1 through 15 or resid 17...B197
2111(chain B and (resid 1 through 15 or resid 17...B200 - 208
2121(chain B and (resid 1 through 15 or resid 17...B211 - 216
2131(chain B and (resid 1 through 15 or resid 17...B223 - 231
2141(chain B and (resid 1 through 15 or resid 17...B223 - 231
2151(chain B and (resid 1 through 15 or resid 17...B241 - 245
2161(chain B and (resid 1 through 15 or resid 17...B247 - 262
311(chain C and (resid 1 through 15 or resid 17...C1 - 15
321(chain C and (resid 1 through 15 or resid 17...C17
331(chain C and (resid 1 through 15 or resid 17...C20
341(chain C and (resid 1 through 15 or resid 17...C78 - 1009
351(chain C and (resid 1 through 15 or resid 17...C117 - 163
361(chain C and (resid 1 through 15 or resid 17...C165 - 175
371(chain C and (resid 1 through 15 or resid 17...C185 - 195
381(chain C and (resid 1 through 15 or resid 17...C200 - 208
391(chain C and (resid 1 through 15 or resid 17...C223 - 231
3101(chain C and (resid 1 through 15 or resid 17...C233 - 239
3111(chain C and (resid 1 through 15 or resid 17...C241 - 245
3121(chain C and (resid 1 through 15 or resid 17...C247 - 262

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein Glutamate receptor 2 / GRIA2 / 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
Source method: isolated from a genetically manipulated source
Details: NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE CRYSTALLIZED PROTEIN IS A L540Y-N775S-MUTANT OF THE GLUA2 LIGAND-BINDING DOMAIN. TRANSMEMBRANE REGIONS ARE REPLACED WITH A GLY-THR LINKER (RESIDUES ...Details: NATIVE GLUA2 IS A MEMBRANE PROTEIN. THE CRYSTALLIZED PROTEIN IS A L540Y-N775S-MUTANT OF THE GLUA2 LIGAND-BINDING DOMAIN. TRANSMEMBRANE REGIONS ARE REPLACED WITH A GLY-THR LINKER (RESIDUES 118-119) AND GLY1-ALA2 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 / Plasmid: pET22b(+) / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Origami B / References: UniProt: P19491

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Non-polymers , 8 types, 844 molecules

#2: Chemical ChemComp-GLU / GLUTAMIC ACID / Glutamic acid


Type: L-peptide linking / Mass: 147.129 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C5H9NO4
#3: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-D45 / 6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide)


Mass: 422.522 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H22N4O4S2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 802 / Source method: isolated from a natural source / Formula: H2O

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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: 5.5
Details: 15% PEG4000, 0.1 M zinc acetate, 0.1 M sodium acetate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 30, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.6→49.24 Å / Num. all: 118901 / Num. obs: 118901 / % possible obs: 100 % / Redundancy: 13.3 % / Biso Wilson estimate: 19.65 Å2 / Rpim(I) all: 0.028 / Rrim(I) all: 0.104 / Rsym value: 0.1 / Net I/av σ(I): 4.1 / Net I/σ(I): 13.6 / Num. measured all: 1579323
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsRpim(I) allRrim(I) allRsym value% possible all
1.6-1.6913.40.850.9171750.2390.8830.85100
1.69-1.7912.70.5581.3162310.1620.5810.558100
1.79-1.9112.60.3571.8153230.1040.3720.357100
1.91-2.0712.80.2242.6142740.0650.2330.224100
2.07-2.2613.90.1463.9131520.040.1520.146100
2.26-2.5313.90.1194.4119490.0330.1240.119100
2.53-2.9213.70.0985.1105740.0270.1010.098100
2.92-3.5813.60.0746.790330.0210.0770.074100
3.58-5.0613.80.0598.870770.0170.0610.059100
5.06-49.2412.60.0637.741130.0190.0660.06399.9

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1FTJ

1ftj


Resolution: 1.6→49.24 Å / SU ML: 0.14 / Cross valid method: THROUGHOUT / σ(F): 0.57 / Phase error: 16.4
RfactorNum. reflection% reflection
Rfree0.1783 5882 4.95 %
Rwork0.1549 --
obs0.1561 118768 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 122.69 Å2 / Biso mean: 28.966 Å2 / Biso min: 10.45 Å2
Refinement stepCycle: final / Resolution: 1.6→49.24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6135 0 215 815 7165
Biso mean--47.47 34.49 -
Num. residues----791
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3307X-RAY DIFFRACTION6.12TORSIONAL
12B3307X-RAY DIFFRACTION6.12TORSIONAL
13C3307X-RAY DIFFRACTION6.12TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.6-1.61820.22141970.205837303927
1.6182-1.63720.21141850.192837683953
1.6372-1.65720.23522200.191636513871
1.6572-1.67820.20632300.186636503880
1.6782-1.70030.20682050.182937483953
1.7003-1.72350.16681810.173837033884
1.7235-1.74820.21951800.172137353915
1.7482-1.77430.21311850.170637443929
1.7743-1.8020.20121800.182437263906
1.802-1.83150.21932190.179837343953
1.8315-1.86310.20131870.16936773864
1.8631-1.8970.19341890.16137543943
1.897-1.93350.19141850.157137283913
1.9335-1.9730.18551950.160337833978
1.973-2.01590.181750.150137123887
2.0159-2.06270.17661920.145437733965
2.0627-2.11430.191960.148436923888
2.1143-2.17150.16382000.148737933993
2.1715-2.23540.17882260.144636993925
2.2354-2.30760.16911870.143737573944
2.3076-2.390.17171920.147937823974
2.39-2.48570.17961990.151737653964
2.4857-2.59880.19352130.150737373950
2.5988-2.73580.16862130.146637633976
2.7358-2.90720.17681870.153637953982
2.9072-3.13170.17332060.152838064012
3.1317-3.44680.18311800.152938524032
3.4468-3.94530.14821820.140938714053
3.9453-4.96990.14731870.128238794066
4.9699-49.26310.19652090.190740794288
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)
10.2667-0.0747-0.02550.2045-0.1450.11-0.0134-0.01340.11970.0947-0.01120.07110.01360.028900.1314-0.00730.00310.1337-0.00120.1353-49.482.996615.3644
20.14160.0571-0.01470.09180.01410.0351-0.0080.14520.1448-0.41910.1737-0.0729-0.27980.0505-0.00040.225-0.03030.04850.25020.02330.1916-41.108681.8962-3.948
30.8454-0.14980.02570.8706-0.2070.94850.0057-0.02530.01650.0473-0.0119-0.1131-0.0510.1077-00.127-0.0074-0.00230.14570.00270.1351-36.497337.65563.2176
40.8257-0.1986-0.59630.57510.2510.8013-0.01940.0203-0.0776-0.037-0.03310.01320.0370.03500.14680.0135-0.01180.13160.00950.1431-39.131325.7919-10.8436
50.4977-0.2529-0.51750.61380.09760.5695-0.0122-0.0465-0.1641-0.0894-0.02970.02890.0997-0.086600.2268-0.0558-0.02760.1997-0.0070.2097-67.47578.23490.244
60.661-0.02730.27830.3159-0.03730.73280.0069-0.04810.0254-0.03720.00530.0221-0.03-0.104500.1494-0.0162-0.00860.1556-0.00430.1511-67.761124.78660.3009
70.9638-0.2119-0.22740.54410.11910.9420.04410.0220.31270.02390.00480.0944-0.0561-0.28510.00310.19890.00940.00210.2161-0.00050.2673-72.907632.816-14.0511
80.9031-0.04930.24960.65-0.36070.2376-0.00950.0905-0.0954-0.12840.0146-0.13820.09540.0013-0.00010.1995-0.030.01080.1605-0.0270.171-59.276417.9113-7.4915
90.53670.43580.17150.5526-0.15390.6859-0.0330.0279-0.02980.03780.0455-0.08340.01950.2799-0.00030.12360.0140.00780.2282-0.01590.1479-35.027675.439210.5401
100.1053-0.1135-0.03250.11150.03250.48670.003-0.0685-0.12160.18280.036-0.07440.16980.0925-00.17550.02150.00710.1739-0.00730.169-42.297968.757315.4768
110.4365-0.2711-0.14480.24570.20960.2399-0.0761-0.0833-0.0534-0.00320.10220.01260.43760.12660.0540.2272-0.01050.01240.12810.04390.1371-51.051861.708518.747
120.0678-0.06710.18740.21010.03030.2805-0.0394-0.0164-0.010.00250.0160.03110.0290.0244-00.131-0.00150.01090.1460.00310.1361-51.994372.352610.2683
130.59340.2824-0.22720.87210.25890.2579-0.00910.03-0.02320.041-0.02160.20090.1022-0.0081-0.00040.1406-0.00090.00840.12590.00230.1831-59.46361.4487-4.8319
140.0537-0.0049-0.09970.16170.10620.3398-0.04730.05540.00120.0988-0.02580.14290.154-0.023800.1726-0.00340.02230.13210.00170.2264-58.742355.6575-1.2464
150.33350.0061-0.07370.0853-0.01940.1158-0.003-0.0672-0.07950.0078-0.0443-0.09390.04870.0957-0.00020.14870.00460.01750.14250.00680.1287-47.23565.1374-6.8894
160.09660.1197-0.03250.2580.21250.16140.049-0.11970.0919-0.1483-0.00380.007-0.1390.12350.00010.18250.00040.00090.2160.00790.1495-50.24870.7773-9.5705
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'C' and (resid 218 through 244 )C218 - 244
2X-RAY DIFFRACTION2chain 'C' and (resid 245 through 263 )C245 - 263
3X-RAY DIFFRACTION3chain 'A' and (resid 1 through 93 )A1 - 93
4X-RAY DIFFRACTION4chain 'A' and (resid 94 through 263 )A94 - 263
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 47 )B1 - 47
6X-RAY DIFFRACTION6chain 'B' and (resid 48 through 123 )B48 - 123
7X-RAY DIFFRACTION7chain 'B' and (resid 124 through 202 )B124 - 202
8X-RAY DIFFRACTION8chain 'B' and (resid 203 through 262 )B203 - 262
9X-RAY DIFFRACTION9chain 'C' and (resid 1 through 47 )C1 - 47
10X-RAY DIFFRACTION10chain 'C' and (resid 48 through 65 )C48 - 65
11X-RAY DIFFRACTION11chain 'C' and (resid 66 through 79 )C66 - 79
12X-RAY DIFFRACTION12chain 'C' and (resid 80 through 116 )C80 - 116
13X-RAY DIFFRACTION13chain 'C' and (resid 117 through 152 )C117 - 152
14X-RAY DIFFRACTION14chain 'C' and (resid 153 through 173 )C153 - 173
15X-RAY DIFFRACTION15chain 'C' and (resid 174 through 202 )C174 - 202
16X-RAY DIFFRACTION16chain 'C' and (resid 203 through 217 )C203 - 217

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