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- PDB-3kg2: AMPA subtype ionotropic glutamate receptor in complex with compet... -

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Basic information

Entry
Database: PDB / ID: 3kg2
TitleAMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775
ComponentsGlutamate receptor 2
Keywordsmembrane protein / transport protein / ion channel / Cell membrane / Glycoprotein / Ion transport / Membrane / Postsynaptic cell membrane / Receptor / RNA editing / Synapse / Transmembrane / Transport / tetramer
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 / AMPA glutamate receptor complex / cellular response to glycine / 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 / extracellular ligand-gated monoatomic ion channel activity / cellular response to brain-derived neurotrophic factor stimulus / presynaptic active zone membrane / glutamate-gated calcium ion channel activity / 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 / presynapse / signaling receptor activity / amyloid-beta binding / presynaptic membrane / growth cone / scaffold protein binding / perikaryon / chemical synaptic transmission / dendritic spine / postsynaptic membrane / neuron projection / postsynaptic density / axon / external side of plasma membrane / neuronal cell body / dendrite / synapse / 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
Helix Hairpins - #70 / Response regulator / 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. ...Helix Hairpins - #70 / Response regulator / 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 / Helix Hairpins / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-ZK1 / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.6 Å
AuthorsSobolevsky, A.I. / Rosconi, M.P. / Gouaux, E.
CitationJournal: Nature / Year: 2009
Title: X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor.
Authors: Sobolevsky, A.I. / Rosconi, M.P. / Gouaux, E.
History
DepositionOct 28, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Mar 21, 2012Group: Database references
Revision 1.3May 27, 2015Group: Refinement description
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 13, 2021Group: Database references / Structure summary / Category: chem_comp / database_2 / struct_ref_seq_dif
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 2.2Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 2.3Oct 30, 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
D: Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)372,48012
Polymers368,1724
Non-polymers4,3078
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25170 Å2
ΔGint-194 kcal/mol
Surface area135070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.715, 109.848, 161.130
Angle α, β, γ (deg.)85.32, 84.75, 78.92
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
13
23
14
24
34
44
15
25
35
45
16
26
36
46
17
27
37
47
18
28
19
29
110
210
310
410
111
211
311
411
112
212
312
412
113
213
313
413

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and resid 10:306
211chain B and resid 10:306
311chain C and resid 10:306
411chain D and resid 10:306
112chain A and resid 307:311
212chain D and resid 307:311
113chain B and resid 307:311
213chain C and resid 307:311
114chain A and resid 312:381
214chain B and resid 312:381
314chain C and resid 312:381
414chain D and resid 312:381
115chain A and resid 396:503
215chain B and resid 396:503
315chain C and resid 396:503
415chain D and resid 396:503
116chain A and resid 513:544
216chain B and resid 513:544
316chain C and resid 513:544
416chain D and resid 513:544
117chain A and resid 568:621
217chain B and resid 568:621
317chain C and resid 568:621
417chain D and resid 568:621
118chain A and resid 622:634
218chain C and resid 622:634
119chain B and resid 622:634
219chain D and resid 622:634
1110chain A and resid 635:773
2110chain B and resid 635:773
3110chain C and resid 635:773
4110chain D and resid 635:773
1111chain A and resid 775:780
2111chain B and resid 775:780
3111chain C and resid 775:780
4111chain D and resid 775:780
1112chain A and resid 788:817
2112chain B and resid 788:817
3112chain C and resid 788:817
4112chain D and resid 788:817
1113chain A and resid 818
2113chain B and resid 818
3113chain C and resid 818
4113chain D and resid 818

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13

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Components

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


Mass: 92043.039 Da / Num. of mol.: 4 / Fragment: sequence database residues 25-847
Mutation: N241E, N385D, N392Q, K410A, E413A, M414A, E416A, and C589A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P19491
#2: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#4: Chemical
ChemComp-ZK1 / {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / [[3,4-Dihydro-7-(4-morpholinyl)-2,3-dioxo-6-(trifluorom ethyl)-1(2H)-quinoxalinyl]methyl]phosphonic acid


Mass: 409.254 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H15F3N3O6P / Comment: medication*YM
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 3

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Sample preparation

CrystalDensity Matthews: 4.25 Å3/Da / Density % sol: 71.08 %
Crystal growTemperature: 277 K / Details: Under paraffin oil, temperature 277K / PH range: 6.0-6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 18, 2008
Details: VERTICALLY COLLIMATING PREMIRROR, LN2 COOLED DOUBLE- CRYSTAL SILICON (111) MONOCHROMATOR, TOROIDAL FOCUSING M2 MIRROR
RadiationMonochromator: DOUBLE-CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.6→50 Å / Num. obs: 69301 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 9.7 % / Biso Wilson estimate: 136.41 Å2 / Rmerge(I) obs: 0.111 / Net I/σ(I): 17.2
Reflection shellResolution: 3.6→3.73 Å / Redundancy: 9.2 % / Rmerge(I) obs: 0.981 / Mean I/σ(I) obs: 2.08 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 3H5V and 1FTL

3h5v

1ftl


Resolution: 3.6→49.89 Å / SU ML: 0.01 / σ(F): 1.96 / Phase error: 33.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.296 3483 5.03 %
Rwork0.286 --
obs0.287 69301 98.8 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 58.87 Å2 / ksol: 0.21 e/Å3
Displacement parametersBiso mean: 192.72 Å2
Baniso -1Baniso -2Baniso -3
1--15.6279 Å2-1.4252 Å235.0738 Å2
2--14.5974 Å2-13.3631 Å2
3---1.0304 Å2
Refinement stepCycle: LAST / Resolution: 3.6→49.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22400 0 286 0 22686
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00223200
X-RAY DIFFRACTIONf_angle_d0.44231770
X-RAY DIFFRACTIONf_dihedral_angle_d9.6967414
X-RAY DIFFRACTIONf_chiral_restr0.0273788
X-RAY DIFFRACTIONf_plane_restr0.0024032
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2209X-RAY DIFFRACTIONPOSITIONAL
12B2209X-RAY DIFFRACTIONPOSITIONAL0.005
13C2209X-RAY DIFFRACTIONPOSITIONAL0.004
14D2209X-RAY DIFFRACTIONPOSITIONAL0.004
21A28X-RAY DIFFRACTIONPOSITIONAL
22D28X-RAY DIFFRACTIONPOSITIONAL0.003
31B28X-RAY DIFFRACTIONPOSITIONAL
32C28X-RAY DIFFRACTIONPOSITIONAL0.004
41A498X-RAY DIFFRACTIONPOSITIONAL
42B498X-RAY DIFFRACTIONPOSITIONAL0.005
43C498X-RAY DIFFRACTIONPOSITIONAL0.004
44D498X-RAY DIFFRACTIONPOSITIONAL0.004
51A793X-RAY DIFFRACTIONPOSITIONAL
52B793X-RAY DIFFRACTIONPOSITIONAL0.004
53C793X-RAY DIFFRACTIONPOSITIONAL0.004
54D793X-RAY DIFFRACTIONPOSITIONAL0.004
61A254X-RAY DIFFRACTIONPOSITIONAL
62B254X-RAY DIFFRACTIONPOSITIONAL0.002
63C254X-RAY DIFFRACTIONPOSITIONAL0.003
64D254X-RAY DIFFRACTIONPOSITIONAL0.003
71A310X-RAY DIFFRACTIONPOSITIONAL
72B310X-RAY DIFFRACTIONPOSITIONAL0.007
73C310X-RAY DIFFRACTIONPOSITIONAL0.006
74D310X-RAY DIFFRACTIONPOSITIONAL0.006
81A95X-RAY DIFFRACTIONPOSITIONAL
82C95X-RAY DIFFRACTIONPOSITIONAL0.133
91B95X-RAY DIFFRACTIONPOSITIONAL
92D95X-RAY DIFFRACTIONPOSITIONAL0.022
101A995X-RAY DIFFRACTIONPOSITIONAL
102B995X-RAY DIFFRACTIONPOSITIONAL0.005
103C995X-RAY DIFFRACTIONPOSITIONAL0.004
104D995X-RAY DIFFRACTIONPOSITIONAL0.004
111A29X-RAY DIFFRACTIONPOSITIONAL
112B29X-RAY DIFFRACTIONPOSITIONAL0.023
113C29X-RAY DIFFRACTIONPOSITIONAL0.007
114D29X-RAY DIFFRACTIONPOSITIONAL0.013
121A217X-RAY DIFFRACTIONPOSITIONAL
122B217X-RAY DIFFRACTIONPOSITIONAL0.003
123C217X-RAY DIFFRACTIONPOSITIONAL0.004
124D217X-RAY DIFFRACTIONPOSITIONAL0.004
131A27X-RAY DIFFRACTIONPOSITIONAL
132B27X-RAY DIFFRACTIONPOSITIONAL0.003
133C27X-RAY DIFFRACTIONPOSITIONAL0.003
134D27X-RAY DIFFRACTIONPOSITIONAL0.002
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.6029-3.65230.45641270.42574X-RAY DIFFRACTION94
3.6523-3.70440.43551400.38982589X-RAY DIFFRACTION100
3.7044-3.75970.36511380.37322669X-RAY DIFFRACTION99
3.7597-3.81840.34591330.37182647X-RAY DIFFRACTION99
3.8184-3.8810.38631450.36672623X-RAY DIFFRACTION99
3.881-3.94790.36081420.36622653X-RAY DIFFRACTION98
3.9479-4.01970.36461460.35232586X-RAY DIFFRACTION99
4.0197-4.09690.2791530.33752605X-RAY DIFFRACTION98
4.0969-4.18050.32991330.32562601X-RAY DIFFRACTION98
4.1805-4.27140.34721680.32072612X-RAY DIFFRACTION98
4.2714-4.37070.3241270.29522626X-RAY DIFFRACTION99
4.3707-4.47990.30251420.29182616X-RAY DIFFRACTION99
4.4799-4.6010.28911350.27882661X-RAY DIFFRACTION99
4.601-4.73630.32021320.27862625X-RAY DIFFRACTION99
4.7363-4.8890.33091370.26312615X-RAY DIFFRACTION99
4.889-5.06360.26871450.26692669X-RAY DIFFRACTION99
5.0636-5.26610.2831510.27282613X-RAY DIFFRACTION99
5.2661-5.50550.28681440.27892650X-RAY DIFFRACTION100
5.5055-5.79530.26391320.28072667X-RAY DIFFRACTION100
5.7953-6.15780.28121240.28592679X-RAY DIFFRACTION100
6.1578-6.63230.2981270.25362664X-RAY DIFFRACTION100
6.6323-7.29790.28821430.25472656X-RAY DIFFRACTION100
7.2979-8.34960.24411420.22882670X-RAY DIFFRACTION100
8.3496-10.50350.20751380.1982667X-RAY DIFFRACTION100
10.5035-49.89230.27581390.30092581X-RAY DIFFRACTION97
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)
14.18660.8276-2.76563.5819-0.63384.4906-0.4393-0.4141-0.20530.11490.13890.36730.4525-0.0347-0.00011.17550.1172-0.0940.9922-0.07651.2748-54.2082-14.6743-29.0048
27.02021.8649-0.41233.78530.48651.6963-0.0033-0.062-0.12820.2306-0.08140.13330.0655-0.1767-00.96970.052-0.14261.086-0.10241.0511-59.824417.1572-15.8351
32.1580.53190.20522.2389-0.20644.1410.1953-0.9780.4810.9470.15880.3133-1.39370.4532-02.0145-0.12120.02632.2069-0.30131.5458-13.173261.071512.9931
42.91410.54811.05032.89310.42166.061-0.1626-1.4817-0.64421.1121-0.31810.15780.361-0.051-0.00021.10270.05760.06492.19480.19411.476-14.474226.245914.5404
54.2372.1328-0.67422.6953-0.27992.2275-0.35050.76750.1015-0.47250.26380.36040.0866-0.105-0.00011.4698-0.0416-0.11471.1687-0.03431.2136-18.6299.7851-65.4644
63.2927-0.3844-1.47911.77160.23363.61820.22180.62430.154-0.5232-0.09170.1772-0.4164-0.14140.00011.6782-0.0561-0.01440.890.04871.4563-15.039459.3039-53.7743
72.85730.2634-0.76822.44510.583.4729-0.08910.064-0.2942-0.18680.2535-0.58140.00031.1697-0.00011.5273-0.29390.11111.3939-0.13781.50736.973855.7359-39.5385
83.73880.68640.41781.7212-0.4822.34710.01850.1997-0.6461-0.4386-0.3051-0.55210.68610.559801.51680.1737-0.02531.30650.02021.30695.15664.2517-54.9975
94.24120.2272-0.83883.07350.09932.5848-0.18441.07250.1563-0.90050.2728-0.5289-0.08650.6428-01.91780.01860.16362.20260.27281.182324.604240.143-98.5753
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resid 10:381A10 - 381
2X-RAY DIFFRACTION2chain B and resid 10:381B10 - 381
3X-RAY DIFFRACTION3chain C and resid 10:381C10 - 381
4X-RAY DIFFRACTION4chain D and resid 10:381D10 - 381
5X-RAY DIFFRACTION5chain A and (resid 396:503 or resid 635:773)A396 - 503
6X-RAY DIFFRACTION5chain A and (resid 396:503 or resid 635:773)A635 - 773
7X-RAY DIFFRACTION6chain B and (resid 396:503 or resid 635:773)B396 - 503
8X-RAY DIFFRACTION6chain B and (resid 396:503 or resid 635:773)B635 - 773
9X-RAY DIFFRACTION7chain C and (resid 396:503 or resid 635:773)C396 - 503
10X-RAY DIFFRACTION7chain C and (resid 396:503 or resid 635:773)C635 - 773
11X-RAY DIFFRACTION8chain D and (resid 396:503 or resid 635:773)D396 - 503
12X-RAY DIFFRACTION8chain D and (resid 396:503 or resid 635:773)D635 - 773
13X-RAY DIFFRACTION9resid 513:544 or resid 568:634 or resid 788:8170

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