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- PDB-4u5c: Crystal structure of GluA2, con-ikot-ikot snail toxin, partial ag... -

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Basic information

Entry
Database: PDB / ID: 4u5c
TitleCrystal structure of GluA2, con-ikot-ikot snail toxin, partial agonist FW and postitive modulator (R,R)-2b complex
Components
  • Con-ikot-ikot
  • Glutamate receptor 2
KeywordsTransport protein/toxin / AMPA receptor / Transport protein-toxin complex
Function / homology
Function and homology information


host cell postsynaptic membrane / ion channel regulator activity / spine synapse / dendritic spine cytoplasm / dendritic spine neck / cellular response to amine stimulus / dendritic spine head / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / perisynaptic space ...host cell postsynaptic membrane / ion channel regulator activity / spine synapse / dendritic spine cytoplasm / dendritic spine neck / cellular response to amine stimulus / dendritic spine head / Activation of AMPA receptors / ligand-gated monoatomic cation channel activity / perisynaptic space / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / AMPA glutamate receptor clustering / kainate selective glutamate receptor activity / immunoglobulin binding / asymmetric synapse / AMPA glutamate receptor complex / regulation of receptor recycling / extracellularly glutamate-gated ion channel activity / cellular response to glycine / ionotropic glutamate receptor complex / conditioned place preference / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / positive regulation of synaptic transmission / response to fungicide / regulation of synaptic transmission, glutamatergic / cytoskeletal protein binding / glutamate-gated receptor activity / extracellular ligand-gated monoatomic ion channel activity / cellular response to brain-derived neurotrophic factor stimulus / regulation of long-term synaptic depression / somatodendritic compartment / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / excitatory synapse / ionotropic glutamate receptor binding / dendrite membrane / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / positive regulation of excitatory postsynaptic potential / synaptic membrane / 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 / receptor internalization / postsynaptic density membrane / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / terminal bouton / synaptic vesicle / long-term synaptic potentiation / synaptic vesicle membrane / amyloid-beta binding / toxin activity / presynapse / signaling receptor activity / growth cone / presynaptic membrane / scaffold protein binding / dendritic spine / chemical synaptic transmission / perikaryon / postsynaptic membrane / neuron projection / postsynaptic density / external side of plasma membrane / axon / neuronal cell body / synapse / dendrite / protein kinase binding / protein-containing complex binding / glutamatergic synapse / cell surface / endoplasmic reticulum / protein-containing complex / extracellular region / membrane / identical protein binding / plasma membrane
Similarity search - Function
Four Helix Bundle (Hemerythrin (Met), subunit A) - #1800 / 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. ...Four Helix Bundle (Hemerythrin (Met), subunit A) - #1800 / 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. / Four Helix Bundle (Hemerythrin (Met), subunit A) / 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 / Up-down Bundle / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-FWD / Chem-FWF / Con-ikot-ikot / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Conus striatus (striated cone)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.6883 Å
AuthorsChen, L. / Gouaux, E.
CitationJournal: Science / Year: 2014
Title: X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism.
Authors: Chen, L. / Durr, K.L. / Gouaux, E.
History
DepositionJul 25, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 13, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 27, 2014Group: Database references
Revision 1.2Oct 1, 2014Group: Database references
Revision 1.3Nov 22, 2017Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Refinement description / Source and taxonomy / Structure summary
Category: citation / entity ...citation / entity / entity_src_gen / pdbx_database_status / pdbx_struct_oper_list / software
Item: _citation.journal_id_CSD / _entity.pdbx_description ..._citation.journal_id_CSD / _entity.pdbx_description / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Refinement description / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / refine_hist / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Dec 27, 2023Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.6Nov 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
B: Glutamate receptor 2
C: Glutamate receptor 2
D: Glutamate receptor 2
E: Con-ikot-ikot
F: Con-ikot-ikot
hetero molecules


Theoretical massNumber of molelcules
Total (without water)387,76216
Polymers385,0486
Non-polymers2,71510
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30310 Å2
ΔGint-183 kcal/mol
Surface area141650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)163.070, 364.780, 109.750
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
11chain A and resid 8:383
21chain B and resid 8:383
31chain C and resid 8:383
41chain D and resid 8:383
12chain A and resid 393:505
22chain B and resid 393:505
32chain C and resid 393:505
42chain D and resid 393:505
13chain A and resid 635:769
23chain B and resid 635:769
33chain C and resid 635:769
43chain D and resid 635:769
14chain A and resid 523:544
24chain C and resid 523:544
34chain B and resid 523:544
44chain D and resid 523:544
15chain A and resid 610:622
25chain B and resid 610:622
35chain C and resid 610:622
45chain D and resid 610:622
16chain A and resid 790:816
26chain B and resid 790:816
36chain C and resid 790:816
46chain D and resid 790:816
17chain E and resid 1:100
27chain F and resid 1:100

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain A and resid 8:383A8 - 383
211chain B and resid 8:383B8 - 383
311chain C and resid 8:383C8 - 383
411chain D and resid 8:383D8 - 383
112chain A and resid 393:505A393 - 505
212chain B and resid 393:505B393 - 505
312chain C and resid 393:505C393 - 505
412chain D and resid 393:505D393 - 505
113chain A and resid 635:769A635 - 769
213chain B and resid 635:769B635 - 769
313chain C and resid 635:769C635 - 769
413chain D and resid 635:769D635 - 769
114chain A and resid 523:544A523 - 544
214chain C and resid 523:544C523 - 544
314chain B and resid 523:544B523 - 544
414chain D and resid 523:544D523 - 544
115chain A and resid 610:622A610 - 622
215chain B and resid 610:622B610 - 622
315chain C and resid 610:622C610 - 622
415chain D and resid 610:622D610 - 622
116chain A and resid 790:816A790 - 816
216chain B and resid 790:816B790 - 816
316chain C and resid 790:816C790 - 816
416chain D and resid 790:816D790 - 816
117chain E and resid 1:100E1 - 100
217chain F and resid 1:100F1 - 100

NCS ensembles :
ID
1
2
3
4
5
6
7

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Components

#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: 91385.320 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Gria2, Glur2 / Cell line (production host): HEK293S GNTI- / Production host: Homo sapiens (human) / References: UniProt: P19491
#2: Protein Con-ikot-ikot


Mass: 9753.155 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Conus striatus (striated cone) / Production host: Escherichia coli (E. coli) / References: UniProt: P0CB20
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#4: Chemical
ChemComp-FWD / 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID / FLUORO-WILLARDIINE


Mass: 217.155 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H8FN3O4
#5: Chemical ChemComp-FWF / N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide


Mass: 480.684 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H36N2O4S2
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: 4.24 Å3/Da / Density % sol: 70.98 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / Details: 0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 4, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.6883→148.87 Å / Num. obs: 69997 / % possible obs: 98.2 % / Redundancy: 3.7 % / Biso Wilson estimate: 116.87 Å2 / Net I/σ(I): 11.8
Reflection shellResolution: 3.6883→3.78 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.734 / Mean I/σ(I) obs: 1.9 / % possible all: 95.1

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Processing

Software
NameVersionClassification
PHENIXrefinement
XDSdata scaling
PDB_EXTRACT3.14data extraction
RefinementResolution: 3.6883→19.984 Å / FOM work R set: 0.8154 / SU ML: 0.51 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.46 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2536 3538 5.09 %
Rwork0.2073 66037 -
obs0.2097 69575 98.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 523.79 Å2 / Biso mean: 139.79 Å2 / Biso min: 11.45 Å2
Refinement stepCycle: final / Resolution: 3.6883→19.984 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24271 0 180 0 24451
Biso mean--122.84 --
Num. residues----3161
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00424968
X-RAY DIFFRACTIONf_angle_d0.88333818
X-RAY DIFFRACTIONf_chiral_restr0.0353843
X-RAY DIFFRACTIONf_plane_restr0.0044271
X-RAY DIFFRACTIONf_dihedral_angle_d13.3628873
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6721X-RAY DIFFRACTION12.401TORSIONAL
12B6721X-RAY DIFFRACTION12.401TORSIONAL
13C6721X-RAY DIFFRACTION12.401TORSIONAL
14D6721X-RAY DIFFRACTION12.401TORSIONAL
21A2068X-RAY DIFFRACTION12.401TORSIONAL
22B2068X-RAY DIFFRACTION12.401TORSIONAL
23C2068X-RAY DIFFRACTION12.401TORSIONAL
24D2068X-RAY DIFFRACTION12.401TORSIONAL
31A2482X-RAY DIFFRACTION12.401TORSIONAL
32B2482X-RAY DIFFRACTION12.401TORSIONAL
33C2482X-RAY DIFFRACTION12.401TORSIONAL
34D2482X-RAY DIFFRACTION12.401TORSIONAL
41A346X-RAY DIFFRACTION12.401TORSIONAL
42C346X-RAY DIFFRACTION12.401TORSIONAL
43B346X-RAY DIFFRACTION12.401TORSIONAL
44D346X-RAY DIFFRACTION12.401TORSIONAL
51A213X-RAY DIFFRACTION12.401TORSIONAL
52B213X-RAY DIFFRACTION12.401TORSIONAL
53C213X-RAY DIFFRACTION12.401TORSIONAL
54D213X-RAY DIFFRACTION12.401TORSIONAL
61A414X-RAY DIFFRACTION12.401TORSIONAL
62B414X-RAY DIFFRACTION12.401TORSIONAL
63C414X-RAY DIFFRACTION12.401TORSIONAL
64D414X-RAY DIFFRACTION12.401TORSIONAL
71E696X-RAY DIFFRACTION12.401TORSIONAL
72F696X-RAY DIFFRACTION12.401TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 25

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.6883-3.73850.37821370.34342449258693
3.7385-3.79150.37691400.31422628276898
3.7915-3.84770.37231380.30126302768100
3.8477-3.90740.33211370.31842641277898
3.9074-3.9710.33781550.30342579273498
3.971-4.03890.29991500.260626462796100
4.0389-4.11170.26261430.24042608275198
4.1117-4.19010.26861540.23092667282199
4.1901-4.27480.2361510.21242622277398
4.2748-4.36680.27961490.20062631278099
4.3668-4.46730.2581230.20472660278399
4.4673-4.57770.24071420.19832625276798
4.5777-4.69990.2261420.191526592801100
4.6999-4.83640.25781380.18412635277398
4.8364-4.99010.23091230.17682664278798
4.9901-5.16550.20851300.175826862816100
5.1655-5.36850.20631510.17872611276298
5.3685-5.60770.25951170.17822694281198
5.6077-5.89610.22991130.18912668278198
5.8961-6.25490.23271660.19352647281398
6.2549-6.72070.28411570.18962658281598
6.7207-7.36610.23471500.18352646279697
7.3661-8.36290.22811230.17252699282297
8.3629-10.29110.19581350.17332656279195
10.2911-19.98440.25951740.22432728290296
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)
12.80321.5349-0.55395.8149-2.29983.54820.00920.48650.5773-0.35920.42070.3037-0.2548-0.0807-0.36460.4992-0.03250.16990.70080.06620.6995-60.971233.4146-18.8714
23.0551.3258-0.19044.5188-0.40033.9549-0.03770.7456-0.0477-1.0943-0.0545-0.65380.22990.25880.10270.69770.1585-0.07350.6741-0.08760.7968-54.8024-25.1197-11.5109
30.5704-0.93170.73562.2734-0.75750.4047-0.38590.18-0.5951.5897-0.9719-1.2620.1404-0.22161.13993.08020.20020.08061.12010.00822.6685-34.7477-78.916420.8006
43.2543-0.87620.45922.50050.56462.28750.30940.4402-0.76320.06640.051-0.77070.79780.7303-0.32880.86980.2583-0.22140.7948-0.22351.1403-49.2135-34.720.969
5-0.0097-0.15910.2762-0.004-0.15750.0543-0.3636-0.20090.10250.13670.05780.4137-0.1373-0.30360.01922.53110.92060.31581.09930.20672.5553-42.7474-87.14085.5307
61.56740.5425-0.43612.9647-2.52644.76620.1448-0.00060.22970.16690.1448-0.2759-0.39770.4405-0.27490.7099-0.13630.18360.9392-0.29090.63-29.298437.8609-3.0321
72.4494-0.1952-1.08384.0236-1.23214.0263-0.18020.10790.5437-0.216-0.2124-0.5706-0.33440.74860.36070.7765-0.0583-0.41641.00130.17661.064-12.9216-20.647125.6121
82.22120.4088-0.99130.1057-0.55180.31980.671-0.8101-0.1997-0.4433-0.26461.69121.19130.8091-0.26233.0781-0.3482-0.02971.19060.42032.525-38.236-76.597838.4581
93.4671-0.6338-0.50315.4679-0.94981.347-0.14330.3828-0.3702-0.3528-0.44030.04670.11260.7090.46440.97780.053-0.3191.00290.11540.8158-12.8927-35.662632.7525
10-0.2323-0.0396-0.07420.03590.19520.5835-0.7845-0.46560.17170.53530.0371-0.2937-0.0908-0.20020.63981.5621-0.3743-0.18951.4238-0.16882.1999-23.2218-83.957631.3479
112.3562-1.1029-0.20953.871.0764.34270.1112-0.28010.1319-0.12610.2352-0.32930.14110.6003-0.30270.8307-0.08570.38821.1416-0.13230.8844-13.722635.328564.9823
121.83130.1585-1.25344.0198-0.29334.98510.1318-0.7690.39771.0332-0.04120.0852-0.50190.1591-0.08521.35040.0559-0.31971.1145-0.10260.9894-31.493-19.892254.5639
131.44921.79310.67764.08690.51481.1632-0.0025-0.56350.34-1.8399-0.71741.02630.414-0.19790.52892.4766-0.165-0.21751.2052-0.07632.3076-55.9733-76.859132.2466
144.61270.0033-0.2223.0817-0.81223.35540.1802-0.85-0.68460.5753-0.20260.46510.28920.04050.0780.9325-0.0645-0.18190.79750.15760.8912-37.9441-30.756444.0701
150.3365-0.13310.02150.02640.0092-0.0315-0.1572-1.3578-0.6979-0.3171-0.3249-0.19061.0122-0.57910.39532.7462-0.4548-0.02521.49180.3232.2297-48.5662-82.973450.3715
161.76670.1718-0.41042.91022.11054.91910.1781-0.05650.29190.12490.01970.318-0.3528-0.7203-0.21380.92940.01540.21271.03580.06520.6237-45.354141.156949.7094
172.6721-0.5285-0.03984.74260.09022.9429-0.1633-0.33310.07920.7082-0.00740.3765-0.21410.00680.13680.61990.0586-0.16990.4956-0.11110.723-73.9089-19.644316.6446
181.04570.5237-0.25910.1938-0.21970.4439-0.04260.3620.29120.5203-0.8931-0.04610.7276-0.97770.70523.19560.6453-0.17381.1747-0.07862.9642-52.6208-80.586315.0369
194.0541.14460.2374.0186-1.0832.53790.2605-0.393-0.74750.1036-0.11450.03060.5364-0.3961-0.13890.69260.0006-0.24780.5779-0.04030.8516-75.0178-35.729912.176
201.7648-0.4044-0.35420.13510.33752.4605-0.7604-0.1758-0.79690.08670.1161.22460.22920.27310.46591.67720.18890.12791.2871-0.04832.1566-65.8756-78.781524.8915
215.2848-1.63370.34736.4658-1.21745.21480.5084-0.05320.2687-0.0837-0.4079-0.50190.30640.5722-0.03890.5716-0.0057-0.29210.57140.00540.9002-50.4202-3.13557.4394
225.72840.34470.33965.7914-0.79994.77880.0496-0.24240.37250.9057-0.3368-0.2778-0.9150.39690.17390.9999-0.006-0.54020.7416-0.12361.329-35.4113-1.128631.5733
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:382)A1 - 382
2X-RAY DIFFRACTION2(chain A and resid 383:507)A383 - 507
3X-RAY DIFFRACTION3(chain A and resid 508:635)A508 - 635
4X-RAY DIFFRACTION4(chain A and resid 636:771)A636 - 771
5X-RAY DIFFRACTION5(chain A and resid 772:817)A772 - 817
6X-RAY DIFFRACTION6(chain B and resid 1:382)B1 - 382
7X-RAY DIFFRACTION7(chain B and resid 383:507)B383 - 507
8X-RAY DIFFRACTION8(chain B and resid 508:635)B508 - 635
9X-RAY DIFFRACTION9(chain B and resid 636:771)B636 - 771
10X-RAY DIFFRACTION10(chain B and resid 772:817)B772 - 817
11X-RAY DIFFRACTION11(chain C and resid 1:382)C1 - 382
12X-RAY DIFFRACTION12(chain C and resid 383:507)C383 - 507
13X-RAY DIFFRACTION13(chain C and resid 508:635)C508 - 635
14X-RAY DIFFRACTION14(chain C and resid 636:771)C636 - 771
15X-RAY DIFFRACTION15(chain C and resid 772:817)C772 - 817
16X-RAY DIFFRACTION16(chain D and resid 1:382)D1 - 382
17X-RAY DIFFRACTION17(chain D and resid 383:507)D383 - 507
18X-RAY DIFFRACTION18(chain D and resid 508:635)D508 - 635
19X-RAY DIFFRACTION19(chain D and resid 636:771)D636 - 771
20X-RAY DIFFRACTION20(chain D and resid 772:817)D772 - 817
21X-RAY DIFFRACTION21(chain E)E0
22X-RAY DIFFRACTION22(chain F)F0

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