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- PDB-6zyu: Structure of the GluA2 ligand-binding domain (L483Y-N754S) in com... -

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Basic information

Entry
Database: PDB / ID: 6zyu
TitleStructure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM549
ComponentsGlutamate receptor 2,Glutamate receptor 2
KeywordsSIGNALING PROTEIN / GLUA2-LBD / GLUA2-S1S2J / AMPA RECEPTOR / LIGAND-BINDING DOMAIN / POSITIVE ALLOSTERIC MODULATOR / MEMBRANE PROTEIN / L483Y / N754S
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 / extracellularly glutamate-gated ion channel activity ...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 / extracellularly glutamate-gated ion channel activity / immunoglobulin binding / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / cellular response to glycine / asymmetric synapse / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / positive regulation of synaptic transmission / extracellular ligand-gated monoatomic ion channel activity / glutamate-gated receptor activity / response to fungicide / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / regulation of synaptic transmission, glutamatergic / ionotropic glutamate receptor binding / somatodendritic compartment / dendrite membrane / cellular response to brain-derived neurotrophic factor stimulus / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / cytoskeletal protein binding / dendrite cytoplasm / ionotropic glutamate receptor signaling pathway / SNARE binding / dendritic shaft / synaptic transmission, glutamatergic / synaptic membrane / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / PDZ domain binding / protein tetramerization / postsynaptic density membrane / establishment of protein localization / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / terminal bouton / receptor internalization / cerebral cortex development / synaptic vesicle membrane / synaptic vesicle / presynapse / signaling receptor activity / presynaptic membrane / amyloid-beta binding / growth cone / scaffold protein binding / chemical synaptic transmission / perikaryon / postsynaptic membrane / dendritic spine / postsynaptic density / neuron projection / axon / neuronal cell body / glutamatergic synapse / dendrite / synapse / protein-containing complex binding / protein kinase binding / 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 / Periplasmic binding protein-like I
Similarity search - Domain/homology
ACETATE ION / CACODYLATE ION / GLUTAMIC ACID / Chem-QSW / Chem-QSZ / Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å
AuthorsDorosz, J. / Christensen, K.M. / Kastrup, J.S.
Funding support Denmark, 2items
OrganizationGrant numberCountry
Danish Council for Independent Research Denmark
Danish Agency for Science Technology and Innovation Denmark
CitationJournal: Acs Chem Neurosci / Year: 2021
Title: Development of Thiochroman Dioxide Analogues of Benzothiadiazine Dioxides as New Positive Allosteric Modulators of alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors.
Authors: Etse, K.S. / Dorosz, J. / McLain Christensen, K. / Thomas, J.Y. / Botez Pop, I. / Goffin, E. / Colson, T. / Lestage, P. / Danober, L. / Pirotte, B. / Kastrup, J.S. / Francotte, P.
History
DepositionAug 3, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 11, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 23, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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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
C: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,47437
Polymers87,9053
Non-polymers3,56834
Water9,584532
1
A: Glutamate receptor 2,Glutamate receptor 2
hetero molecules

A: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,39630
Polymers58,6032
Non-polymers2,79328
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_455-x-1,-y,z1
Buried area5440 Å2
ΔGint-198 kcal/mol
Surface area24220 Å2
MethodPISA
2
B: Glutamate receptor 2,Glutamate receptor 2
C: Glutamate receptor 2,Glutamate receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,77622
Polymers58,6032
Non-polymers2,17220
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4360 Å2
ΔGint-155 kcal/mol
Surface area23810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)114.324, 163.084, 47.449
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 23 or resid 25...
21(chain B and (resid 1 through 23 or resid 25...
31(chain C and (resid 1 through 23 or resid 25...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 1 through 23 or resid 25...A1 - 23
121(chain A and (resid 1 through 23 or resid 25...A25 - 99
131(chain A and (resid 1 through 23 or resid 25...A1 - 263
141(chain A and (resid 1 through 23 or resid 25...A1 - 263
151(chain A and (resid 1 through 23 or resid 25...A109 - 138
161(chain A and (resid 1 through 23 or resid 25...A146 - 1639
171(chain A and (resid 1 through 23 or resid 25...A199 - 202
181(chain A and (resid 1 through 23 or resid 25...A204 - 221
191(chain A and (resid 1 through 23 or resid 25...A247 - 248
1101(chain A and (resid 1 through 23 or resid 25...A250 - 262
211(chain B and (resid 1 through 23 or resid 25...B1 - 23
221(chain B and (resid 1 through 23 or resid 25...B25 - 99
231(chain B and (resid 1 through 23 or resid 25...B101 - 107
241(chain B and (resid 1 through 23 or resid 25...B109 - 138
251(chain B and (resid 1 through 23 or resid 25...B146 - 163
261(chain B and (resid 1 through 23 or resid 25...B165 - 19
271(chain B and (resid 1 through 23 or resid 25...B197
281(chain B and (resid 1 through 23 or resid 25...B199 - 202
291(chain B and (resid 1 through 23 or resid 25...B204 - 221
2101(chain B and (resid 1 through 23 or resid 25...B223 - 245
2111(chain B and (resid 1 through 23 or resid 25...B247 - 248
2121(chain B and (resid 1 through 23 or resid 25...B250 - 262
311(chain C and (resid 1 through 23 or resid 25...C1 - 23
321(chain C and (resid 1 through 23 or resid 25...C25 - 99
331(chain C and (resid 1 through 23 or resid 25...C1 - 262
341(chain C and (resid 1 through 23 or resid 25...C1 - 262
351(chain C and (resid 1 through 23 or resid 25...C1 - 262
361(chain C and (resid 1 through 23 or resid 25...C146 - 163
371(chain C and (resid 1 through 23 or resid 25...C0
381(chain C and (resid 1 through 23 or resid 25...C1 - 262
391(chain C and (resid 1 through 23 or resid 25...C204 - 221
3101(chain C and (resid 1 through 23 or resid 25...C223 - 245
3111(chain C and (resid 1 through 23 or resid 25...C247 - 248
3121(chain C and (resid 1 through 23 or resid 25...C250 - 262

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Components

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Protein , 1 types, 3 molecules ABC

#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: 29301.729 Da / Num. of mol.: 3 / Mutation: L483Y,N754S
Source method: isolated from a genetically manipulated source
Details: LIGAND-BINDING DOMAIN, UNP RESIDUES 413-527 AND 653-797 CONNECTED BY A GT LINKER (NUMBERING WITH SIGNAL PEPTIDE),LIGAND-BINDING DOMAIN, UNP RESIDUES 413-527 AND 653-797 CONNECTED BY A GT ...Details: LIGAND-BINDING DOMAIN, UNP RESIDUES 413-527 AND 653-797 CONNECTED BY A GT LINKER (NUMBERING WITH SIGNAL PEPTIDE),LIGAND-BINDING DOMAIN, UNP RESIDUES 413-527 AND 653-797 CONNECTED BY A GT LINKER (NUMBERING WITH SIGNAL PEPTIDE)
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 , 9 types, 566 molecules

#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-CAC / CACODYLATE ION / dimethylarsinate


Mass: 136.989 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6AsO2
#4: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H3O2
#5: 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
#6: Chemical ChemComp-QSZ / (4~{S})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide / BPAM549


Mass: 240.294 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C12H13FO2S / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical ChemComp-QSW / (4~{R})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide / BPAM549


Mass: 240.294 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C12H13FO2S / Feature type: SUBJECT OF INVESTIGATION
#8: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#9: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 532 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
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: 2.52 Å3/Da / Density % sol: 51.31 %
Crystal growTemperature: 299 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: Zinc acetate, polyethylene glycol 4000, cacodylate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Mar 6, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 1.9→49.094 Å / Num. obs: 71004 / % possible obs: 100 % / Redundancy: 6.7 % / Rpim(I) all: 0.037 / Rrim(I) all: 0.095 / Rsym value: 0.087 / Net I/av σ(I): 6.4 / Net I/σ(I): 12.4
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) allRsym valueNet I/σ(I) obs% possible all
1.9-26.90.6031.269915101930.2480.6530.6033.3100
2-2.126.70.35326491696920.1470.3830.3535.2100
2.12-2.276.30.2313.15788791200.0990.2520.2317100
2.27-2.456.90.1754.15863584940.0720.190.1759100
2.45-2.696.80.1265.65345378740.0520.1370.12611.3100
2.69-36.50.0927.54613571420.0390.10.09214.6100
3-3.476.90.0689.44407463420.0280.0740.06821.3100
3.47-4.256.40.05710.73485154210.0240.0620.05726.5100
4.25-6.016.70.04912.22851742410.020.0530.04928.1100
6.01-49.0946.10.04511.71508324850.0190.0490.04526.899.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation1.9 Å49.09 Å
Translation1.9 Å49.09 Å

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Processing

Software
NameVersionClassification
XDSdata reduction
SCALA3.3.22data scaling
PHASER2.5.7phasing
PHENIX1.14refinement
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3TKD

3tkd


Resolution: 1.9→49.094 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 0.32 / Phase error: 18.04 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1868 3505 4.94 %
Rwork0.1624 67414 -
obs0.1637 70919 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 109.38 Å2 / Biso mean: 32.3958 Å2 / Biso min: 12.95 Å2
Refinement stepCycle: final / Resolution: 1.9→49.094 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6129 0 213 534 6876
Biso mean--40.91 35.76 -
Num. residues----787
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3503X-RAY DIFFRACTION9.945TORSIONAL
12B3503X-RAY DIFFRACTION9.945TORSIONAL
13C3503X-RAY DIFFRACTION9.945TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
1.9-1.9260.23891400.21212612
1.926-1.95350.25281390.20632665
1.9535-1.98270.23211380.19922672
1.9827-2.01370.20771490.18042602
2.0137-2.04670.21081370.17562700
2.0467-2.0820.23661370.17472649
2.082-2.11990.18721530.17812658
2.1199-2.16060.20811270.1662698
2.1606-2.20470.1971330.15782660
2.2047-2.25270.19651240.15812715
2.2527-2.30510.18341280.15762639
2.3051-2.36270.19061370.15652684
2.3627-2.42660.21591410.16332675
2.4266-2.4980.19091260.1592731
2.498-2.57860.20691570.16352623
2.5786-2.67080.18981350.15562704
2.6708-2.77770.17841450.15672694
2.7777-2.90410.18481270.16032686
2.9041-3.05720.18531430.16522709
3.0572-3.24870.17641460.1582712
3.2487-3.49950.18881380.15982717
3.4995-3.85150.17111580.15232721
3.8515-4.40850.13981610.13242750
4.4085-5.55310.15061440.14472785
5.5531-49.0940.23971420.20552953
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)
12.99970.2592-0.33423.39310.6132.060.14610.09620.25550.0191-0.10720.1517-0.2345-0.2131-0.02730.21030.03750.03440.1723-0.00650.2323-68.326870.858-1.6351
21.3095-0.2760.34730.5932-0.18422.9278-0.02260.016-0.09730.00410.02270.10290.1561-0.22060.02250.1971-0.00350.03270.1517-0.03080.2149-66.204155.2914-2.292
34.12880.6593-0.30055.17821.60533.7556-0.0423-0.2473-0.48910.0177-0.11690.37680.2416-0.35370.13920.1940.0051-0.00750.25050.01410.2838-71.530349.953415.5438
43.50030.3658-1.963.09820.82756.65840.0365-0.13940.23350.09360.0584-0.3669-0.42290.0941-0.06950.18080.027-0.01590.1077-0.01720.2843-56.742266.08353.3811
52.0063-0.5528-0.00192.33070.16182.4337-0.01710.06290.1479-0.06240.0485-0.1161-0.16910.2636-0.02520.101-0.0390.00330.1624-0.00670.1105-39.191410.2091-12.9426
60.66570.0624-0.30650.7247-0.3743.4641-0.01430.0276-0.0062-0.05570.01730.0624-0.1057-0.0070.00550.1059-0.0084-0.01480.12630.00090.1143-51.89889.6261-10.1446
74.5322-0.58362.42123.49350.37426.1887-0.08620.05870.1583-0.1055-0.06590.3079-0.2845-0.16750.08710.1431-0.009-0.00790.06490.01540.2033-58.931620.5364.397
80.5923-0.0414-0.10021.81210.53830.7061-0.0144-0.02340.02170.1136-0.00090.0214-0.03450.0744-0.00650.1256-0.0121-0.00620.15330.02080.1106-49.040210.98181.1164
93.17260.94540.23.74940.27343.320.0650.035-0.21850.0253-0.0182-0.46690.22980.4144-0.030.17690.02110.02050.161-0.00150.2011-37.85837.1641-0.8082
104.44831.58720.61433.9739-0.08512.9555-0.020.2102-0.1349-0.21830.1356-0.7077-0.1440.46-0.01420.17740.00260.06320.222300.2136-34.615546.9023-5.4939
113.46131.0982-0.01451.72650.1053.0042-0.09370.07230.6748-0.2167-0.097-0.1089-0.76271.02730.03310.3993-0.1640.05220.33910.03330.3761-31.792957.7072-8.723
121.02350.58350.07711.25240.44113.3923-0.11650.01440.1119-0.0534-0.0007-0.0041-0.18370.17920.11120.2074-0.01880.01530.1639-0.00010.2047-41.717354.393-0.1622
134.33640.33691.60026.4086-1.86886.8337-0.2045-0.03650.49730.2127-0.0925-0.0379-0.44230.24980.22790.2213-0.0936-0.0130.19460.01990.2849-34.898865.539414.9714
146.88434.48280.54912.995-0.20452.498-0.00520.02510.39580.0157-0.0242-0.3147-0.20680.3104-0.00290.312-0.1059-0.02490.27440.06140.25-29.278867.320611.4401
155.2992-0.64753.54215.5808-1.37325.8644-0.1101-0.05290.0123-0.0469-0.0282-0.44070.06470.3620.10490.2424-0.04780.05540.25370.00450.1814-32.622853.39717.3133
165.821-3.64424.79535.1988-3.64635.6202-0.0517-0.6655-0.27690.29580.15330.1609-0.1187-0.1721-0.14810.3281-0.05270.06810.36010.01230.2609-39.257153.092519.7202
174.26620.73341.37243.1365-0.35796.1043-0.25280.2920.1822-0.30940.12990.35030.03010.1410.0940.1859-0.01780.00770.1053-0.00620.1974-50.163248.1797-5.3718
185.12971.39613.98733.27390.21387.80820.2694-0.6946-0.13870.2802-0.2107-0.09030.2408-0.3773-0.21880.279-0.02940.03310.21780.03390.2293-46.563440.410913.0035
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'C' and (resid 1 through 65 )C1 - 65
2X-RAY DIFFRACTION2chain 'C' and (resid 66 through 116 )C66 - 116
3X-RAY DIFFRACTION3chain 'C' and (resid 117 through 217 )C117 - 217
4X-RAY DIFFRACTION4chain 'C' and (resid 218 through 262 )C218 - 262
5X-RAY DIFFRACTION5chain 'A' and (resid 1 through 79 )A1 - 79
6X-RAY DIFFRACTION6chain 'A' and (resid 80 through 116 )A80 - 116
7X-RAY DIFFRACTION7chain 'A' and (resid 117 through 152 )A117 - 152
8X-RAY DIFFRACTION8chain 'A' and (resid 153 through 263 )A153 - 263
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 47 )B1 - 47
10X-RAY DIFFRACTION10chain 'B' and (resid 48 through 65 )B48 - 65
11X-RAY DIFFRACTION11chain 'B' and (resid 66 through 79 )B66 - 79
12X-RAY DIFFRACTION12chain 'B' and (resid 80 through 116 )B80 - 116
13X-RAY DIFFRACTION13chain 'B' and (resid 117 through 152 )B117 - 152
14X-RAY DIFFRACTION14chain 'B' and (resid 153 through 173 )B153 - 173
15X-RAY DIFFRACTION15chain 'B' and (resid 174 through 202 )B174 - 202
16X-RAY DIFFRACTION16chain 'B' and (resid 203 through 217 )B203 - 217
17X-RAY DIFFRACTION17chain 'B' and (resid 218 through 243 )B218 - 243
18X-RAY DIFFRACTION18chain 'B' and (resid 244 through 262 )B244 - 262

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