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- PDB-6k9f: Structure of unknow protein 4 -

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Basic information

Entry
Database: PDB / ID: 6k9f
TitleStructure of unknow protein 4
ComponentsCaspase recruitment domain-containing protein 8
KeywordsSIGNALING PROTEIN / filament
Function / homology
Function and homology information


CARD8 inflammasome complex assembly / NACHT domain binding / Formation of apoptosome / cysteine-type endopeptidase activator activity / inhibition of cysteine-type endopeptidase activity / negative regulation of NLRP3 inflammasome complex assembly / NLRP3 inflammasome complex / CARD domain binding / negative regulation of lipopolysaccharide-mediated signaling pathway / self proteolysis ...CARD8 inflammasome complex assembly / NACHT domain binding / Formation of apoptosome / cysteine-type endopeptidase activator activity / inhibition of cysteine-type endopeptidase activity / negative regulation of NLRP3 inflammasome complex assembly / NLRP3 inflammasome complex / CARD domain binding / negative regulation of lipopolysaccharide-mediated signaling pathway / self proteolysis / Regulation of the apoptosome activity / Hydrolases; Acting on peptide bonds (peptidases) / regulation of canonical NF-kappaB signal transduction / negative regulation of interleukin-1 beta production / pattern recognition receptor activity / negative regulation of NF-kappaB transcription factor activity / cysteine-type endopeptidase activator activity involved in apoptotic process / antiviral innate immune response / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of canonical NF-kappaB signal transduction / positive regulation of interleukin-1 beta production / molecular condensate scaffold activity / peptidase activity / regulation of apoptotic process / defense response to virus / protein homodimerization activity / protein-containing complex / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
FIIND domain / Function to find / FIIND domain profile. / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Death-like domain superfamily
Similarity search - Domain/homology
Caspase recruitment domain-containing protein 8
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsGong, Q. / Xu, C. / Zhang, J. / Boo, Z.Z. / Wu, B.
Funding support Singapore, 2items
OrganizationGrant numberCountry
Ministry of Education (Singapore)tier2 Singapore
Ministry of Education (Singapore)tier1 Singapore
CitationJournal: Nat Commun / Year: 2021
Title: Structural basis for distinct inflammasome complex assembly by human NLRP1 and CARD8.
Authors: Qin Gong / Kim Robinson / Chenrui Xu / Phuong Thao Huynh / Kelvin Han Chung Chong / Eddie Yong Jun Tan / Jiawen Zhang / Zhao Zhi Boo / Daniel Eng Thiam Teo / Kenneth Lay / Yaming Zhang / ...Authors: Qin Gong / Kim Robinson / Chenrui Xu / Phuong Thao Huynh / Kelvin Han Chung Chong / Eddie Yong Jun Tan / Jiawen Zhang / Zhao Zhi Boo / Daniel Eng Thiam Teo / Kenneth Lay / Yaming Zhang / John Soon Yew Lim / Wah Ing Goh / Graham Wright / Franklin L Zhong / Bruno Reversade / Bin Wu /
Abstract: Nod-like receptor (NLR) proteins activate pyroptotic cell death and IL-1 driven inflammation by assembling and activating the inflammasome complex. Closely related sensor proteins NLRP1 and CARD8 ...Nod-like receptor (NLR) proteins activate pyroptotic cell death and IL-1 driven inflammation by assembling and activating the inflammasome complex. Closely related sensor proteins NLRP1 and CARD8 undergo unique auto-proteolysis-dependent activation and are implicated in auto-inflammatory diseases; however, their mechanisms of activation are not understood. Here we report the structural basis of how the activating domains (FIIND-CARD) of NLRP1 and CARD8 self-oligomerize to assemble distinct inflammasome complexes. Recombinant FIIND-CARD of NLRP1 forms a two-layered filament, with an inner core of oligomerized CARD surrounded by an outer ring of FIIND. Biochemically, self-assembled NLRP1-CARD filaments are sufficient to drive ASC speck formation in cultured human cells-a process that is greatly enhanced by NLRP1-FIIND which forms oligomers in vitro. The cryo-EM structures of NLRP1-CARD and CARD8-CARD filaments, solved here at 3.7 Å, uncover unique structural features that enable NLRP1 and CARD8 to discriminate between ASC and pro-caspase-1. In summary, our findings provide structural insight into the mechanisms of activation for human NLRP1 and CARD8 and reveal how highly specific signaling can be achieved by heterotypic CARD interactions within the inflammasome complexes.
History
DepositionJun 15, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 16, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2021Group: Database references / Structure summary / Category: audit_author / citation / citation_author
Item: _audit_author.name / _citation.country ..._audit_author.name / _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 1.2Mar 27, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

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  • Deposited structure unit
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Structure viewerMolecule:
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Assembly

Deposited unit
A: Caspase recruitment domain-containing protein 8
B: Caspase recruitment domain-containing protein 8
C: Caspase recruitment domain-containing protein 8
D: Caspase recruitment domain-containing protein 8
E: Caspase recruitment domain-containing protein 8
F: Caspase recruitment domain-containing protein 8
G: Caspase recruitment domain-containing protein 8
H: Caspase recruitment domain-containing protein 8
I: Caspase recruitment domain-containing protein 8
J: Caspase recruitment domain-containing protein 8
K: Caspase recruitment domain-containing protein 8
L: Caspase recruitment domain-containing protein 8


Theoretical massNumber of molelcules
Total (without water)125,34912
Polymers125,34912
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: assay for oligomerization
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Caspase recruitment domain-containing protein 8 / Apoptotic protein NDPP1 / CARD-inhibitor of NF-kappa-B-activating ligand / CARDINAL / DACAR / Tumor ...Apoptotic protein NDPP1 / CARD-inhibitor of NF-kappa-B-activating ligand / CARDINAL / DACAR / Tumor up-regulated CARD-containing antagonist of CASP9 / TUCAN


Mass: 10445.787 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CARD8, KIAA0955, NDPP1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9Y2G2

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: caspase recruitment domain containing=protein 8 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli K-12 (bacteria) / Strain: K-12
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DARK FIELD / Nominal magnification: 115000 X / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 80 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 1424
Image scansMovie frames/image: 40

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Processing

SoftwareName: PHENIX / Version: (dev_2405: ???) / Classification: refinement
EM software
IDNameVersionCategory
2EPU2.3image acquisition
4RELION2CTF correction
7Coot0.8.9.1 ELmodel fitting
9RELION2initial Euler assignment
10RELION2final Euler assignment
11RELION2classification
12RELION23D reconstruction
13PHENIXdev 2405model refinement
CTF correctionType: NONE
Helical symmertyAngular rotation/subunit: -99.16 ° / Axial rise/subunit: 5.409 Å / Axial symmetry: C1
Particle selectionNum. of particles selected: 1201108
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 98280 / Symmetry type: HELICAL
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
RefinementResolution: 3.7→92.4 Å / SU ML: 1.19 / σ(F): 0.04 / Phase error: 51.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3017 967 3.36 %
Rwork0.253 --
obs0.2547 28800 99.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0028544
ELECTRON MICROSCOPYf_angle_d0.42311448
ELECTRON MICROSCOPYf_dihedral_angle_d22.4775424
ELECTRON MICROSCOPYf_chiral_restr0.031296
ELECTRON MICROSCOPYf_plane_restr0.0031524
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.7001-3.89520.54811280.5483969ELECTRON MICROSCOPY100
3.8952-4.13930.47841520.51744011ELECTRON MICROSCOPY100
4.1393-4.45880.4581440.46623926ELECTRON MICROSCOPY100
4.4588-4.90750.41891320.37714008ELECTRON MICROSCOPY100
4.9075-5.61760.40321240.30623977ELECTRON MICROSCOPY100
5.6176-7.07720.40591460.30593990ELECTRON MICROSCOPY100
7.0772-92.42880.19321410.15293952ELECTRON MICROSCOPY100
Refinement TLS params.

Method: refined / Refine-ID: ELECTRON MICROSCOPY

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)
13.4386-4.0187-1.26647.095-1.53745.7363-1.1303-1.7546-0.7146-0.46350.37542.65121.5732-2.48640.51041.6053-0.2365-0.09262.2289-0.12182.1878120.545105.4263126.102
23.6930.2777-3.5533.24692.73618.4773-1.6803-4.8845-2.2294-0.22830.614-0.2903-0.92711.1171.10532.55150.69390.16072.28920.5532.2829137.6324107.6605129.0704
36.6718-6.7461-4.61429.7882.70054.4702-2.3934.3596.36250.88961.4957-5.6264-1.8154-1.8921.362.4245-0.3239-0.05142.7590.05123.3864133.5162118.2451125.1177
46.4122-7.94495.59937.5761-1.86677.684-0.7886-0.73911.03360.3633-0.4379-1.14543.412-0.22960.83692.4317-0.16560.50832.2619-0.062.0515128.5411105.6298125.4959
52.96313.62393.05293.33.28562.9287-2.16261.9619-3.3034-2.08382.46930.62311.5108-2.0924-0.50172.3596-0.360.0482.2669-0.10512.5343116.659799.0499133.8835
66.46156.1529-3.01038.25421.29076.1163-1.3481.29240.7860.52931.47112.0018-0.54112.45260.64542.38830.3221-0.1132.11440.12721.8566107.714115.9981147.7366
74.41111.32690.73884.05664.90255.2637-3.7171-0.5472-0.25841.3765.19065.21893.18725.87690.68823.60970.38670.51232.26690.22722.4315122.6619107.7602150.7697
83.4437-0.941-5.30174.2239-0.68418.8421-2.58944.4207-1.60972.7352-0.4017-6.7505-4.5774-0.00730.3352.18780.73120.2762.7039-0.24933.6075125.5478118.6737146.864
9-0.60031.8658-1.01267.76051.76485.9637-0.94-0.5810.4074-0.28941.0368-0.69110.71360.11420.71042.4557-0.07250.33912.7856-0.14982.2745114.137111.4254147.2473
101.96162.05431.7331.5521.92923.89641.26260.113-1.89330.13080.18691.3451-2.6788-0.2222-1.28182.6667-0.33730.34883.18990.11942.3285100.6397113.1403155.4652
113.72972.4014-10.5369.79452.87789.4812-0.1252-0.2748-0.26010.7626-1.25460.6069-0.24040.46710.84252.37120.28710.07071.79990.10531.7619107.9656121.3182111.0512
126.4816-0.9153-4.8789.96954.92152.0095-4.1761.3488-0.30912.1495-1.257-7.5087-7.71988.17890.66932.94260.6962-0.14012.09630.65363.107121.0412121.7826108.9486
136.48213.5455-7.2475.0745-0.88846.474-0.8613-0.2521-2.85391.7938-0.0559-2.00090.2917-0.58381.00432.44590.15460.12072.8454-0.07472.0196107.531120.2976109.2839
143.57454.57774.66226.51615.27065.6173-1.62782.5636-0.91110.85530.12892.5879-0.2109-0.19780.58792.7391-0.0158-0.1812.1223-0.10482.439396.3335127.7583117.6812
152.8647-7.1402-5.81966.0797-1.03989.3453-1.12981.1471-2.2397-2.3836-1.17491.80441.7984-1.98240.38862.2816-0.51850.08211.9808-0.28422.3676132.3963103.7918164.0336
165.2653-3.4598-4.45764.37042.6164.13943.6206-4.27221.9908-1.9976-2.6136-0.6350.29092.23230.64212.64450.5295-0.1924.1818-0.33152.1246146.574113.173166.81
175.2659-0.8958-6.93093.9295-0.44159.6621-0.5902-1.63834.233-1.3543-0.3258-0.9001-10.5227-1.6172-1.11732.26081.1204-0.19062.423-0.39163.1569138.16120.8906163.0627
182.57950.99440.93311.9384-0.06552.7615-2.3373-2.0170.1963-1.47621.1836-1.7036-0.02052.53680.33872.55520.38930.54952.111-0.16382.5335135.5761111.5707160.7296
194.43421.9735-2.52693.9242-6.27586.97140.1643-1.2878-0.5640.4217-1.9990.59740.1274-0.05731.62643.4205-0.17460.57722.1242-0.42792.2847137.769299.8298169.0009
205.2953-2.80713.53974.65063.06066.6304-1.4357-1.12131.81060.8716-0.72260.2307-0.41830.03851.46522.8386-0.0585-0.12352.47850.68382.0803119.733154.6379153.1781
212.28260.91981.23712.82772.30771.93461.11910.9512-2.0785-3.0976-1.6998-1.78233.4097-0.15461.26952.4023-0.15730.4673.21590.41712.0786109.1367141.1516156.0735
222.74121.09871.49711.86143.19638.67870.1089-1.5578-9.2341-0.5355-1.4275-0.65072.26091.40111.17022.3846-0.00160.56722.54110.57883.8067119.4781136.4814152.2723
234.63580.3082-1.37681.034.33132.66011.0692-0.2954-0.12820.6995-1.3357-0.5512-0.3754-0.16121.46512.58290.3027-0.31751.58990.13771.9364114.1291148.9243152.6999
245.3834-0.49165.04171.73-3.17248.52990.85690.46124.02373.5122-2.0121-1.8189-3.12421.34290.49393.14290.7172-0.02241.47870.12152.9935117.9515161.9322160.9161
256.9324-5.05931.49396.4409-5.04725.717-0.396-0.0038-3.07-5.43450.5081-0.1744-1.05350.2207-0.15542.3848-0.67330.57972.1214-0.01592.3133137.2876104.7299104.4437
264.77320.1753-2.2043.2575-3.61424.73632.5127-1.9022-3.13911.2879-3.6025-1.5655-4.81533.43581.06461.8425-0.59140.01482.6560.3732.1349149.4924116.556107.4515
278.68432.4298-1.37929.0455-8.69212.0784-2.0381-2.86046.72060.9353-1.95031.1985-6.4128-8.9166-0.36132.6547-0.02580.15822.6996-0.39982.544139.8707122.6401103.6018
288.60953.0273-1.30074.0897-5.12086.4347-0.072-2.06252.97210.4167-0.6222-3.0726-0.42130.71320.53732.76450.18770.10852.12820.10462.084143.5919109.5713103.9776
292.58372.8946-0.35149.15445.83045.9198-2.8781-3.2131-4.6249-3.7971.5405-2.0104-0.093-1.36931.72012.17480.42590.55362.16610.45182.9323137.975497.1486112.255
307.93677.14412.40636.86790.21233.30150.903-0.8848-4.34861.5722-2.1253-1.78162.54561.6883-0.16132.71020.62840.15282.3336-0.18072.4273156.1315124.7454120.6607
312.43252.774-2.14155.5731-4.82124.86421.7301-0.53871.24031.73780.6349-0.1976-3.7096-2.73970.1952.7616-0.38780.01542.19080.20582.3351151.1806141.1207123.5814
328.83562.13928.45371.92896.26762.04465.5283-0.55953.25040.81-7.17753.74840.8671-4.5291-0.84453.21020.79840.53151.49680.27113.2233141.443135.4586119.7267
335.95237.57963.94177.32154.61414.1905-0.131-0.8007-0.04041.2808-0.59240.06841.32461.61230.09992.79780.82860.07982.78830.31082.3517154.7011132.6199120.1312
34-0.1299-0.0688-0.26675.8774-0.66192.84363.29986.57012.05093.6669-2.4391-3.83980.52872.3856-0.77621.61640.42330.08783.3390.31132.1244163.1242121.8566128.5057
352.4881-3.67552.93217.79513.31673.4307-1.4763-1.61252.3377-1.35260.2865-1.77180.89481.73330.28771.8237-0.4382-0.06232.61410.30321.9739131.4918156.6851115.2268
366.6494-1.66595.53843.8219-0.29535.1129-0.3635-3.34750.80382.41892.37711.04282.5391-6.65171.20752.11580.66670.26413.1522-0.10011.9805116.0096149.1811118.1784
375.69512.04725.46425.05163.9577.2515-4.19080.3593-10.0034-0.5032.67761.33997.38625.96760.71243.13720.36160.49493.37930.70953.0982123.2474140.4982114.4393
383.1749-7.6213-0.15576.29864.8388.889-0.623-1.1817-2.69481.2622-0.37922.80531.0817-0.61560.9692.9079-0.71-0.09642.71250.0442.5116123.8545154.0257114.7746
392.5938-0.39862.33554.4467-5.64597.2193-0.15371.48453.3667-4.26930.86751.0228-0.4031-4.31880.5812.42530.1430.23732.51960.19652.1586133.162163.9651123.1617
407.34662.80790.09236.66086.39276.80.17360.21722.50961.7707-1.42142.6582-3.18222.1990.45992.1212-0.2142-0.17122.05850.10292.23107.1191143.5033131.4081
412.89512.02554.02243.47950.66847.71955.80811.04954.42012.6471-3.352.73135.32751.43470.4772.6378-0.53670.81892.899-0.11852.3228106.7796126.353134.4802
425.29931.82635.18082.17041.27414.88741.5751.3204-5.3117-0.8462-0.4041-2.5698-0.0426-1.80280.1683.20970.7550.29462.6918-0.09583.3971117.8022128.8524130.5452
436.93647.0871-1.73325.8293-0.0655.4951.2538-1.5296-1.57320.9397-1.463-0.4642-0.4271-2.27040.4942.78180.44960.0792.82360.01962.2413106.098135.6472130.9472
441.2137-1.49780.82432.7046-3.35394.48790.52454.0218-0.3663-1.2504-2.2487-0.5142-2.1303-2.28691.52392.95340.60880.12772.93270.06542.1888101.4207148.3726139.381
458.84022.0512-0.00466.0393-0.99694.4346-3.23173.01980.8384-2.09793.135-2.38633.849-0.3303-0.01462.58320.21630.07693.07310.20962.6283146.9108150.7745136.8871
468.3026-1.96172.93222.2282-1.47571.9517-0.3074-3.88092.1644-1.35721.9657-0.9244-1.6578-4.7910.29022.89970.7757-0.16253.370.06781.9729130.1584153.828139.9109
479.5475-6.93425.64185.5907-6.08568.6214-0.02512.2667-2.24772.4520.59745.27443.9430.20120.29213.197-0.22930.27462.26790.20713.227130.8082142.5753135.938
482.6356-3.3181-0.60544.52443.57578.5495-0.9352-0.6992-0.13151.23151.50980.5889-0.92470.13180.1882.8563-0.4184-0.0233.550.07492.2051139.3918153.0701136.3776
496.352.7247-5.8422.7681-0.69146.3508-5.49450.15152.7881-3.57841.993-1.6274.82613.24942.39363.2124-0.1316-0.20572.59010.45382.5441152.5531155.6375144.8488
506.8138-5.8233-2.57936.38442.62174.4065-0.57-0.636-1.59131.9909-0.63990.11522.1914-0.53090.99023.0525-0.28610.47141.6091-0.02792.0423147.704110.4166142.3658
512.74752.4435-2.18997.8690.32652.31521.46642.7201-1.78313.6168-0.9626-2.2249-5.01581.83230.75152.2036-0.3297-0.22012.82540.19622.077153.5174126.5268145.2309
526.75363.2397-1.39951.6411-1.06456.44543.4811-3.70877.39340.7759-4.48651.31-0.5911-4.21911.35212.0925-0.00880.2132.1117-0.59554.2249142.2639127.6702141.3673
537.24944.30450.37681.17010.4647.76680.0625-0.55230.9921.3555-0.38920.58170.39030.35890.95142.36310.03240.34952.32210.23832.4166151.2062117.5108141.8235
545.3879-5.5109-0.07456.10542.19124.62683.2657-0.4602-2.0992-3.0109-2.9036-3.24940.0036-1.53531.35422.57220.67970.1823.19450.51382.3954151.6587104.0101150.288
556.998.37092.58442.9907-1.67727.1368-0.6067-0.0748-1.461-0.6151-1.077-2.4775-0.5964-0.63790.55742.33720.73710.43671.79290.04472.2679155.9214136.629158.6252
564.23192.59711.98124.43421.58442.0919-0.53763.88760.14335.50731.07250.5224-3.4798-1.56461.4763.01650.53530.64642.6857-0.03162.3513144.2735149.1664161.4256
572.77960.96740.90076.1313-4.53053.22952.84233.00670.71184.0691-4.66965.7852.7752-5.31080.64392.665-0.68970.78662.28040.02183.3674138.0607139.6334157.7827
587.97772.72374.06335.3887-0.71254.034-1.12780.89381.14961.14160.36361.8248-1.60081.8671.08122.08380.02590.19622.89430.61572.0444151.1977143.0237158.1223
591.73742.7117-3.59095.1831-5.66816.7155-3.2489-0.16193.8777-5.44153.2347-3.63120.73241.58850.30472.803-0.57340.04122.86760.20122.0724163.4355137.3576166.4111
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1ELECTRON MICROSCOPY1chain 'A' and (resid 451 through 468 )
2ELECTRON MICROSCOPY2chain 'A' and (resid 469 through 482 )
3ELECTRON MICROSCOPY3chain 'A' and (resid 483 through 494 )
4ELECTRON MICROSCOPY4chain 'A' and (resid 495 through 524 )
5ELECTRON MICROSCOPY5chain 'A' and (resid 525 through 537 )
6ELECTRON MICROSCOPY6chain 'B' and (resid 451 through 468 )
7ELECTRON MICROSCOPY7chain 'B' and (resid 469 through 482 )
8ELECTRON MICROSCOPY8chain 'B' and (resid 483 through 494 )
9ELECTRON MICROSCOPY9chain 'B' and (resid 495 through 524 )
10ELECTRON MICROSCOPY10chain 'B' and (resid 525 through 537 )
11ELECTRON MICROSCOPY11chain 'C' and (resid 451 through 482 )
12ELECTRON MICROSCOPY12chain 'C' and (resid 483 through 494 )
13ELECTRON MICROSCOPY13chain 'C' and (resid 495 through 524 )
14ELECTRON MICROSCOPY14chain 'C' and (resid 525 through 537 )
15ELECTRON MICROSCOPY15chain 'D' and (resid 451 through 468 )
16ELECTRON MICROSCOPY16chain 'D' and (resid 469 through 482 )
17ELECTRON MICROSCOPY17chain 'D' and (resid 483 through 494 )
18ELECTRON MICROSCOPY18chain 'D' and (resid 495 through 509 )
19ELECTRON MICROSCOPY19chain 'D' and (resid 510 through 537 )
20ELECTRON MICROSCOPY20chain 'E' and (resid 451 through 468 )
21ELECTRON MICROSCOPY21chain 'E' and (resid 469 through 482 )
22ELECTRON MICROSCOPY22chain 'E' and (resid 483 through 494 )
23ELECTRON MICROSCOPY23chain 'E' and (resid 495 through 524 )
24ELECTRON MICROSCOPY24chain 'E' and (resid 525 through 537 )
25ELECTRON MICROSCOPY25chain 'F' and (resid 451 through 468 )
26ELECTRON MICROSCOPY26chain 'F' and (resid 469 through 482 )
27ELECTRON MICROSCOPY27chain 'F' and (resid 483 through 494 )
28ELECTRON MICROSCOPY28chain 'F' and (resid 495 through 524 )
29ELECTRON MICROSCOPY29chain 'F' and (resid 525 through 537 )
30ELECTRON MICROSCOPY30chain 'G' and (resid 451 through 468 )
31ELECTRON MICROSCOPY31chain 'G' and (resid 469 through 482 )
32ELECTRON MICROSCOPY32chain 'G' and (resid 483 through 494 )
33ELECTRON MICROSCOPY33chain 'G' and (resid 495 through 524 )
34ELECTRON MICROSCOPY34chain 'G' and (resid 525 through 537 )
35ELECTRON MICROSCOPY35chain 'H' and (resid 451 through 468 )
36ELECTRON MICROSCOPY36chain 'H' and (resid 469 through 482 )
37ELECTRON MICROSCOPY37chain 'H' and (resid 483 through 494 )
38ELECTRON MICROSCOPY38chain 'H' and (resid 495 through 524 )
39ELECTRON MICROSCOPY39chain 'H' and (resid 525 through 537 )
40ELECTRON MICROSCOPY40chain 'I' and (resid 451 through 468 )
41ELECTRON MICROSCOPY41chain 'I' and (resid 469 through 482 )
42ELECTRON MICROSCOPY42chain 'I' and (resid 483 through 494 )
43ELECTRON MICROSCOPY43chain 'I' and (resid 495 through 524 )
44ELECTRON MICROSCOPY44chain 'I' and (resid 525 through 537 )
45ELECTRON MICROSCOPY45chain 'J' and (resid 451 through 468 )
46ELECTRON MICROSCOPY46chain 'J' and (resid 469 through 482 )
47ELECTRON MICROSCOPY47chain 'J' and (resid 483 through 494 )
48ELECTRON MICROSCOPY48chain 'J' and (resid 495 through 524 )
49ELECTRON MICROSCOPY49chain 'J' and (resid 525 through 537 )
50ELECTRON MICROSCOPY50chain 'K' and (resid 451 through 468 )
51ELECTRON MICROSCOPY51chain 'K' and (resid 469 through 482 )
52ELECTRON MICROSCOPY52chain 'K' and (resid 483 through 494 )
53ELECTRON MICROSCOPY53chain 'K' and (resid 495 through 524 )
54ELECTRON MICROSCOPY54chain 'K' and (resid 525 through 537 )
55ELECTRON MICROSCOPY55chain 'L' and (resid 451 through 468 )
56ELECTRON MICROSCOPY56chain 'L' and (resid 469 through 482 )
57ELECTRON MICROSCOPY57chain 'L' and (resid 483 through 494 )
58ELECTRON MICROSCOPY58chain 'L' and (resid 495 through 524 )
59ELECTRON MICROSCOPY59chain 'L' and (resid 525 through 537 )

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