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- PDB-6k99: Structure of ASC CARD filament -

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Basic information

Entry
Database: PDB / ID: 6k99
TitleStructure of ASC CARD filament
ComponentsApoptosis-associated speck-like protein containing a CARD
KeywordsSIGNALING PROTEIN / filament
Function / homology
Function and homology information


Pyrin domain binding / NLRP6 inflammasome complex / myosin I binding / positive regulation of antigen processing and presentation of peptide antigen via MHC class II / myeloid dendritic cell activation involved in immune response / negative regulation of protein serine/threonine kinase activity / regulation of intrinsic apoptotic signaling pathway / myeloid dendritic cell activation / IkappaB kinase complex / The AIM2 inflammasome ...Pyrin domain binding / NLRP6 inflammasome complex / myosin I binding / positive regulation of antigen processing and presentation of peptide antigen via MHC class II / myeloid dendritic cell activation involved in immune response / negative regulation of protein serine/threonine kinase activity / regulation of intrinsic apoptotic signaling pathway / myeloid dendritic cell activation / IkappaB kinase complex / The AIM2 inflammasome / AIM2 inflammasome complex / macropinocytosis / icosanoid biosynthetic process / NLRP1 inflammasome complex / canonical inflammasome complex / interleukin-6 receptor binding / positive regulation of adaptive immune response / NLRP3 inflammasome complex assembly / BMP receptor binding / NLRP3 inflammasome complex / cysteine-type endopeptidase activator activity / CLEC7A/inflammasome pathway / negative regulation of interferon-beta production / osmosensory signaling pathway / regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of extrinsic apoptotic signaling pathway / pattern recognition receptor signaling pathway / positive regulation of macrophage cytokine production / negative regulation of NF-kappaB transcription factor activity / pattern recognition receptor activity / tropomyosin binding / pyroptotic inflammatory response / positive regulation of actin filament polymerization / positive regulation of release of cytochrome c from mitochondria / positive regulation of activated T cell proliferation / intrinsic apoptotic signaling pathway by p53 class mediator / positive regulation of interleukin-10 production / The NLRP3 inflammasome / cellular response to interleukin-1 / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of T cell migration / Purinergic signaling in leishmaniasis infection / positive regulation of chemokine production / positive regulation of DNA-binding transcription factor activity / tumor necrosis factor-mediated signaling pathway / positive regulation of phagocytosis / positive regulation of defense response to virus by host / negative regulation of canonical NF-kappaB signal transduction / negative regulation of cytokine production involved in inflammatory response / activation of innate immune response / intrinsic apoptotic signaling pathway / positive regulation of interleukin-1 beta production / positive regulation of interleukin-8 production / positive regulation of JNK cascade / apoptotic signaling pathway / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of NF-kappaB transcription factor activity / protein homooligomerization / regulation of protein stability / positive regulation of T cell activation / positive regulation of interleukin-6 production / positive regulation of type II interferon production / positive regulation of inflammatory response / positive regulation of tumor necrosis factor production / SARS-CoV-1 activates/modulates innate immune responses / azurophil granule lumen / cellular response to tumor necrosis factor / cellular response to lipopolysaccharide / regulation of inflammatory response / protease binding / secretory granule lumen / defense response to Gram-negative bacterium / defense response to virus / microtubule / transmembrane transporter binding / positive regulation of canonical NF-kappaB signal transduction / positive regulation of ERK1 and ERK2 cascade / protein dimerization activity / regulation of autophagy / defense response to Gram-positive bacterium / positive regulation of apoptotic process / inflammatory response / Golgi membrane / innate immune response / neuronal cell body / apoptotic process / Neutrophil degranulation / nucleolus / enzyme binding / endoplasmic reticulum / signal transduction / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular region / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
CARD8/ASC/NALP1, CARD domain / : / DAPIN domain / DAPIN domain profile. / PAAD/DAPIN/Pyrin domain / PAAD/DAPIN/Pyrin domain / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Death-like domain superfamily
Similarity search - Domain/homology
Apoptosis-associated speck-like protein containing a CARD
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsGong, Q. / Xu, C. / Zhang, J. / Boo, Z.Z. / Wu, B.
Funding support Singapore, 1items
OrganizationGrant numberCountry
Ministry of Education (Singapore)tier2 and 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 14, 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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Assembly

Deposited unit
G: Apoptosis-associated speck-like protein containing a CARD
A: Apoptosis-associated speck-like protein containing a CARD
B: Apoptosis-associated speck-like protein containing a CARD
C: Apoptosis-associated speck-like protein containing a CARD
D: Apoptosis-associated speck-like protein containing a CARD
E: Apoptosis-associated speck-like protein containing a CARD
F: Apoptosis-associated speck-like protein containing a CARD
H: Apoptosis-associated speck-like protein containing a CARD
I: Apoptosis-associated speck-like protein containing a CARD
J: Apoptosis-associated speck-like protein containing a CARD
K: Apoptosis-associated speck-like protein containing a CARD
L: Apoptosis-associated speck-like protein containing a CARD


Theoretical massNumber of molelcules
Total (without water)117,30212
Polymers117,30212
Non-polymers00
Water00
1


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

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Components

#1: Protein
Apoptosis-associated speck-like protein containing a CARD / hASC / Caspase recruitment domain-containing protein 5 / PYD and CARD domain-containing protein / ...hASC / Caspase recruitment domain-containing protein 5 / PYD and CARD domain-containing protein / Target of methylation-induced silencing 1


Mass: 9775.143 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PYCARD, ASC, CARD5, TMS1 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: Q9ULZ3

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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: ASC CARD filament / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: Bl21(DE3)
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 R2/2
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 / Calibrated defocus min: 1500 nm / Calibrated defocus max: 2500 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 3183

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Processing

SoftwareName: PHENIX / Version: (dev_2405: ???) / Classification: refinement
EM software
IDNameVersionCategory
1RELION2particle selection
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: -100.614 ° / Axial rise/subunit: 5.27 Å / Axial symmetry: C1
Particle selectionNum. of particles selected: 877408
3D reconstructionResolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 59566 / Symmetry type: HELICAL
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
RefinementResolution: 4.1→62.582 Å / SU ML: 0.7 / σ(F): 0.09 / Phase error: 35.06 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2255 762 3.7 %
Rwork0.1871 --
obs0.1886 20584 99.55 %
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_d0.0038436
ELECTRON MICROSCOPYf_angle_d0.69311448
ELECTRON MICROSCOPYf_dihedral_angle_d15.8335076
ELECTRON MICROSCOPYf_chiral_restr0.0431260
ELECTRON MICROSCOPYf_plane_restr0.0041452
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.1-4.41650.45461670.40633891ELECTRON MICROSCOPY100
4.4165-4.86080.3781150.3144026ELECTRON MICROSCOPY99
4.8608-5.56380.33421960.25173952ELECTRON MICROSCOPY100
5.5638-7.00830.3151320.24893965ELECTRON MICROSCOPY100
7.0083-62.5890.12271520.09953988ELECTRON 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)
15.20742.66145.64153.43051.95536.3224-3.5806-1.4117-0.168-1.00370.73760.70220.1648-3.411-0.10954.8119-0.85050.46372.5658-0.06511.3898139.9298158.2209-119.5417
24.83095.035-3.05315.9159-3.23172.4152.18233.4444.5297-0.9404-1.79543.174-1.2682.6829-0.43492.33930.17370.0472.38250.0551.1772132.9456151.7167-126.212
35.66842.28315.26872.0034-1.4686.2886.44452.3004-1.5078-2.5792-3.8573-1.26167.8969-2.0664-1.99622.49450.3756-0.29353.0334-0.00591.4256143.8744144.2576-131.7535
45.71972.9321-4.04622.01914.48296.18220.2655-2.41234.69413.5553-1.2258-2.49965.58532.5579-1.48711.9982-1.3601-0.59510.99310.39081.6695150.831141.4915-124.8927
51.79741.26330.84964.63332.07733.30163.43022.05982.752.0464-3.7651-1.39063.5778-1.39130.53231.698-0.6797-0.33622.1747-0.35522.3577140.4141135.3606-125.5012
63.4118-0.8697-0.04864.20314.31324.446-1.20240.21582.30431.85781.4588-0.5348-1.9431-0.64880.21711.3724-0.179-0.01871.16-0.34081.2594137.2802144.0071-121.0068
77.1052-4.9074-3.92253.83792.42152.08861.28350.35912.0083-4.1729-1.37-3.6134-6.05042.7093-0.82863.3058-0.85010.24812.51580.22261.3817147.0819153.9942-125.066
81.96180.3419-1.88580.13611.01145.2153-1.3107-4.44066.8305-5.10684.49430.9729-7.8456-9.3758-3.9193.97161.34950.26713.16260.45112.7019135.8892160.2837-132.3286
95.65261.74546.79872.62512.378.1773-0.72871.08571.26520.66363.0731-0.77454.39320.8744-2.5012.03550.6011-0.23733.88680.21711.621699.6464132.7235-124.8042
101.9696-2.7529-0.46514.636-3.77344.9973-1.74893.8308-8.1631-3.9167-0.51121.3107-1.6712-1.5299-1.3022.26030.2443-0.11991.86380.14891.4406107.262127.2123-131.5372
114.09443.2390.12574.1551-2.35963.8987-0.88391.48383.5797-2.61742.0522-0.3509-1.1142-0.53650.38382.77680.20090.1051.7519-0.10231.6995112.6576139.2951-137.0962
124.8412-5.4207-0.93436.5886-0.93375.0963-0.69370.0037-0.2103-1.4450.5088-0.0907-1.36850.7323-0.1762.8640.23-0.26351.4215-0.41651.9471119.4711140.3503-130.5681
136.96644.0683-6.26283.0377-3.05575.16412.2791-2.53832.2741-0.08310.43140.1512-0.94911.6095-1.53381.74370.14990.00411.2848-0.24061.1577114.1663132.7523-126.2808
142.97961.63473.60294.28773.30624.2492-0.37071.44790.34-2.96140.49812.6169-3.6567-1.4812-0.77842.20240.72090.04522.86170.29911.3143102.4206140.5847-130.3524
151.57241.5431.52914.12644.41886.04791.58485.207-0.30282.9847-3.73842.9470.5012-5.88440.73242.41480.18670.10162.2879-0.20172.530398.3446128.4175-137.5329
162.46462.46781.95682.3431.64562.0065-1.55542.6302-2.0733-1.46360.757-0.45872.5272-3.03252.5133.1334-0.40370.20743.8575-0.08051.711157.2602144.2636-98.5765
178.9752-1.9655-5.5392.12393.7648.8539-0.71710.76530.885-2.79661.63080.3224-0.19560.26330.09192.29790.3991-0.31662.1711-0.16461.1984149.1947138.3712-107.6056
183.79263.90421.94024.15592.43225.88580.98641.7777-1.0859-1.5937-1.87171.27362.5861-1.78541.78682.43850.20470.01241.829-0.14491.6062145.9572126.1548-104.3131
196.9023-0.82755.97868.8323-3.34695.7438-0.00611.07610.5191-1.4473-0.2532-0.55160.12642.95630.32881.26960.0145-0.03371.7461-0.09711.1324153.3751135.7422-102.117
202.05771.93492.14847.6371-9.17871.8903-2.5982.63796.17760.0361.7059-3.4102-13.5882-4.5961-0.75543.82750.44920.6142.53180.42552.7267155.7572148.4644-111.0649
216.54650.6649-2.97758.36354.9354.53341.3237-0.22032.46731.8125-0.04511.3926-1.03831.94024.53214.6881-1.5996-0.12753.01910.10751.9578110.87104.8055-109.1284
227.5929-0.37884.15963.3511-0.70775.0882.05590.9772-1.0907-2.1771-1.22520.22030.8855-1.8184-0.3542.20460.09950.01272.30340.22791.1686116.2811113.1071-118.1377
235.09584.6065-0.57396.73252.05995.9021-1.4271-1.30542.9626-1.4249-0.2561-0.8071-0.06930.58931.28332.0144-0.1021-0.09432.02810.16781.4827114.7409125.6383-114.7609
244.6968-5.665-0.64817.51610.49198.3391.71880.0003-0.1514-0.9157-0.89750.3710.6925-1.8732-0.56421.8744-0.2946-0.15832.2943-0.02081.3058111.2965113.9101-112.7094
259.03211.20683.99854.71384.42445.0647-1.52820.0545-9.4323-2.2756-0.04840.30444.17478.6436-0.02233.18930.57380.22922.96610.28812.7489113.6816101.3686-121.8364
263.4897-0.49711.95288.2618-4.94055.2505-0.68472.1424-0.54151.07284.5865-1.92420.61744.6088-0.64832.5949-0.37010.08191.8772-0.32841.6186147.4211154.6607-156.6724
272.53582.4117-7.44952.80522.6056.08353.194.53882.1481-4.4451-3.780.0417-0.4551-0.12270.86731.42240.0992-0.34741.3572-0.02441.5026142.7219145.7661-165.6324
285.45441.91054.16865.1041-2.936.5739-4.29583.42350.6319-0.7851.54860.4793.00730.43491.70071.5740.68120.07181.3913-0.2491.5038145.5614133.3984-162.284
297.74793.37336.47229.2214-0.37596.0086-0.51111.9709-0.0799-0.32431.076-0.42370.24462.3287-0.44331.4755-0.28140.01071.7471-0.13551.1742147.7667145.3969-160.2143
308.36183.0647-6.11291.3313-2.69739.2370.3254-0.10651.634-2.60333.38780.447-0.1793-5.47-2.40843.2825-0.3238-0.42531.3606-0.24742.0047143.9664157.7117-169.1288
316.40731.1275-5.36533.78041.49577.2420.60462.40462.8134-2.48340.1844-1.4397-4.7303-5.0966-1.51843.52560.4510.28292.75970.22691.4915117.3892156.88-140.6502
326.57224.8709-3.81459.3404-7.72415.9296-0.03931.86290.34830.94641.54160.03060.1331-0.7266-1.02932.2326-0.1351-0.01131.8863-0.43691.2487122.4953148.3053-149.8345
332.8936-2.55711.87553.91151.61337.1949-1.18960.7451-0.60450.58590.84570.91051.11322.3372-0.13672.0384-0.04550.21051.737-0.31781.5987134.3756144.1064-146.4504
348.31731.5166-5.88199.41677.84998.91310.32640.29611.0861-2.87290.73610.2678-4.81130.8623-0.5322.2247-0.0163-0.10811.03110.04870.9272125.4275152.347-144.3719
355.80191.73534.8160.70231.16085.62052.64742.90874.2018-7.7311-0.23367.1587-1.5379-6.3827-2.39363.18081.1101-0.46142.98460.45393.3664113.0476155.7356-153.3183
361.61020.97371.74724.03442.40712.3051-0.5829-1.28521.7746-2.1654-1.7892-2.93392.799-0.6562.48982.56730.96720.28762.49110.5241.7288110.2129152.3369-103.8849
374.50770.33350.71238.6263-1.20811.42161.65893.2677-0.6245-1.6733-0.2991.169-2.98510.1807-0.72572.298-0.30850.31561.8901-0.20160.8901117.3929145.559-112.947
384.7914-3.8796-4.13724.25731.28386.7545-0.7038-0.9182-1.31911.1431-0.8526-2.23230.64740.1351.81622.4124-0.5287-0.00741.73340.06731.619129.9803144.6176-109.5331
395.41032.34190.58518.61457.00055.66020.38340.6370.393-1.11470.3736-0.0467-2.2958-0.7637-0.21622.0290.05920.05051.4935-0.03681.234119.0875150.2243-107.4416
406.13922.38295.42972.69292.52065.0931-0.0058-0.80891.84190.1651-0.83513.8879-0.4506-5.443-1.40552.8362-0.00010.49452.9967-0.05612.4402106.2946150.0956-116.5462
411.59991.74021.31872.4674-0.14448.6401-0.87951.4262-1.25711.8381.2896-2.0596-4.86732.5981-1.5313.04670.851-0.32.764-0.51981.6943157.5407113.9309-114.3853
425.0908-3.75133.03214.37131.21258.3323-1.08841.17950.82260.88410.5190.0230.8873-0.37720.72442.2047-0.069-0.37232.2536-0.15941.4112148.2095117.7619-123.3806
435.7519-3.201-1.16633.61283.93124.9562-0.63310.41471.08271.2292-0.39360.9011-0.9631-0.4310.78672.21090.227-0.19051.33640.08871.7565136.1812113.9451-120.0428
443.5124-0.68662.82074.1767-3.00322.82340.0606-0.8273-1.26143.90230.61381.4921-2.0987-0.7483-0.51341.74840.32340.16171.42750.3131.2815143.9384119.0775-115.746
458.87645.1066-3.21074.6264-0.41561.8803-1.71321.0646-1.0965-3.06030.4828-0.33850.49060.80130.7922.95680.7668-0.04661.8276-0.05921.3502152.0413107.5926-119.9178
465.07294.9459-6.11016.6287-6.16037.4447-3.3795-3.3124-2.62081.5615-2.5761-8.2989-1.56996.57151.27472.40790.3061-0.1642.94920.3683.0527160.2381117.5254-127.0998
473.0911.96840.85232.04877.67355.4233-2.63228.20591.95934.39160.95062.56096.7047-2.57890.04922.2102-0.695-0.61122.6480.60871.9578105.0597110.9993-145.9543
487.6939-5.03171.62745.0254-2.50017.45161.45121.6468-1.5265-2.4638-0.8447-0.10991.1269-2.6039-0.44451.8601-0.01110.08531.90780.11011.3979112.5083117.5914-155.1411
492.66160.65570.79097.42746.20995.4121-0.70732.52530.43961.0421-0.866-1.8534-0.42451.57981.26431.21190.19770.14261.71390.33681.4317114.2976130.1286-151.7318
509.3924-1.3518-6.87787.1648-4.54026.4455-0.20492.3417-0.5671-0.28730.86570.06910.8153-2.3764-0.18471.3053-0.2443-0.13051.9032-0.21010.8864107.9962119.6429-149.6957
512.02893.09441.91473.94052.39736.7091-1.94826.2637-5.0347-6.21156.88570.50812.43686.7001-4.72973.0064-0.5474-0.01822.2098-0.02892.435107.0965106.8634-158.6611
520.1061-0.3794-0.39841.66011.54351.69541.0867-2.56930.77631.099-0.03440.3936-1.61583.7414-0.46524.8625-0.4209-0.1652.246-0.25071.4435132.21297.9424-130.1201
536.37865.27182.69559.19784.70731.90421.2562.71370.6359-0.8545-0.0142-0.62041.10670.0068-0.85262.6109-0.0805-0.04182.12310.09931.2678130.5424107.68-139.2516
546.90135.5958-1.01713.305-1.20775.24490.98984.83671.32262.5080.07920.5994-2.1603-2.5907-1.28352.1886-0.40670.23181.9666-0.08711.4377120.9227115.9473-135.814
555.9961-1.4457-0.15477.7712-6.07855.073-1.43911.8054-1.3154-1.86782.43330.99332.9858-1.225-1.01721.9399-0.4767-0.00811.3986-0.00780.967126.3505104.9799-133.7899
562.02062.03212.26338.4035-1.96361.9557-6.5914-6.5944-7.4515-2.9346-0.8641-1.2937-0.194310.9037-4.35051.45480.4688-0.17253.5905-0.31862.7023136.689297.3696-142.8743
572.27332.2278-0.87989.312-1.23451.503-0.3296-3.9645-1.3512-1.89630.14683.95554.00251.6908-1.51653.03011.2866-0.28282.5962-0.681.5058152.5231107.1625-151.3567
584.2559-1.44332.1725.54463.54193.5647-0.16850.29011.1039-1.07210.65920.00590.1030.0039-0.24721.79750.23560.10421.64310.22811.5253144.6587113.4047-160.437
597.1051-0.4153-7.65042.99820.10397.4934-0.6163-0.04440.3972-1.6391-0.7840.6695-0.7447-1.20360.55851.4932-0.0762-0.34991.6784-0.13271.4444131.9591112.9863-157.0708
607.1312.8278-0.37726.3668-6.11476.08370.87740.7450.0229-2.66060.28840.03542.12131.2199-1.1462.00340.0934-0.16621.24330.0051.2183143.3917108.5707-155.082
617.07425.7875-4.8924.7191-3.66354.43975.99992.4599-2.1714-5.7577-1.2859-3.43592.61271.046-4.01781.86490.93750.36893.0411-0.00232.3852156.1105110.0285-164.0021
628.48265.5891.47059.00332.98421.0730.17835.1705-5.0289-4.28776.2091-2.7261-4.15014.6999-1.83592.89920.2420.34873.2251-0.30861.7452160.3498136.1867-135.4165
6310.5787-5.8382-3.17597.5786-0.01078.07050.32840.2077-0.0317-4.61511.51130.13011.0651-0.2913-0.89852.4284-0.0279-0.03731.7967-0.01291.0144151.0037132.7926-144.5172
644.64-5.48653.50686.1414-5.37435.3122.434-0.33622.2329-3.359-2.3719-1.24841.4831-2.1518-0.07352.13250.3063-0.37381.8284-0.11731.6247144.6169121.9109-141.1321
655.7769-2.42646.37467.3434-1.48185.83381.64482.5876-0.8034-0.6565-1.3029-0.2783-0.7153.5181-0.14511.42470.3574-0.03992.0451-0.03741.2206154.4075129.1439-139.1144
661.9085-0.47221.80617.4781-8.92011.9816-0.80625.84027.93056.69490.2395-8.1933-6.6552-1.7511-1.20333.84060.4069-0.06832.18420.06153.6503160.1778140.6738-148.0864
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1ELECTRON MICROSCOPY1chain 'G' and (resid 112 through 117 )
2ELECTRON MICROSCOPY2chain 'G' and (resid 118 through 128 )
3ELECTRON MICROSCOPY3chain 'G' and (resid 129 through 136 )
4ELECTRON MICROSCOPY4chain 'G' and (resid 137 through 142 )
5ELECTRON MICROSCOPY5chain 'G' and (resid 143 through 154 )
6ELECTRON MICROSCOPY6chain 'G' and (resid 155 through 168 )
7ELECTRON MICROSCOPY7chain 'G' and (resid 169 through 184 )
8ELECTRON MICROSCOPY8chain 'G' and (resid 185 through 194 )
9ELECTRON MICROSCOPY9chain 'A' and (resid 112 through 117 )
10ELECTRON MICROSCOPY10chain 'A' and (resid 118 through 128 )
11ELECTRON MICROSCOPY11chain 'A' and (resid 129 through 136 )
12ELECTRON MICROSCOPY12chain 'A' and (resid 137 through 154 )
13ELECTRON MICROSCOPY13chain 'A' and (resid 155 through 168 )
14ELECTRON MICROSCOPY14chain 'A' and (resid 169 through 184 )
15ELECTRON MICROSCOPY15chain 'A' and (resid 185 through 194 )
16ELECTRON MICROSCOPY16chain 'B' and (resid 112 through 117 )
17ELECTRON MICROSCOPY17chain 'B' and (resid 118 through 136 )
18ELECTRON MICROSCOPY18chain 'B' and (resid 137 through 154 )
19ELECTRON MICROSCOPY19chain 'B' and (resid 155 through 184 )
20ELECTRON MICROSCOPY20chain 'B' and (resid 185 through 194 )
21ELECTRON MICROSCOPY21chain 'C' and (resid 112 through 117 )
22ELECTRON MICROSCOPY22chain 'C' and (resid 118 through 136 )
23ELECTRON MICROSCOPY23chain 'C' and (resid 137 through 154 )
24ELECTRON MICROSCOPY24chain 'C' and (resid 155 through 184 )
25ELECTRON MICROSCOPY25chain 'C' and (resid 185 through 194 )
26ELECTRON MICROSCOPY26chain 'D' and (resid 112 through 117 )
27ELECTRON MICROSCOPY27chain 'D' and (resid 118 through 136 )
28ELECTRON MICROSCOPY28chain 'D' and (resid 137 through 154 )
29ELECTRON MICROSCOPY29chain 'D' and (resid 155 through 184 )
30ELECTRON MICROSCOPY30chain 'D' and (resid 185 through 194 )
31ELECTRON MICROSCOPY31chain 'E' and (resid 112 through 117 )
32ELECTRON MICROSCOPY32chain 'E' and (resid 118 through 136 )
33ELECTRON MICROSCOPY33chain 'E' and (resid 137 through 154 )
34ELECTRON MICROSCOPY34chain 'E' and (resid 155 through 184 )
35ELECTRON MICROSCOPY35chain 'E' and (resid 185 through 194 )
36ELECTRON MICROSCOPY36chain 'F' and (resid 112 through 117 )
37ELECTRON MICROSCOPY37chain 'F' and (resid 118 through 136 )
38ELECTRON MICROSCOPY38chain 'F' and (resid 137 through 154 )
39ELECTRON MICROSCOPY39chain 'F' and (resid 155 through 184 )
40ELECTRON MICROSCOPY40chain 'F' and (resid 185 through 194 )
41ELECTRON MICROSCOPY41chain 'H' and (resid 112 through 117 )
42ELECTRON MICROSCOPY42chain 'H' and (resid 118 through 136 )
43ELECTRON MICROSCOPY43chain 'H' and (resid 137 through 154 )
44ELECTRON MICROSCOPY44chain 'H' and (resid 155 through 168 )
45ELECTRON MICROSCOPY45chain 'H' and (resid 169 through 184 )
46ELECTRON MICROSCOPY46chain 'H' and (resid 185 through 194 )
47ELECTRON MICROSCOPY47chain 'I' and (resid 112 through 117 )
48ELECTRON MICROSCOPY48chain 'I' and (resid 118 through 136 )
49ELECTRON MICROSCOPY49chain 'I' and (resid 137 through 154 )
50ELECTRON MICROSCOPY50chain 'I' and (resid 155 through 184 )
51ELECTRON MICROSCOPY51chain 'I' and (resid 185 through 194 )
52ELECTRON MICROSCOPY52chain 'J' and (resid 112 through 117 )
53ELECTRON MICROSCOPY53chain 'J' and (resid 118 through 136 )
54ELECTRON MICROSCOPY54chain 'J' and (resid 137 through 154 )
55ELECTRON MICROSCOPY55chain 'J' and (resid 155 through 184 )
56ELECTRON MICROSCOPY56chain 'J' and (resid 185 through 194 )
57ELECTRON MICROSCOPY57chain 'K' and (resid 112 through 117 )
58ELECTRON MICROSCOPY58chain 'K' and (resid 118 through 136 )
59ELECTRON MICROSCOPY59chain 'K' and (resid 137 through 154 )
60ELECTRON MICROSCOPY60chain 'K' and (resid 155 through 184 )
61ELECTRON MICROSCOPY61chain 'K' and (resid 185 through 194 )
62ELECTRON MICROSCOPY62chain 'L' and (resid 112 through 117 )
63ELECTRON MICROSCOPY63chain 'L' and (resid 118 through 136 )
64ELECTRON MICROSCOPY64chain 'L' and (resid 137 through 154 )
65ELECTRON MICROSCOPY65chain 'L' and (resid 155 through 184 )
66ELECTRON MICROSCOPY66chain 'L' and (resid 185 through 194 )

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