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- PDB-7kzr: Structure of the human Fanconi Anaemia Core-UBE2T-ID complex -

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Basic information

Entry
Database: PDB / ID: 7kzr
TitleStructure of the human Fanconi Anaemia Core-UBE2T-ID complex
Components
  • (Fanconi anemia core complex-associated protein ...) x 2
  • (Fanconi anemia group ...) x 7
  • E3 ubiquitin-protein ligase FANCL
  • Fanconi anemia, complementation group I
  • Ubiquitin-conjugating enzyme E2 T
KeywordsLIGASE / Complex
Function / homology
Function and homology information


regulation of germ cell proliferation / regulation of CD40 signaling pathway / Fanconi anaemia nuclear complex / protein K27-linked ubiquitination / regulation of regulatory T cell differentiation / protein K29-linked ubiquitination / homologous chromosome pairing at meiosis / male meiotic nuclear division / double-strand break repair involved in meiotic recombination / gamete generation ...regulation of germ cell proliferation / regulation of CD40 signaling pathway / Fanconi anaemia nuclear complex / protein K27-linked ubiquitination / regulation of regulatory T cell differentiation / protein K29-linked ubiquitination / homologous chromosome pairing at meiosis / male meiotic nuclear division / double-strand break repair involved in meiotic recombination / gamete generation / neuronal stem cell population maintenance / replication-born double-strand break repair via sister chromatid exchange / protein K6-linked ubiquitination / brain morphogenesis / protein K11-linked ubiquitination / myeloid cell homeostasis / DNA repair complex / mitotic intra-S DNA damage checkpoint signaling / E2 ubiquitin-conjugating enzyme / female gonad development / protein monoubiquitination / germ cell development / ubiquitin conjugating enzyme activity / protein K63-linked ubiquitination / spermatid development / negative regulation of double-strand break repair via homologous recombination / positive regulation of double-strand break repair via homologous recombination / protein autoubiquitination / protein K48-linked ubiquitination / interstrand cross-link repair / DNA polymerase binding / condensed chromosome / ovarian follicle development / removal of superoxide radicals / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / response to gamma radiation / mitochondrion organization / TP53 Regulates Transcription of DNA Repair Genes / nucleotide-excision repair / Fanconi Anemia Pathway / RING-type E3 ubiquitin transferase / response to radiation / PKR-mediated signaling / protein polyubiquitination / ubiquitin-protein transferase activity / male gonad development / ubiquitin protein ligase activity / nuclear envelope / chromosome / regulation of cell population proliferation / cellular response to oxidative stress / regulation of inflammatory response / protein-containing complex assembly / damaged DNA binding / nuclear body / intracellular membrane-bounded organelle / DNA repair / centrosome / DNA damage response / chromatin binding / ubiquitin protein ligase binding / chromatin / nucleolus / mitochondrion / DNA binding / nucleoplasm / ATP binding / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Fanconi anaemia group C protein / Fanconi anemia-associated protein of 100kDa / Fanconi anemia group B protein / Fanconi anemia group G protein / Fanconi anaemia group C protein / Fanconi anemia-associated / Fanconi Anaemia group E protein, C-terminal / Fanconi anemia group F protein / FANCF, C-terminal domain superfamily / Fanconi anemia group E protein ...Fanconi anaemia group C protein / Fanconi anemia-associated protein of 100kDa / Fanconi anemia group B protein / Fanconi anemia group G protein / Fanconi anaemia group C protein / Fanconi anemia-associated / Fanconi Anaemia group E protein, C-terminal / Fanconi anemia group F protein / FANCF, C-terminal domain superfamily / Fanconi anemia group E protein / Fanconi anemia group F protein (FANCF) / Fanconi Anaemia group E protein FANCE / Fanconi anaemia group A protein / Fanconi anaemia group A protein, N-terminal domain / Fanconi anaemia group A protein / Fanconi anaemia group A protein N terminus / Fanconi anemia complex, subunit FancL, WD-repeat containing domain / E3 ubiquitin-protein ligase FANCL / FANCL C-terminal domain / FANCL, UBC-like domain 3 superfamily / FANCL, UBC-like domain 2 / FANCL, UBC-like domain 3 / FANCL UBC-like domain 1 / FANCL C-terminal domain / FANCL UBC-like domain 2 / FANCL UBC-like domain 3 / FANCL C-terminal domain / Fanconi anemia group I protein / FANCI solenoid 1 cap / FANCI solenoid 1 domain / FANCI helical domain 1 / FANCI helical domain 2 / FANCI solenoid 3 domain / FANCI solenoid 4 domain / FANCI solenoid 2 domain / FANCI solenoid 1 cap / FANCI solenoid 1 / FANCI solenoid 2 / FANCI solenoid 3 / FANCI solenoid 4 / FANCI helical domain 1 / FANCI helical domain 2 / Fanconi anaemia protein FANCD2 / Fanconi anaemia protein FancD2 nuclease / : / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
Fanconi anemia, complementation group I / Fanconi anemia group G protein / Fanconi anemia group A protein / Fanconi anemia group C protein / Fanconi anemia core complex-associated protein 100 / Fanconi anemia group B protein / Fanconi anemia group D2 protein / Fanconi anemia group E protein / Ubiquitin-conjugating enzyme E2 T / Fanconi anemia group F protein / E3 ubiquitin-protein ligase FANCL
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsWang, S.L. / Pavletich, N.P.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nat Struct Mol Biol / Year: 2021
Title: Structure of the FA core ubiquitin ligase closing the ID clamp on DNA.
Authors: Shengliu Wang / Renjing Wang / Christopher Peralta / Ayat Yaseen / Nikola P Pavletich /
Abstract: The Fanconi anemia (FA) pathway is essential for the repair of DNA interstrand crosslinks. Central to the pathway is the FA core complex, a ubiquitin ligase of nine subunits that monoubiquitinates ...The Fanconi anemia (FA) pathway is essential for the repair of DNA interstrand crosslinks. Central to the pathway is the FA core complex, a ubiquitin ligase of nine subunits that monoubiquitinates the FANCI-FANCD2 (ID) DNA clamp. The 3.1 Å structure of the 1.1-MDa human FA core complex, described here, reveals an asymmetric assembly with two copies of all but the FANCC, FANCE and FANCF subunits. The asymmetry is crucial, as it prevents the binding of a second FANCC-FANCE-FANCF subcomplex that inhibits the recruitment of the UBE2T ubiquitin conjugating enzyme, and instead creates an ID binding site. A single active site then ubiquitinates FANCD2 and FANCI sequentially. We also present the 4.2-Å structures of the human core-UBE2T-ID-DNA complex in three conformations captured during monoubiquitination. They reveal the core-UBE2T complex remodeling the ID-DNA complex, closing the clamp on the DNA before ubiquitination. Monoubiquitination then prevents clamp opening after release from the core.
History
DepositionDec 10, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 10, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Mar 6, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / refine
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine.ls_d_res_high / _refine.ls_d_res_low

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Structure visualization

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Assembly

Deposited unit
A: Fanconi anemia group A protein
B: Fanconi anemia group B protein
C: Fanconi anemia group C protein
E: Fanconi anemia group E protein
F: Fanconi anemia group F protein
G: Fanconi anemia group G protein
H: Fanconi anemia group G protein
L: E3 ubiquitin-protein ligase FANCL
M: E3 ubiquitin-protein ligase FANCL
O: Fanconi anemia group B protein
P: Fanconi anemia core complex-associated protein 100
Q: Fanconi anemia core complex-associated protein 100
S: Fanconi anemia group A protein
W: Fanconi anemia core complex-associated protein 20
U: Fanconi anemia, complementation group I
V: Fanconi anemia group D2 protein
X: Ubiquitin-conjugating enzyme E2 T
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,470,67422
Polymers1,470,34717
Non-polymers3275
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Fanconi anemia group ... , 7 types, 10 molecules ASBOCEFGHV

#1: Protein Fanconi anemia group A protein / Protein FACA


Mass: 165513.016 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCA, FAA, FACA, FANCH / Production host: Homo sapiens (human) / References: UniProt: O15360
#2: Protein Fanconi anemia group B protein / Protein FACB / Fanconi anemia-associated polypeptide of 95 kDa / FAAP95


Mass: 100640.172 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCB / Production host: Homo sapiens (human) / References: UniProt: Q8NB91
#3: Protein Fanconi anemia group C protein / Protein FACC


Mass: 66290.359 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCC, FAC, FACC / Production host: Homo sapiens (human) / References: UniProt: Q00597
#4: Protein Fanconi anemia group E protein / Protein FACE


Mass: 61026.086 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCE, FACE / Production host: Homo sapiens (human) / References: UniProt: Q9HB96
#5: Protein Fanconi anemia group F protein / Protein FACF


Mass: 45108.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCF / Production host: Homo sapiens (human) / References: UniProt: Q9NPI8
#6: Protein Fanconi anemia group G protein / Protein FACG / DNA repair protein XRCC9


Mass: 70873.727 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCG, XRCC9 / Production host: Homo sapiens (human) / References: UniProt: O15287
#11: Protein Fanconi anemia group D2 protein / Protein FACD2


Mass: 164325.516 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCD2, FACD / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9BXW9

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Protein , 3 types, 4 molecules LMUX

#7: Protein E3 ubiquitin-protein ligase FANCL / Fanconi anemia group L protein / Fanconi anemia-associated polypeptide of 43 kDa / FAAP43 / RING- ...Fanconi anemia group L protein / Fanconi anemia-associated polypeptide of 43 kDa / FAAP43 / RING-type E3 ubiquitin transferase FANCL


Mass: 45203.953 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCL, PHF9 / Production host: Homo sapiens (human)
References: UniProt: Q9NW38, RING-type E3 ubiquitin transferase
#10: Protein Fanconi anemia, complementation group I


Mass: 149512.078 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCI / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: B7ZMF2
#12: Protein Ubiquitin-conjugating enzyme E2 T / Cell proliferation-inducing gene 50 protein / E2 ubiquitin-conjugating enzyme T / Ubiquitin carrier ...Cell proliferation-inducing gene 50 protein / E2 ubiquitin-conjugating enzyme T / Ubiquitin carrier protein T / Ubiquitin-protein ligase T


Mass: 22553.873 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2T, HSPC150, PIG50 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9NPD8, E2 ubiquitin-conjugating enzyme

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Fanconi anemia core complex-associated protein ... , 2 types, 3 molecules PQW

#8: Protein Fanconi anemia core complex-associated protein 100 / Fanconi anemia-associated protein of 100 kDa


Mass: 96513.898 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FAAP100, C17orf70 / Production host: Homo sapiens (human) / References: UniProt: Q0VG06
#9: Protein/peptide Fanconi anemia core complex-associated protein 20


Mass: 4041.667 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)

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Non-polymers , 1 types, 5 molecules

#13: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn

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Details

Has ligand of interestN
Sequence detailsThe complete sequence of FAAP20 is MEAARRPRLGLSRRRPPPAGGPSGGRPWFLLGGDERERLWAELLRTVSPELILDHEVPSL ...The complete sequence of FAAP20 is MEAARRPRLGLSRRRPPPAGGPSGGRPWFLLGGDERERLWAELLRTVSPELILDHEVPSL PAFPGQEPRCGPEPTEVFTVGPKTFSWTPFPPDLWGPGRSYRLLHGAGGHLESPARSLPQ RPAPDPCRAPRVEQQPSVEGAAALRSCPMCQKEFAPRLTQLDVDSHLAQCLAESTEDVTW

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Human Fanconi Anaemia Core-UBE2T-ID complex / Type: COMPLEX / Entity ID: #1-#12 / Source: RECOMBINANT
Molecular weightValue: 1.4 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMBicineC6H13NO41
2150 mMsodium chlorideNaCl1
31 mMDithiothreitolC4H10O2S21
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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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: BRIGHT FIELD
Image recordingElectron dose: 60 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: REFMAC / Version: 5.8.0267 / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 114249 / Symmetry type: POINT
RefinementResolution: 4.4→4.4 Å / Cor.coef. Fo:Fc: 0.967 / SU B: 114.471 / SU ML: 0.615 / ESU R: 0.735
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.31228 --
obs0.31228 623501 100 %
Solvent computationIon probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: MASK
Displacement parametersBiso mean: 79.835 Å2
Baniso -1Baniso -2Baniso -3
1--5.84 Å24.59 Å22.14 Å2
2--6.49 Å28.29 Å2
3----0.65 Å2
Refinement stepCycle: 1 / Total: 86745
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0120.01388489
ELECTRON MICROSCOPYr_bond_other_d0.0130.01786047
ELECTRON MICROSCOPYr_angle_refined_deg1.561.632119890
ELECTRON MICROSCOPYr_angle_other_deg1.611.571198197
ELECTRON MICROSCOPYr_dihedral_angle_1_deg8.608510913
ELECTRON MICROSCOPYr_dihedral_angle_2_deg33.70722.0784356
ELECTRON MICROSCOPYr_dihedral_angle_3_deg16.0091515704
ELECTRON MICROSCOPYr_dihedral_angle_4_deg16.24915579
ELECTRON MICROSCOPYr_chiral_restr0.0810.211498
ELECTRON MICROSCOPYr_gen_planes_refined0.0060.0298196
ELECTRON MICROSCOPYr_gen_planes_other0.0030.0219810
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it2.77812.35443976
ELECTRON MICROSCOPYr_mcbond_other2.77812.35443975
ELECTRON MICROSCOPYr_mcangle_it5.15354781
ELECTRON MICROSCOPYr_mcangle_other5.15354782
ELECTRON MICROSCOPYr_scbond_it2.03312.43244513
ELECTRON MICROSCOPYr_scbond_other2.03312.43244514
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other4.14665110
ELECTRON MICROSCOPYr_long_range_B_refined14.202276938
ELECTRON MICROSCOPYr_long_range_B_other14.202276938
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 4.2→4.309 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0 0 -
Rwork0.468 46230 -
obs--100 %
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)
12.6717-2.9431.949116.68535.05555.3109-0.2935-0.4656-0.47381.39330.01871.58510.2056-0.54410.27491.0958-0.21780.15730.95280.23050.659378.387206.27886.489
23.2192-3.3279-1.84695.67460.81943.6117-0.23830.00990.17650.56870.12630.03990.7445-0.36790.11190.8296-0.1543-0.00230.91660.13290.737690.29199.80976.225
34.60121.0081-1.95053.72182.9314.0622-0.2171-0.14920.43330.5744-0.20980.64320.6539-0.04490.42680.8330.12540.01540.94690.07680.903486.585215.64685.645
41.6128-2.8952-0.67216.9688-0.46472.02540.0187-0.09450.15920.0269-0.0181-0.22760.1409-0.0912-0.00070.7812-0.03720.03641.05380.09980.821593.071208.61972.521
52.6464-1.4006-2.50361.76453.08735.481-0.1031-0.07680.14610.16070.2141-0.14570.11670.277-0.1110.8015-0.0250.0420.85750.14391.0802104.516217.17172.521
62.72155.7173-0.006124.99356.44933.31390.0632-0.015-0.125-0.096-0.2058-0.2479-0.07480.21120.14270.70760.038-0.01581.0310.16990.784103.869196.31851.161
725.36184.3764-12.66040.8459-2.14386.35750.0774-2.3018-0.30910.1455-0.0218-0.1280.05751.3195-0.05570.80450.4481-0.44911.7795-0.29131.6923107.974182.08854.35
81.83110.34370.4890.64170.40350.9867-0.0698-0.04020.1760.12340.00490.0776-0.0611-0.01940.06480.70390.07880.01740.89410.12720.885278.739190.46852.923
91.0091-0.2023-1.35890.08940.22892.3107-0.1012-0.031-0.1363-0.1333-0.12660.01460.2008-0.07090.22790.74040.1296-0.09690.95670.11971.084262.702179.82933.555
105.22846.1384-4.45557.2285-5.23213.79850.2462-0.2137-0.19120.3737-0.3721-0.2282-0.22910.18080.12590.959-0.0124-0.00221.0551-0.06841.114156.435165.35343.322
1112.302-1.4699-6.27838.56733.3724.0253-0.20160.4226-0.2631-0.02710.05260.1230.0635-0.21180.14890.6572-0.0425-0.10240.94540.07990.986959.554178.59745.104
124.5897-3.71611.39577.258-1.51740.4731-0.11470.5922-0.00040.75050.08510.5638-0.06810.16590.02960.6048-0.0228-0.07871.09020.01281.027445.809184.29836.008
130.66211.21920.81752.31691.5821.0921-0.02710.0699-0.1186-0.032-0.0396-0.0039-0.0278-0.11410.06660.56190.04740.15611.09430.01341.070437.882184.47544.699
141.13521.31541.62223.85052.40552.6002-0.3032-0.27570.79850.362-0.47761.4775-0.3048-0.37810.78080.41620.34370.16321.0782-0.07182.242346.726199.33746.01
152.4468-3.191-1.09465.7247-1.24025.4622-0.2335-0.17290.13490.32330.35070.01110.32570.3812-0.11720.69010.05750.01110.94270.10610.8669102.89167.35746.901
164.00661.1592-3.20797.56113.93287.36-0.4566-0.0864-0.0371-0.59870.4980.4849-0.23840.8051-0.04150.6660.07140.05490.94950.17470.758190.839173.90239.687
177.59673.45461.41995.0547.731614.6995-0.26790.73360.8646-0.31650.69010.0712-0.39710.7824-0.42220.7627-0.1062-0.08580.92940.08130.878390.035164.46430.355
1820.1852.34817.3143.25455.672719.3622-0.46810.9441-0.25530.54910.20990.31250.44770.96820.25830.80390.1150.08060.83930.32090.918991.84159.88448.366
1920.2652-9.77.22944.8184-1.967116.7261-0.5677-1.2495-0.04460.18550.49030.0193-0.2389-0.42250.07750.8950.1649-0.0081.05140.05790.9086100.386166.15566.432
203.0725-1.29661.95220.5682-0.59784.0278-0.0121-0.04670.00860.02270.0866-0.0021-0.02580.2506-0.07460.77640.02370.00780.87740.10330.92789.048170.96350.765
210.5722.07611.09347.73324.12022.31450.21940.0353-0.05620.4782-0.0917-0.16510.3035-0.4074-0.12770.76660.0350.00421.16150.32121.119580.074161.49348.059
224.1191-7.09322.17725.120613.012223.0033-0.2954-0.57910.25640.88361.2242-1.41710.2532-0.0593-0.92880.75020.0453-0.10081.03510.3170.862384.677169.13363.822
2313.015112.358613.19421.231213.846513.57330.4238-0.38520.0911.5219-0.52030.3380.6691-0.36750.09650.75190.07040.06430.94060.19480.755277.871171.37254.674
243.30354.44875.79236.23527.868610.2330.447-0.45710.35830.9866-0.93530.79030.9776-0.93820.48841.1813-0.10250.37961.253-0.01581.396970.048165.22356.511
255.9855-2.19211.70244.43291.09991.39610.1508-0.8120.39070.5355-0.27690.25830.1361-0.52370.12610.6532-0.01980.19631.05450.13260.786761.918182.22561.384
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1154.4381-0.77130.9563.58051.06161.52060.30320.36810.1397-0.08780.2022-0.9405-0.31630.2711-0.50540.32380.15130.37951.4350.25940.8019132.893126.771172.69
1162.8428-1.6534-0.78632.27933.00786.98720.10330.10410.0696-0.31190.035-0.0747-0.49170.4341-0.13840.63480.12030.0711.02980.19080.48109.517132.002179.83
1172.08911.79750.02384.5180.89214.12380.2802-0.00880.0307-0.2467-0.1287-0.1469-0.2541-0.1761-0.15160.58440.14050.2040.90160.22180.667892.798132.137192.359
1182.00460.5841-0.24161.5309-0.77641.66260.12160.0180.06540.0751-0.01580.0501-0.0705-0.0486-0.10570.6750.04860.10520.90520.21060.713380.446124.783208.692
1192.00961.4894-1.29461.3978-0.84531.7557-0.0899-0.0779-0.1253-0.06220.09390.0110.18790.0006-0.00410.7038-0.07680.04020.95860.24830.717363.092104.251230.073
1201.4443-0.3219-0.38625.16910.05460.2722-0.1030.2035-0.5454-0.7662-0.28961.3-0.1004-0.49230.39260.92650.133-0.31051.8233-0.10441.739428.283106.378230.905
1210.2314-0.4719-0.27571.06470.65130.41030.21210.3441-0.3163-0.3667-0.48470.5205-0.2601-0.18020.27261.41370.2306-0.03832.32270.24551.510732.161120.968205.288
1220.014-0.011-0.00530.00910.00550.00750.11460.06570.0721-0.0967-0.0283-0.0666-0.05420.0412-0.08621.10720.12140.52481.6353-0.02671.223232.654147.515205.008
1230.0005-0.0004-0.00020.0035-0.0070.0162-0.01070.02830.00630.06920.01840.0058-0.1187-0.1079-0.00761.7294-0.0590.66932.19870.09521.100448.491164.889206.465
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1ELECTRON MICROSCOPY1C1 - 14
2ELECTRON MICROSCOPY2C15 - 49
3ELECTRON MICROSCOPY3C50 - 70
4ELECTRON MICROSCOPY4C71 - 94
5ELECTRON MICROSCOPY5C95 - 144
6ELECTRON MICROSCOPY6C145 - 169
7ELECTRON MICROSCOPY7C170 - 178
8ELECTRON MICROSCOPY8C179 - 326
9ELECTRON MICROSCOPY9C327 - 378
10ELECTRON MICROSCOPY10C379 - 390
11ELECTRON MICROSCOPY11C391 - 400
12ELECTRON MICROSCOPY12C401 - 425
13ELECTRON MICROSCOPY13C426 - 483
14ELECTRON MICROSCOPY14C484 - 558
15ELECTRON MICROSCOPY15E12 - 25
16ELECTRON MICROSCOPY16E26 - 47
17ELECTRON MICROSCOPY17E48 - 59
18ELECTRON MICROSCOPY18E60 - 72
19ELECTRON MICROSCOPY19E73 - 83
20ELECTRON MICROSCOPY20E84 - 104
21ELECTRON MICROSCOPY21E105 - 120
22ELECTRON MICROSCOPY22E121 - 130
23ELECTRON MICROSCOPY23E131 - 142
24ELECTRON MICROSCOPY24E143 - 154
25ELECTRON MICROSCOPY25E155 - 181
26ELECTRON MICROSCOPY26F1 - 183
27ELECTRON MICROSCOPY27F184 - 355
28ELECTRON MICROSCOPY28L1 - 103
29ELECTRON MICROSCOPY29L104 - 197
30ELECTRON MICROSCOPY30L198 - 296
31ELECTRON MICROSCOPY31L297 - 402
32ELECTRON MICROSCOPY32M1 - 103
33ELECTRON MICROSCOPY33M104 - 197
34ELECTRON MICROSCOPY34M198 - 296
35ELECTRON MICROSCOPY35M297 - 402
36ELECTRON MICROSCOPY36G12 - 342
37ELECTRON MICROSCOPY36S32 - 55
38ELECTRON MICROSCOPY37G343 - 611
39ELECTRON MICROSCOPY37S19 - 31
40ELECTRON MICROSCOPY38S56 - 246
41ELECTRON MICROSCOPY39S265 - 524
42ELECTRON MICROSCOPY40S542 - 627
43ELECTRON MICROSCOPY41S648 - 1033
44ELECTRON MICROSCOPY42S1043 - 1215
45ELECTRON MICROSCOPY43S1216 - 1443
46ELECTRON MICROSCOPY44H12 - 386
47ELECTRON MICROSCOPY44A29 - 55
48ELECTRON MICROSCOPY45H387 - 611
49ELECTRON MICROSCOPY45A19 - 28
50ELECTRON MICROSCOPY46A56 - 248
51ELECTRON MICROSCOPY47A262 - 401
52ELECTRON MICROSCOPY48A402 - 524
53ELECTRON MICROSCOPY49A648 - 1034
54ELECTRON MICROSCOPY49A2001 - 2107
55ELECTRON MICROSCOPY50A1043 - 1215
56ELECTRON MICROSCOPY51A1216 - 1443
57ELECTRON MICROSCOPY52B7 - 254
58ELECTRON MICROSCOPY53B255 - 369
59ELECTRON MICROSCOPY54B385 - 476
60ELECTRON MICROSCOPY55B477 - 493
61ELECTRON MICROSCOPY56B494 - 502
62ELECTRON MICROSCOPY57B503 - 511
63ELECTRON MICROSCOPY58B512 - 518
64ELECTRON MICROSCOPY59B519 - 531
65ELECTRON MICROSCOPY60B532 - 574
66ELECTRON MICROSCOPY61B575 - 601
67ELECTRON MICROSCOPY62B602 - 612
68ELECTRON MICROSCOPY63B613 - 634
69ELECTRON MICROSCOPY64B635 - 644
70ELECTRON MICROSCOPY65B645 - 663
71ELECTRON MICROSCOPY66B664 - 687
72ELECTRON MICROSCOPY67B688 - 735
73ELECTRON MICROSCOPY68B736 - 770
74ELECTRON MICROSCOPY69B771 - 837
75ELECTRON MICROSCOPY70B838 - 859
76ELECTRON MICROSCOPY71P5 - 86
77ELECTRON MICROSCOPY72P87 - 130
78ELECTRON MICROSCOPY73P131 - 155
79ELECTRON MICROSCOPY74P156 - 217
80ELECTRON MICROSCOPY75P218 - 280
81ELECTRON MICROSCOPY76P281 - 346
82ELECTRON MICROSCOPY77P347 - 371
83ELECTRON MICROSCOPY78P372 - 418
84ELECTRON MICROSCOPY79P419 - 433
85ELECTRON MICROSCOPY80P434 - 457
86ELECTRON MICROSCOPY81P458 - 509
87ELECTRON MICROSCOPY82P510 - 531
88ELECTRON MICROSCOPY83P532 - 548
89ELECTRON MICROSCOPY84P549 - 557
90ELECTRON MICROSCOPY85P558 - 584
91ELECTRON MICROSCOPY86P585 - 593
92ELECTRON MICROSCOPY87P594 - 605
93ELECTRON MICROSCOPY88P606 - 636
94ELECTRON MICROSCOPY89P637 - 654
95ELECTRON MICROSCOPY90P655 - 709
96ELECTRON MICROSCOPY91P710 - 754
97ELECTRON MICROSCOPY92P755 - 768
98ELECTRON MICROSCOPY93P769 - 784
99ELECTRON MICROSCOPY94P785 - 808
100ELECTRON MICROSCOPY95P809 - 836
101ELECTRON MICROSCOPY96P837 - 881
102ELECTRON MICROSCOPY97O7 - 369
103ELECTRON MICROSCOPY98O391 - 432
104ELECTRON MICROSCOPY98Q449 - 500
105ELECTRON MICROSCOPY99O471 - 655
106ELECTRON MICROSCOPY100O656 - 749
107ELECTRON MICROSCOPY100Q669 - 685
108ELECTRON MICROSCOPY101O750 - 859
109ELECTRON MICROSCOPY101Q823 - 881
110ELECTRON MICROSCOPY102Q5 - 435
111ELECTRON MICROSCOPY103Q501 - 668
112ELECTRON MICROSCOPY104Q701 - 822
113ELECTRON MICROSCOPY105X1 - 153
114ELECTRON MICROSCOPY106U1 - 169
115ELECTRON MICROSCOPY107U170 - 305
116ELECTRON MICROSCOPY108U306 - 398
117ELECTRON MICROSCOPY109U411 - 684
118ELECTRON MICROSCOPY110U696 - 791
119ELECTRON MICROSCOPY111U801 - 934
120ELECTRON MICROSCOPY112U949 - 1039
121ELECTRON MICROSCOPY113U1040 - 1154
122ELECTRON MICROSCOPY114U1155 - 1280
123ELECTRON MICROSCOPY115V45 - 187
124ELECTRON MICROSCOPY116V188 - 254
125ELECTRON MICROSCOPY117V255 - 311
126ELECTRON MICROSCOPY118V337 - 465
127ELECTRON MICROSCOPY119V466 - 623
128ELECTRON MICROSCOPY120V624 - 839
129ELECTRON MICROSCOPY121V916 - 1145
130ELECTRON MICROSCOPY122V1150 - 1250
131ELECTRON MICROSCOPY123V1251 - 1376

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