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- PDB-6vae: Mono-ubiquitinated Fanconi Anemia ID complex bound to ICL DNA -

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Basic information

Entry
Database: PDB / ID: 6vae
TitleMono-ubiquitinated Fanconi Anemia ID complex bound to ICL DNA
Components
  • (DNA (29-MER)) x 2
  • Fanconi anemia group D2 protein
  • Fanconi anemia, complementation group I
  • Ubiquitin
KeywordsDNA BINDING PROTEIN/DNA / DNA clamp / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


regulation of CD40 signaling pathway / regulation of regulatory T cell differentiation / gamete generation / double-strand break repair involved in meiotic recombination / homologous chromosome pairing at meiosis / neuronal stem cell population maintenance / brain morphogenesis / mitotic intra-S DNA damage checkpoint signaling / DNA repair complex / interstrand cross-link repair ...regulation of CD40 signaling pathway / regulation of regulatory T cell differentiation / gamete generation / double-strand break repair involved in meiotic recombination / homologous chromosome pairing at meiosis / neuronal stem cell population maintenance / brain morphogenesis / mitotic intra-S DNA damage checkpoint signaling / DNA repair complex / interstrand cross-link repair / condensed chromosome / DNA polymerase binding / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / positive regulation of protein ubiquitination / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / response to gamma radiation / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / TP53 Regulates Transcription of DNA Repair Genes / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Negative regulation of FGFR3 signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Fanconi Anemia Pathway / Peroxisomal protein import / Degradation of AXIN / Regulation of TNFR1 signaling / Negative regulation of FGFR2 signaling
Similarity search - Function
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 ...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 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
DNA / DNA (> 10) / Fanconi anemia, complementation group I / Polyubiquitin-C / Fanconi anemia group D2 protein / Fanconi anemia group I protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsPavletich, N.P.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nature / Year: 2020
Title: DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex.
Authors: Renjing Wang / Shengliu Wang / Ankita Dhar / Christopher Peralta / Nikola P Pavletich /
Abstract: The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions. These proteins are mutated in Fanconi anaemia, a disease ...The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions. These proteins are mutated in Fanconi anaemia, a disease in which patients are predisposed to cancer. The Fanconi anaemia pathway of ICL repair is activated when a replication fork stalls at an ICL; this triggers monoubiquitination of the ID complex, in which one ubiquitin molecule is conjugated to each of FANCI and FANCD2. Monoubiquitination of ID is essential for ICL repair by excision, translesion synthesis and homologous recombination; however, its function remains unknown. Here we report a cryo-electron microscopy structure of the monoubiquitinated human ID complex bound to DNA, and reveal that it forms a closed ring that encircles the DNA. By comparison with the structure of the non-ubiquitinated ID complex bound to ICL DNA-which we also report here-we show that monoubiquitination triggers a complete rearrangement of the open, trough-like ID structure through the ubiquitin of one protomer binding to the other protomer in a reciprocal fashion. These structures-together with biochemical data-indicate that the monoubiquitinated ID complex loses its preference for ICL and related branched DNA structures, and becomes a sliding DNA clamp that can coordinate the subsequent repair reactions. Our findings also reveal how monoubiquitination in general can induce an alternative protein structure with a new function.
History
DepositionDec 17, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 18, 2020Provider: repository / Type: Initial release
Revision 1.1Apr 22, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / em_admin / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_modification_feature / refine / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _em_admin.last_update / _refine.ls_d_res_high / _refine.ls_d_res_low / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

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  • Deposited structure unit
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  • Superimposition on EM map
  • EMDB-21138
  • Imaged by UCSF Chimera
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Fanconi anemia, complementation group I
B: Fanconi anemia group D2 protein
C: Ubiquitin
D: Ubiquitin
S: DNA (29-MER)
T: DNA (29-MER)


Theoretical massNumber of molelcules
Total (without water)348,8676
Polymers348,8676
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11C
21D

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: VAL / End label comp-ID: VAL / Refine code: 1 / Auth seq-ID: 1 - 70 / Label seq-ID: 1 - 70

Dom-IDAuth asym-IDLabel asym-ID
1CC
2DD

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Components

#1: Protein Fanconi anemia, complementation group I


Mass: 149566.047 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: isopeptide bond between Lys523 Nz and the C-terminus of ubiquitin (chain C)
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCI / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: B7ZMF2, UniProt: Q9NVI1*PLUS
#2: Protein Fanconi anemia group D2 protein / Protein FACD2


Mass: 164314.516 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: isopeptide bond between Lys561 Nz and the C-terminus of ubiquitin (chain D)
Source: (gene. exp.) Homo sapiens (human) / Gene: FANCD2, FACD / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9BXW9
#3: Protein Ubiquitin


Mass: 8576.831 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: isopeptide bond between C-terminus of ubiquitin (chain C) and Lys523 Nz of FANCI (chain A); isopeptide bond between C-terminus of ubiquitin (chain D) and Lys561 Nz of FANCD2 (chain B)
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48
#4: DNA chain DNA (29-MER)


Mass: 8951.746 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#5: DNA chain DNA (29-MER)


Mass: 8880.711 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
Has protein modificationY

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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: Mono-ubiquitinated Fanconi Anemia ID complex bound to DNA
Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Molecular weightUnits: MEGADALTONS / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: unspecified
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: 51 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: REFMAC / Version: 5.8.0257 / Classification: refinement
EM software
IDNameVersionCategory
4CTFFIND4CTF correction
7Omodel fitting
9RELION3initial Euler assignment
13REFMAC5model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 301158 / Symmetry type: POINT
Atomic model buildingB value: 150 / Protocol: OTHER / Space: RECIPROCAL / Target criteria: R-factor
Atomic model buildingPDB-ID: 3S4W

3s4w


Accession code: 3S4W / Source name: PDB / Type: experimental model
RefinementResolution: 3.6→3.6 Å / Cor.coef. Fo:Fc: 0.867 / SU B: 58.88 / SU ML: 0.383 / ESU R: 0.72
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.30174 --
obs0.30174 130228 99.84 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK
Displacement parametersBiso mean: 142.942 Å2
Baniso -1Baniso -2Baniso -3
1--1.09 Å2-1.12 Å2-1.33 Å2
2---1.16 Å21.72 Å2
3---2.26 Å2
Refinement stepCycle: 1 / Total: 21167
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.010.01321719
ELECTRON MICROSCOPYr_bond_other_d0.0070.01720266
ELECTRON MICROSCOPYr_angle_refined_deg1.421.59729474
ELECTRON MICROSCOPYr_angle_other_deg1.5371.61647190
ELECTRON MICROSCOPYr_dihedral_angle_1_deg6.9255.1022791
ELECTRON MICROSCOPYr_dihedral_angle_2_deg35.30323.557967
ELECTRON MICROSCOPYr_dihedral_angle_3_deg16.695153893
ELECTRON MICROSCOPYr_dihedral_angle_4_deg13.4811592
ELECTRON MICROSCOPYr_chiral_restr0.1370.2062927
ELECTRON MICROSCOPYr_gen_planes_refined0.0070.0222651
ELECTRON MICROSCOPYr_gen_planes_other0.0040.024200
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_it2.6310.8599997
ELECTRON MICROSCOPYr_mcbond_other2.6310.8599995
ELECTRON MICROSCOPYr_mcangle_it4.0021.28112456
ELECTRON MICROSCOPYr_mcangle_other4.0021.28112456
ELECTRON MICROSCOPYr_scbond_it3.8051.04211722
ELECTRON MICROSCOPYr_scbond_other3.8051.04211721
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other5.821.46817018
ELECTRON MICROSCOPYr_long_range_B_refined5.22517.95455603
ELECTRON MICROSCOPYr_long_range_B_other5.22517.95455604
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
Refine LS restraints NCSNumber: 1102 / Type: tight thermal / Rms dev position: 0.65 Å / Weight position: 0.5
LS refinement shellResolution: 3.5→3.59 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0 0 -
Rwork0.575 9523 -
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)
10.0761-0.02880.00720.0177-0.00850.0077-0.2141-0.41050.36580.08230.0504-0.26820.06330.03320.16374.03410.4097-0.32734.0097-0.11564.384671.495132.865419.515
20.845-1.23060.75142.2154-1.3240.7977-0.0143-0.8901-0.4185-0.64370.34660.32480.4499-0.3034-0.33233.79490.3116-0.09213.7020.10083.709880.799249.237826.2927
33.4789-1.0060.5396.3650.03795.95670.07830.8303-0.3605-0.77480.2251-0.53070.44310.3847-0.30341.5183-0.04060.06071.6475-0.01051.655377.54274.282734.6444
415.74125.72-1.0411.33521.71042.6834-0.41780.9504-0.8794-0.2438-0.0576-0.18520.6539-0.2920.47540.57620.08580.1120.4542-0.030.644175.981193.855845.7891
56.373-5.1369-5.55688.27724.225.0390.00870.5998-0.23510.0027-0.32470.95020.2578-0.66010.3160.413-0.09520.07290.6007-0.11980.91252.1154111.316657.6379
63.8631.0699-3.271111.41912.11833.82690.93-0.30670.88431.0247-0.71850.6971-0.8615-0.2804-0.21161.15190.18290.24531.2819-0.44221.730752.8662141.417870.41
76.13923.7782-0.85739.57680.757712.36150.1946-0.77931.4111.1226-0.7065-0.9046-0.43460.95730.5121.195-0.10360.40211.0159-0.311.666866.6145.204967.0452
810.8267-0.5241-1.38313.1615-0.16667.70660.15510.46571.2007-0.03010.1969-0.2979-1.02060.4219-0.3520.4720.04070.41560.5517-0.03930.969573.8146138.70151.2827
99.6176-3.6465-0.91138.9038-2.4748.33680.07741.1281.489-0.4693-0.2136-0.3439-0.68650.49750.13620.74130.29090.29060.93130.14751.160593.9151130.269844.8271
107.85541.54151.263812.83622.88838.19270.23711.01890.6072-0.7193-0.1977-0.7703-0.54910.6179-0.03940.3630.13730.20450.52510.25510.8219107.5706111.935550.1202
1112.41443.19052.603417.21655.966614.6614-0.15991.05-0.1713-0.62230.352-0.2545-0.0251.6812-0.19210.25960.10820.07960.40490.25870.6363111.3813100.742254.3892
129.5939-0.04433.44949.79482.009712.73370.144-0.35270.14210.5677-0.3457-1.0272-0.65550.90940.20180.4007-0.09850.00990.29990.41140.8619115.198496.424269.1281
135.81750.13180.05915.03850.77166.3980.0232-0.17640.7240.20170.29131.6345-0.0591-1.9329-0.31441.54560.19420.20182.57020.16762.493422.5242123.639475.7007
148.8345-2.91231.26941.82040.43225.0387-0.1776-1.28150.17751.22880.3120.3084-0.2904-0.5274-0.13442.25970.02850.20171.8344-0.02681.581540.5285114.800590.4686
155.6829-2.3015-1.93544.93661.23855.541-0.1295-1.2354-0.01651.39690.08230.04540.24890.20260.04721.73040.0873-0.3361.6697-0.0621.495655.9242100.755191.1349
165.2748-2.2839-0.023510.19884.34394.31080.1321-0.2364-0.30020.8002-0.0725-0.64730.51730.2014-0.05971.48360.1452-0.37691.08710.12241.661162.741484.77778.1039
171.73060.18160.14776.87682.13612.19290.25390.4152-0.1573-0.2962-0.16470.8060.154-0.1465-0.08931.6050.0542-0.26521.73830.13611.614562.12554.521959.9769
184.6835-1.60720.23156.8482-0.51225.35270.23480.9818-1.5618-0.9548-0.3454-0.30570.95410.35390.11062.1047-0.0994-0.60641.9139-0.25362.159985.680629.1761.8059
199.1889-3.23492.71327.8177-1.5058.95190.1328-0.1078-0.19140.0871-0.2196-0.3497-0.09-0.08210.08681.5017-0.349-0.35751.1176-0.00971.539389.880943.565776.2021
205.8122-0.9271.23026.88391.14566.16410.0754-1.234-0.72941.3815-0.4190.480.3054-0.04960.34361.6896-0.4814-0.17131.37250.14131.425196.809250.222590.3894
217.3307-0.6166-2.1610.9286-1.7769.16010.5143-0.9296-0.34681.0049-0.2517-1.06360.44070.7269-0.26251.0913-0.3427-0.36310.76430.2631.1587113.888967.593184.2295
226.35440.84171.50418.2353.16598.5627-0.0586-1.45130.17931.27850.1677-0.3789-0.24060.8613-0.10911.028-0.051-0.26181.02040.22710.9963114.381688.951684.2705
234.90852.05363.118111.08-1.49414.3433-0.40930.3159-0.09660.10670.32651.06940.7243-0.91290.08281.5634-0.12370.0271.4641-0.06151.689832.348192.928277.2728
246.6006-2.6312-1.48285.7744-0.69212.29790.30181.1221-0.4485-0.80.23651.54220.7834-1.3219-0.53832.1589-0.36-0.26912.3455-0.06252.4654.968269.618431.9393
251.29522.46121.140318.11167.92564.07611.4176-0.32950.1164-0.334-2.3431-0.6564-0.2255-1.04950.92552.26780.0301-0.02282.83220.20592.438590.0603114.824172.038
260.68960.0283-1.32834.08313.10635.8327-0.25251.0721-0.12341.8947-0.1502-1.18861.5611-1.630.40272.6571-0.1543-0.23742.97470.32252.7741101.405771.169458.9507
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1ELECTRON MICROSCOPY1A1 - 81
2ELECTRON MICROSCOPY2A82 - 169
3ELECTRON MICROSCOPY3A170 - 305
4ELECTRON MICROSCOPY4A306 - 399
5ELECTRON MICROSCOPY5A408 - 617
6ELECTRON MICROSCOPY6A618 - 743
7ELECTRON MICROSCOPY7A744 - 800
8ELECTRON MICROSCOPY8A801 - 934
9ELECTRON MICROSCOPY9A949 - 1039
10ELECTRON MICROSCOPY10A1040 - 1154
11ELECTRON MICROSCOPY11A1155 - 1221
12ELECTRON MICROSCOPY12A1233 - 1297
13ELECTRON MICROSCOPY12B1339 - 1400
14ELECTRON MICROSCOPY13B45 - 187
15ELECTRON MICROSCOPY14B188 - 254
16ELECTRON MICROSCOPY15B255 - 311
17ELECTRON MICROSCOPY16B337 - 465
18ELECTRON MICROSCOPY17B466 - 645
19ELECTRON MICROSCOPY18B646 - 841
20ELECTRON MICROSCOPY19B916 - 1020
21ELECTRON MICROSCOPY20B1021 - 1145
22ELECTRON MICROSCOPY21B1150 - 1250
23ELECTRON MICROSCOPY22B1251 - 1338
24ELECTRON MICROSCOPY23C1 - 76
25ELECTRON MICROSCOPY24D1 - 76
26ELECTRON MICROSCOPY25S1 - 18
27ELECTRON MICROSCOPY25T41 - 58
28ELECTRON MICROSCOPY26T30 - 40
29ELECTRON MICROSCOPY26S19 - 29

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