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- PDB-6bcu: Cryo-EM structure of the activated RHEB-mTORC1 refined to 3.4 angstrom -

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Basic information

Entry
Database: PDB / ID: 6bcu
TitleCryo-EM structure of the activated RHEB-mTORC1 refined to 3.4 angstrom
Components
  • Eukaryotic translation initiation factor 4E-binding protein 1
  • GTP-binding protein Rheb
  • Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR
  • Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR
  • Target of rapamycin complex subunit LST8MTOR
KeywordsTRANSFERASE / PIKK
Function / homology
Function and homology information


regulation of type B pancreatic cell development / RNA polymerase III type 2 promoter sequence-specific DNA binding / positive regulation of cytoplasmic translational initiation / RNA polymerase III type 1 promoter sequence-specific DNA binding / positive regulation of pentose-phosphate shunt / T-helper 1 cell lineage commitment / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / cellular response to leucine starvation ...regulation of type B pancreatic cell development / RNA polymerase III type 2 promoter sequence-specific DNA binding / positive regulation of cytoplasmic translational initiation / RNA polymerase III type 1 promoter sequence-specific DNA binding / positive regulation of pentose-phosphate shunt / T-helper 1 cell lineage commitment / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / cellular response to leucine starvation / eukaryotic initiation factor 4E binding / TFIIIC-class transcription factor complex binding / TORC2 complex / heart valve morphogenesis / regulation of membrane permeability / negative regulation of lysosome organization / RNA polymerase III type 3 promoter sequence-specific DNA binding / TORC1 complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / calcineurin-NFAT signaling cascade / regulation of autophagosome assembly / TORC1 signaling / positive regulation of odontoblast differentiation / voluntary musculoskeletal movement / regulation of osteoclast differentiation / positive regulation of keratinocyte migration / cellular response to L-leucine / MTOR signalling / Amino acids regulate mTORC1 / cellular response to nutrient / energy reserve metabolic process / Energy dependent regulation of mTOR by LKB1-AMPK / nucleus localization / ruffle organization / protein serine/threonine kinase inhibitor activity / negative regulation of cell size / cellular response to osmotic stress / positive regulation of osteoclast differentiation / enzyme-substrate adaptor activity / anoikis / cardiac muscle cell development / negative regulation of cold-induced thermogenesis / positive regulation of transcription by RNA polymerase III / negative regulation of protein localization to nucleus / regulation of myelination / negative regulation of calcineurin-NFAT signaling cascade / Macroautophagy / regulation of cell size / negative regulation of macroautophagy / lysosome organization / small GTPase-mediated signal transduction / positive regulation of oligodendrocyte differentiation / positive regulation of actin filament polymerization / protein kinase activator activity / positive regulation of myotube differentiation / behavioral response to pain / TOR signaling / oligodendrocyte differentiation / mTORC1-mediated signalling / germ cell development / Constitutive Signaling by AKT1 E17K in Cancer / social behavior / cellular response to nutrient levels / CD28 dependent PI3K/Akt signaling / positive regulation of phosphoprotein phosphatase activity / positive regulation of translational initiation / neuronal action potential / HSF1-dependent transactivation / positive regulation of TOR signaling / positive regulation of G1/S transition of mitotic cell cycle / positive regulation of epithelial to mesenchymal transition / regulation of macroautophagy / endomembrane system / 'de novo' pyrimidine nucleobase biosynthetic process / response to amino acid / positive regulation of lipid biosynthetic process / phagocytic vesicle / positive regulation of lamellipodium assembly / translation initiation factor binding / heart morphogenesis / regulation of cellular response to heat / cytoskeleton organization / negative regulation of translational initiation / translation repressor activity / cardiac muscle contraction / positive regulation of stress fiber assembly / positive regulation of TORC1 signaling / cellular response to amino acid starvation / T cell costimulation / cellular response to starvation / positive regulation of endothelial cell proliferation / positive regulation of glycolytic process / protein serine/threonine kinase activator activity / positive regulation of mitotic cell cycle / response to nutrient levels / post-embryonic development / response to nutrient / negative regulation of autophagy / positive regulation of translation / 14-3-3 protein binding
Similarity search - Function
Eukaryotic translation initiation factor 4E binding / Eukaryotic translation initiation factor 4E binding protein (EIF4EBP) / Raptor, N-terminal CASPase-like domain / Raptor N-terminal CASPase like domain / Raptor N-terminal CASPase like domain / Regulatory associated protein of TOR / Target of rapamycin complex subunit LST8 / Domain of unknown function DUF3385, target of rapamycin protein / Domain of unknown function (DUF3385) / Domain of unknown function ...Eukaryotic translation initiation factor 4E binding / Eukaryotic translation initiation factor 4E binding protein (EIF4EBP) / Raptor, N-terminal CASPase-like domain / Raptor N-terminal CASPase like domain / Raptor N-terminal CASPase like domain / Regulatory associated protein of TOR / Target of rapamycin complex subunit LST8 / Domain of unknown function DUF3385, target of rapamycin protein / Domain of unknown function (DUF3385) / Domain of unknown function / FKBP12-rapamycin binding domain / Serine/threonine-protein kinase TOR / FKBP12-rapamycin binding domain superfamily / FKBP12-rapamycin binding domain / HEAT repeat / HEAT repeat / Rapamycin binding domain / PIK-related kinase, FAT / FAT domain / FATC domain / FATC / FATC domain / PIK-related kinase / FAT domain profile. / FATC domain profile. / Quinoprotein alcohol dehydrogenase-like superfamily / Phosphatidylinositol 3- and 4-kinases signature 1. / Small GTPase, Ras-type / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / small GTPase Ras family profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Tetratricopeptide-like helical domain superfamily / Small GTP-binding protein domain / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Serine/threonine-protein kinase mTOR / Eukaryotic translation initiation factor 4E-binding protein 1 / GTP-binding protein Rheb / Regulatory-associated protein of mTOR / Target of rapamycin complex subunit LST8
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsPavletich, N.P. / Yang, H.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nature / Year: 2017
Title: Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40.
Authors: Haijuan Yang / Xiaolu Jiang / Buren Li / Hyo J Yang / Meredith Miller / Angela Yang / Ankita Dhar / Nikola P Pavletich /
Abstract: The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to nutrients, energy levels, and growth factors. It contains the atypical kinase mTOR and the ...The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to nutrients, energy levels, and growth factors. It contains the atypical kinase mTOR and the RAPTOR subunit that binds to the Tor signalling sequence (TOS) motif of substrates and regulators. mTORC1 is activated by the small GTPase RHEB (Ras homologue enriched in brain) and inhibited by PRAS40. Here we present the 3.0 ångström cryo-electron microscopy structure of mTORC1 and the 3.4 ångström structure of activated RHEB-mTORC1. RHEB binds to mTOR distally from the kinase active site, yet causes a global conformational change that allosterically realigns active-site residues, accelerating catalysis. Cancer-associated hyperactivating mutations map to structural elements that maintain the inactive state, and we provide biochemical evidence that they mimic RHEB relieving auto-inhibition. We also present crystal structures of RAPTOR-TOS motif complexes that define the determinants of TOS recognition, of an mTOR FKBP12-rapamycin-binding (FRB) domain-substrate complex that establishes a second substrate-recruitment mechanism, and of a truncated mTOR-PRAS40 complex that reveals PRAS40 inhibits both substrate-recruitment sites. These findings help explain how mTORC1 selects its substrates, how its kinase activity is controlled, and how it is activated by cancer-associated mutations.
History
DepositionOct 20, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 20, 2017Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2018Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Jan 24, 2018Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _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 1.3Oct 3, 2018Group: Data collection / Refinement description / Category: refine
Revision 1.4Nov 20, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Mar 13, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / refine / struct_conn
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 / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id

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Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
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  • Superimposition on EM map
  • EMDB-7086
  • Imaged by UCSF Chimera
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR
D: Target of rapamycin complex subunit LST8
W: Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR
X: Eukaryotic translation initiation factor 4E-binding protein 1
S: GTP-binding protein Rheb
B: Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR
E: Target of rapamycin complex subunit LST8
Y: Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR
Z: Eukaryotic translation initiation factor 4E-binding protein 1
R: GTP-binding protein Rheb
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,016,87720
Polymers1,014,67110
Non-polymers2,20710
Water0
1


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

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Components

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Protein , 5 types, 10 molecules ABDEWYXZSR

#1: Protein Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR / FK506-binding protein 12-rapamycin complex-associated protein 1 / FKBP12-rapamycin complex- ...FK506-binding protein 12-rapamycin complex-associated protein 1 / FKBP12-rapamycin complex-associated protein / Mammalian target of rapamycin


Mass: 287399.125 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1 / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
References: UniProt: P42345, non-specific serine/threonine protein kinase
#2: Protein Target of rapamycin complex subunit LST8 / MTOR / TORC subunit LST8 / G protein beta subunit-like / Protein GbetaL / Mammalian lethal with SEC13 ...TORC subunit LST8 / G protein beta subunit-like / Protein GbetaL / Mammalian lethal with SEC13 protein 8 / mLST8


Mass: 35910.090 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MLST8, GBL, LST8 / Production host: Homo sapiens (human) / References: UniProt: Q9BVC4
#3: Protein Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR / Raptor / p150 target of rapamycin (TOR)-scaffold protein


Mass: 150197.000 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RPTOR, KIAA1303, RAPTOR / Production host: Homo sapiens (human) / References: UniProt: Q8N122
#4: Protein Eukaryotic translation initiation factor 4E-binding protein 1 / eIF4E-binding protein 1 / Phosphorylated heat- and acid-stable protein regulated by insulin 1 / PHAS-I


Mass: 12951.344 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF4EBP1 / Production host: Homo sapiens (human) / References: UniProt: Q13541
#5: Protein GTP-binding protein Rheb / Ras homolog enriched in brain


Mass: 20877.826 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RHEB, RHEB2 / Production host: Homo sapiens (human) / References: UniProt: Q15382

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Non-polymers , 3 types, 10 molecules

#6: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine triphosphate


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM

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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: active complex / Type: COMPLEX / Entity ID: #1-#5 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding 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 FIELDBright-field microscopy
Image recordingElectron dose: 56 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: REFMAC / Version: 5.8.0158 / Classification: refinement
EM software
IDNameVersionCategory
9REFMACmodel refinement
13RELION23D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 198237 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL
RefinementResolution: 3.8→3.8 Å / Cor.coef. Fo:Fc: 0.869 / SU B: 44.652 / SU ML: 0.268 / ESU R: 0.473
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.32438 --
obs0.32438 568359 100 %
Solvent computationIon probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.812 Å2
Baniso -1Baniso -2Baniso -3
1--1.5 Å2-2.13 Å2-0.53 Å2
2--0.63 Å2-0.37 Å2
3---0.87 Å2
Refinement stepCycle: 1 / Total: 59662
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0110.01960942
ELECTRON MICROSCOPYr_bond_other_d0.0020.0257194
ELECTRON MICROSCOPYr_angle_refined_deg1.5751.95882676
ELECTRON MICROSCOPYr_angle_other_deg1.1953132344
ELECTRON MICROSCOPYr_dihedral_angle_1_deg8.31457444
ELECTRON MICROSCOPYr_dihedral_angle_2_deg37.64723.8072758
ELECTRON MICROSCOPYr_dihedral_angle_3_deg16.6491510624
ELECTRON MICROSCOPYr_dihedral_angle_4_deg15.44515436
ELECTRON MICROSCOPYr_chiral_restr0.0880.29378
ELECTRON MICROSCOPYr_gen_planes_refined0.0060.02166922
ELECTRON MICROSCOPYr_gen_planes_other0.0020.0212376
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_it3.5381.99729926
ELECTRON MICROSCOPYr_mcbond_other3.5371.99729925
ELECTRON MICROSCOPYr_mcangle_it6.2513.98837320
ELECTRON MICROSCOPYr_mcangle_other6.2513.98837321
ELECTRON MICROSCOPYr_scbond_it4.1032.20131016
ELECTRON MICROSCOPYr_scbond_other4.1042.20131003
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other7.324.29945337
ELECTRON MICROSCOPYr_long_range_B_refined10.98978.465132281
ELECTRON MICROSCOPYr_long_range_B_other10.98978.465132279
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 3.43→3.519 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rwork0.741 42011 -
Rfree-0 -
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)
15.93730.15371.08642.6699-0.3123.24280.13250.36980.355-0.3247-0.2679-0.1493-0.10540.29620.13541.34120.25860.04961.2413-0.07120.749146.9129158.456127.2824
25.68490.3073-1.05362.73910.32223.03220.11510.3663-0.3377-0.3278-0.27780.17410.1252-0.34250.16261.32810.242-0.03061.25090.08660.765145.573775.495127.278
33.6538-0.9389-2.80020.44450.93892.39850.0841-0.01291.0731-0.1484-0.03430.31340.0095-0.06-0.04982.09220.25750.11912.11840.23082.3075170.488798.746127.843
47.5742-0.21641.90641.8916-1.61382.7324-0.04770.36670.3762-0.03270.39330.4034-0.07110.2981-0.34571.26140.45470.18311.40820.19210.8548172.531778.857828.7773
56.856-0.0143-3.61246.9333.05053.3321-0.08890.4339-0.90510.2987-0.0922-0.21690.3849-0.43510.1811.34170.284-0.07241.51520.22850.88186.672463.964928.715
67.07925.1268-1.12725.09540.08810.7842-0.1439-0.4491-0.35070.03370.2163-0.5930.09920.3234-0.07251.53680.2174-0.32351.37570.08881.175208.866572.071724.6017
76.2437-2.5258-1.60589.39491.7282.09190.1684-0.3460.03150.2106-0.173-0.61360.36090.38750.00461.06020.1932-0.24561.1265-0.06730.6386213.7838101.289233.3375
85.85970.4463-2.49153.46540.60886.48310.01260.2139-0.5552-0.23260.11740.05110.70410.076-0.130.54450.106-0.06910.2967-0.00480.3941191.1799117.957454.2716
93.61952.1447-0.75779.4413-4.87725.9417-0.2043-0.1144-0.24440.03790.01990.51630.6846-0.76650.18440.99650.1532-0.0310.7233-0.08330.76174.274397.43869.0758
106.1446-3.44962.594611.56270.45184.8709-0.2513-0.04130.2862-0.16940.0644-0.31420.41660.43980.18680.8830.2610.13751.00310.08640.5083146.159581.835957.8133
116.1142-2.66432.30413.731-1.28663.98980.16910.747-0.019-0.4782-0.20040.038-0.01450.37240.03130.71370.19930.07130.63210.06360.3316116.817799.010642.5378
127.394-4.05762.35795.5695-3.04835.97420.68221.2381-0.2505-0.6696-0.4627-0.07490.71980.7431-0.21941.02280.68230.24180.9890.11940.2818163.162564.758254.8258
133.34080.01430.05217.28351.14134.0928-0.0043-0.2750.23530.2613-0.10490.08350.43410.04060.10920.36150.25080.05010.22180.01120.0243156.825963.629296.5528
140.181-0.68910.17494.6313-0.74240.24880.06970.0671-0.22810.19230.0802-0.69020.3338-0.1619-0.14991.76060.1164-0.06991.74050.06111.6888196.54864.414177.28
154.2445-0.2463-0.00263.6941.0157.7026-0.10460.1499-0.1631-0.47930.08010.01090.35790.23840.02451.00360.54230.06070.75280.050.248189.542986.225676.8836
168.7944-1.0513-0.35292.16320.83732.53920.0333-0.84910.13640.1162-0.19830.17410.24650.46930.1650.80330.33570.04770.45320.04210.2624171.445790.6917114.9921
1711.39181.8914-0.5278.4865-0.2448.17180.12890.76830.9284-0.4846-0.23330.756-0.3825-0.86820.10440.39180.3136-0.17610.3314-0.10940.3693135.152788.028795.5483
183.71871.6894-3.65272.4377-0.96174.9605-0.3433-0.6751-0.62410.6438-0.53020.98760.9869-0.63640.87361.3279-0.00770.03611.6613-0.00681.5256115.560870.6637108.7933
196.19381.0194-0.02917.2308-1.40096.0456-0.0124-0.7137-0.6130.76530.0365-0.04460.8108-0.1356-0.02411.28310.22220.13420.8742-0.2050.4651150.064228.5075111.4896
205.648-1.5882-0.34357.4252-0.54045.07860.00240.196-0.6842-0.1039-0.0071-0.07120.76060.21440.00470.44990.2980.09560.22550.05120.124106.133272.292166.5201
219.11771.86891.30279.38541.36039.9255-0.0158-0.67670.46290.58410.0836-0.5453-0.81850.3179-0.06790.33750.18910.03410.27290.01640.0929100.843696.477671.227
2213.28572.6444-0.10436.7827-0.95752.773-0.0202-0.053-0.4559-0.0058-0.24610.16780.4696-0.61090.26630.37940.19770.01830.5049-0.09290.183177.242995.898167.7659
2310.4098-0.39661.2435.0529-0.34264.6825-0.022-0.2391-0.59380.01520.14310.37710.3276-0.5483-0.12110.69090.205-0.08460.7171-0.01790.581151.733693.307670.8833
241.92761.4852-0.10176.0838-2.81184.4344-0.21280.1684-1.4941-0.44220.0324-0.01331.3285-1.09760.18041.7058-0.0401-0.08291.6321-0.30341.879434.121285.360658.3115
255.7132-0.73730.31744.65040.23242.9758-0.20060.80780.6575-0.57690.08770.4829-0.4227-0.35760.11292.04350.37240.03111.77340.29011.112734.2452118.628340.517
264.9085-0.59383.30870.4149-0.6912.48750.1432-0.1333-1.3454-0.24980.0108-0.56780.0956-0.0067-0.1542.14010.3044-0.10222.1397-0.26162.2029122.0209135.23127.839
277.95870.0006-2.18861.11211.57563.62480.00580.3427-0.3878-0.05890.3394-0.35740.102-0.3774-0.34521.28410.4578-0.13531.4065-0.17620.8705119.9685155.118928.7687
287.6938-0.23613.79996.7051-3.07933.2407-0.15160.47710.93460.3792-0.04560.1938-0.3130.44560.19721.30880.27960.10091.5208-0.22080.8945105.8197170.004528.7051
297.03244.96391.15824.7565-0.0420.8058-0.1386-0.41510.3319-0.00610.22090.587-0.0515-0.2748-0.08231.50360.21320.3221.3523-0.04851.154483.6289161.885324.5977
306.4512-2.56781.35249.2824-1.70512.03910.2028-0.3325-0.03120.1642-0.17480.642-0.3655-0.4454-0.0281.05130.16320.27871.12650.09210.632278.7292132.668333.3419
316.40270.53512.79353.5479-0.52056.6097-0.00170.18930.5921-0.24190.094-0.059-0.6939-0.0936-0.09230.54620.10450.13480.2920.05290.3796101.3492116.02154.2757
323.90332.14190.56679.17624.6526.348-0.2229-0.11560.236-0.0008-0.0135-0.4917-0.73690.73410.23640.99430.16430.06040.72110.1090.7547118.2443136.550569.072
335.7594-3.2315-2.949211.1408-0.28675.2777-0.2394-0.0761-0.2692-0.16580.05910.2668-0.3595-0.40060.18030.86740.2579-0.10620.9975-0.04960.5356146.3555152.140657.817
345.7893-2.582-2.24753.69561.24263.92050.13780.6985-0.0074-0.4513-0.1645-0.02630.0491-0.34180.02670.70660.202-0.00490.6419-0.02430.3388175.7074134.972942.5397
355.8107-2.9529-1.30264.66821.73084.43240.41140.89860.2891-0.5041-0.22460.1057-0.4386-0.5083-0.18680.91790.5149-0.12270.9228-0.07310.3285129.3553169.228354.8256
363.28070.0682-0.14527.2334-1.19574.0829-0.0067-0.2732-0.2280.2735-0.1046-0.0671-0.4316-0.03460.11130.36640.25220.00620.22050.03170.0194135.7025170.364896.5504
370.2179-0.8171-0.19814.76330.72210.2380.08810.03380.2130.15830.08450.7086-0.32550.1514-0.17251.75280.13640.08691.764-0.02141.698495.972169.566377.2851
384.2681-0.2627-0.04673.8025-0.9087.5143-0.10660.11810.152-0.50840.0693-0.0305-0.3181-0.23770.03731.01050.5398-0.01140.744-0.01910.2634102.9824147.757176.8885
398.5657-1.05680.38712.2012-0.82532.45150.046-0.8344-0.12250.123-0.2133-0.1646-0.1913-0.44790.16730.79150.32620.00340.4574-0.00120.2715121.0883143.2982114.9945
4011.42281.93290.77228.81680.16898.09360.13910.7866-0.9571-0.4778-0.2359-0.71840.37350.86870.09680.39430.3240.24640.34260.14560.3518157.3788145.967995.5435
413.99891.55433.51822.74610.57314.0146-0.3775-0.66970.71820.5852-0.579-1.0901-0.93250.43240.95651.3494-0.04420.05831.66690.07841.4669176.9663163.3353108.7844
426.20551.00640.02627.34871.48696.1269-0.0394-0.68610.5920.76980.03150.0563-0.79360.16080.00791.28330.2227-0.09180.87050.2480.4572142.4369205.4549111.4825
435.5958-1.61070.3027.33890.61725.0074-0.02650.18830.6804-0.09680.01220.0766-0.7657-0.21940.01430.44970.2954-0.05960.2308-0.02630.1118186.41161.719366.5228
449.06852.0603-1.26179.2605-1.37449.8203-0.025-0.6707-0.45580.54940.06540.53440.8369-0.3135-0.04040.34120.18170.01840.26450.01590.098191.6858137.532571.2367
4513.14332.70210.10387.04010.98823.0929-0.0035-0.06330.4461-0.0136-0.2638-0.1547-0.5010.59530.26730.37490.20990.02660.50170.12240.183215.2852138.09467.7683
4610.5267-0.5235-1.09975.03970.45475.0409-0.0493-0.22430.5939-0.0180.1402-0.3969-0.30680.5424-0.09090.69360.21060.11510.72140.03460.5622240.7947140.665270.8771
471.89681.72160.41476.3332.51433.847-0.27060.17061.4117-0.3871-0.02150.0232-1.31771.05960.29211.6784-0.02440.0941.64210.2931.7883258.4069148.592258.2965
485.5552-0.6272-0.34214.4542-0.17352.8552-0.23390.7904-0.6863-0.52040.1371-0.47060.42190.29590.09692.07950.3907-0.0071.7712-0.27281.141258.2524115.316740.516
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1ELECTRON MICROSCOPY1R4 - 202
2ELECTRON MICROSCOPY2S4 - 202
3ELECTRON MICROSCOPY3A17 - 100
4ELECTRON MICROSCOPY4A101 - 186
5ELECTRON MICROSCOPY5A187 - 275
6ELECTRON MICROSCOPY6A276 - 490
7ELECTRON MICROSCOPY7A497 - 633
8ELECTRON MICROSCOPY8A644 - 786
9ELECTRON MICROSCOPY9A791 - 903
10ELECTRON MICROSCOPY10A933 - 1005
11ELECTRON MICROSCOPY11A1006 - 1222
12ELECTRON MICROSCOPY12A1261 - 1391
13ELECTRON MICROSCOPY13A2241 - 3002
14ELECTRON MICROSCOPY13A2192 - 2228
15ELECTRON MICROSCOPY13A1392 - 1442
16ELECTRON MICROSCOPY14A1443 - 1537
17ELECTRON MICROSCOPY15A1538 - 1677
18ELECTRON MICROSCOPY16A1678 - 2001
19ELECTRON MICROSCOPY17A2002 - 2021
20ELECTRON MICROSCOPY17A2119 - 2191
21ELECTRON MICROSCOPY17A2229 - 2240
22ELECTRON MICROSCOPY18A2022 - 2118
23ELECTRON MICROSCOPY19D8 - 324
24ELECTRON MICROSCOPY20W54 - 270
25ELECTRON MICROSCOPY20W341 - 371
26ELECTRON MICROSCOPY21W271 - 340
27ELECTRON MICROSCOPY21W372 - 406
28ELECTRON MICROSCOPY22W45 - 53
29ELECTRON MICROSCOPY22W407 - 512
30ELECTRON MICROSCOPY22X111 - 118
31ELECTRON MICROSCOPY23W39 - 44
32ELECTRON MICROSCOPY23W513 - 631
33ELECTRON MICROSCOPY23W958 - 970
34ELECTRON MICROSCOPY24W632 - 840
35ELECTRON MICROSCOPY24W950 - 957
36ELECTRON MICROSCOPY25W18 - 38
37ELECTRON MICROSCOPY25W971 - 1331
38ELECTRON MICROSCOPY26B17 - 100
39ELECTRON MICROSCOPY27B101 - 186
40ELECTRON MICROSCOPY28B187 - 275
41ELECTRON MICROSCOPY29B276 - 490
42ELECTRON MICROSCOPY30B497 - 633
43ELECTRON MICROSCOPY31B644 - 786
44ELECTRON MICROSCOPY32B791 - 903
45ELECTRON MICROSCOPY33B933 - 1005
46ELECTRON MICROSCOPY34B1006 - 1222
47ELECTRON MICROSCOPY35B1261 - 1391
48ELECTRON MICROSCOPY36B2241 - 3002
49ELECTRON MICROSCOPY36B2192 - 2228
50ELECTRON MICROSCOPY36B1392 - 1442
51ELECTRON MICROSCOPY37B1443 - 1537
52ELECTRON MICROSCOPY38B1538 - 1677
53ELECTRON MICROSCOPY39B1678 - 2001
54ELECTRON MICROSCOPY40B2002 - 2021
55ELECTRON MICROSCOPY40B2119 - 2191
56ELECTRON MICROSCOPY40B2229 - 2240
57ELECTRON MICROSCOPY41B2022 - 2118
58ELECTRON MICROSCOPY42E8 - 324
59ELECTRON MICROSCOPY43Y54 - 270
60ELECTRON MICROSCOPY43Y341 - 371
61ELECTRON MICROSCOPY44Y271 - 340
62ELECTRON MICROSCOPY44Y372 - 406
63ELECTRON MICROSCOPY45Y45 - 53
64ELECTRON MICROSCOPY45Y407 - 512
65ELECTRON MICROSCOPY45Z111 - 118
66ELECTRON MICROSCOPY46Y39 - 44
67ELECTRON MICROSCOPY46Y513 - 631
68ELECTRON MICROSCOPY46Y958 - 970
69ELECTRON MICROSCOPY47Y632 - 840
70ELECTRON MICROSCOPY47Y950 - 957
71ELECTRON MICROSCOPY48Y18 - 38
72ELECTRON MICROSCOPY48Y971 - 1331

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