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- PDB-6bcx: mTORC1 structure refined to 3.0 angstroms -

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Basic information

Entry
Database: PDB / ID: 6bcx
TitlemTORC1 structure refined to 3.0 angstroms
Components
  • Eukaryotic translation initiation factor 4E-binding protein 1
  • Regulatory-associated protein of mTOR
  • Serine/threonine-protein kinase mTOR
  • Target of rapamycin complex subunit LST8
KeywordsTRANSFERASE / PIKK
Function / homology
Function and homology information


RNA polymerase III type 2 promoter sequence-specific DNA binding / RNA polymerase III type 1 promoter sequence-specific DNA binding / positive regulation of cytoplasmic translational initiation / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / T-helper 1 cell lineage commitment / positive regulation of pentose-phosphate shunt / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / eukaryotic initiation factor 4E binding / TORC2 complex ...RNA polymerase III type 2 promoter sequence-specific DNA binding / RNA polymerase III type 1 promoter sequence-specific DNA binding / positive regulation of cytoplasmic translational initiation / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / T-helper 1 cell lineage commitment / positive regulation of pentose-phosphate shunt / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / eukaryotic initiation factor 4E binding / TORC2 complex / cellular response to leucine starvation / TFIIIC-class transcription factor complex binding / regulation of membrane permeability / heart valve morphogenesis / negative regulation of lysosome organization / nucleus localization / 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 osteoclast differentiation / voluntary musculoskeletal movement / TORC1 signaling / positive regulation of odontoblast differentiation / positive regulation of keratinocyte migration / cellular response to L-leucine / Amino acids regulate mTORC1 / MTOR signalling / cellular response to nutrient / cellular response to methionine / Energy dependent regulation of mTOR by LKB1-AMPK / regulation of autophagosome assembly / energy reserve metabolic process / negative regulation of cell size / ruffle organization / cellular response to osmotic stress / positive regulation of osteoclast differentiation / protein serine/threonine kinase inhibitor activity / enzyme-substrate adaptor activity / anoikis / cardiac muscle cell development / negative regulation of protein localization to nucleus / positive regulation of transcription by RNA polymerase III / negative regulation of calcineurin-NFAT signaling cascade / regulation of myelination / regulation of cell size / negative regulation of macroautophagy / positive regulation of oligodendrocyte differentiation / positive regulation of actin filament polymerization / lysosome organization / Macroautophagy / positive regulation of myotube differentiation / protein kinase activator activity / oligodendrocyte differentiation / Constitutive Signaling by AKT1 E17K in Cancer / mTORC1-mediated signalling / germ cell development / behavioral response to pain / : / CD28 dependent PI3K/Akt signaling / social behavior / HSF1-dependent transactivation / positive regulation of TOR signaling / neuronal action potential / response to amino acid / TOR signaling / 'de novo' pyrimidine nucleobase biosynthetic process / regulation of macroautophagy / positive regulation of G1/S transition of mitotic cell cycle / positive regulation of translational initiation / cellular response to nutrient levels / endomembrane system / positive regulation of lamellipodium assembly / phosphorylation / positive regulation of lipid biosynthetic process / phagocytic vesicle / positive regulation of epithelial to mesenchymal transition / heart morphogenesis / cardiac muscle contraction / regulation of cellular response to heat / translation repressor activity / positive regulation of stress fiber assembly / 14-3-3 protein binding / negative regulation of translational initiation / cytoskeleton organization / positive regulation of endothelial cell proliferation / T cell costimulation / translation initiation factor binding / cellular response to amino acid starvation / positive regulation of glycolytic process / positive regulation of mitotic cell cycle / cellular response to starvation / protein serine/threonine kinase activator activity / negative regulation of autophagy / response to nutrient / response to nutrient levels / post-embryonic development / VEGFR2 mediated vascular permeability / regulation of signal transduction by p53 class mediator / positive regulation of peptidyl-threonine phosphorylation
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 / Serine/threonine-protein kinase mTOR domain / 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 / Serine/threonine-protein kinase mTOR domain / Domain of unknown function / FKBP12-rapamycin binding domain / Serine/threonine-protein kinase TOR / FKBP12-rapamycin binding domain superfamily / FKBP12-rapamycin binding domain / Rapamycin binding domain / HEAT repeat / HEAT repeat / : / FATC domain / PIK-related kinase, FAT / FAT 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. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / 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 / Armadillo-like helical / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase-like domain superfamily
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Serine/threonine-protein kinase mTOR / Eukaryotic translation initiation factor 4E-binding protein 1 / 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: 3.23 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 1.1Dec 27, 2017Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 10, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 17, 2018Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 3, 2018Group: Data collection / Refinement description / Category: refine
Revision 1.5Nov 20, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Mar 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
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  • Superimposition on EM map
  • EMDB-7087
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)974,02714
Polymers972,9158
Non-polymers1,1126
Water00
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 , 4 types, 8 molecules ABDEWYXZ

#1: Protein 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 / mTOR


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 / Production host: Homo sapiens (human)
References: UniProt: P42345, non-specific serine/threonine protein kinase
#2: Protein Target of rapamycin complex subunit LST8 / 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 / Fragment: mLST8
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 / 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

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Non-polymers , 2 types, 6 molecules

#5: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


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


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg

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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: Dimer of two mTOR-mLST8-RAPTOR-4EBP1 complexes. / Type: COMPLEX / Entity ID: #1-#4 / 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 FIELD
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: 3.23 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 580768 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL
RefinementResolution: 3.23→3.23 Å / Cor.coef. Fo:Fc: 0.859 / SU B: 23.164 / SU ML: 0.172 / ESU R: 0.272
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.31946 --
obs0.31946 926567 100 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 31.329 Å2
Baniso -1Baniso -2Baniso -3
1--0.68 Å2-0.45 Å2-0.09 Å2
2--1.79 Å2-0.09 Å2
3----1.11 Å2
Refinement stepCycle: 1 / Total: 56580
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0080.01957784
ELECTRON MICROSCOPYr_bond_other_d0.0010.0254296
ELECTRON MICROSCOPYr_angle_refined_deg1.191.95678396
ELECTRON MICROSCOPYr_angle_other_deg0.913125572
ELECTRON MICROSCOPYr_dihedral_angle_1_deg6.01757054
ELECTRON MICROSCOPYr_dihedral_angle_2_deg34.52723.7252620
ELECTRON MICROSCOPYr_dihedral_angle_3_deg15.2121510062
ELECTRON MICROSCOPYr_dihedral_angle_4_deg13.01715424
ELECTRON MICROSCOPYr_chiral_restr0.0670.28906
ELECTRON MICROSCOPYr_gen_planes_refined0.0050.02163450
ELECTRON MICROSCOPYr_gen_planes_other0.0010.0211780
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_it6.0963.02128384
ELECTRON MICROSCOPYr_mcbond_other6.0963.02128383
ELECTRON MICROSCOPYr_mcangle_it9.6314.535382
ELECTRON MICROSCOPYr_mcangle_other9.6314.535383
ELECTRON MICROSCOPYr_scbond_it8.0833.3829400
ELECTRON MICROSCOPYr_scbond_other8.0833.3829401
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other12.3924.83543015
ELECTRON MICROSCOPYr_long_range_B_refined16.01737.71564130
ELECTRON MICROSCOPYr_long_range_B_other16.01737.71564131
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 3→3.078 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rwork0.859 68685 -
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)
10.14370.06730.69970.04740.37433.65150.109-0.06020.01460.03360.13550.01550.64750.1998-0.24451.57070.00220.0571.5328-0.01421.5845190.6454102.386224.9193
20.04980.00930.00650.0020.00090.00640.0781-0.22520.23780.0169-0.0850.02840.12660.01320.00692.64390.0340.10942.59220.10492.2615191.974382.599725.9233
30.54670.87840.46811.44610.76380.4048-0.0071-0.17090.19730.0585-0.07630.13150.0184-0.07920.08342.67590.00190.03252.6078-0.0382.3013206.709467.654524.4136
40.0140.0007-0.00230.00020.00130.0125-0.0163-0.0127-0.17260.0190.0044-0.01070.1742-0.00190.01192.4439-0.0913-0.02432.0754-0.01122.1623228.448974.886726.1057
58.3137-2.7812-1.6646.47530.32093.39940.02120.2752-0.9799-0.2886-0.3156-0.5920.85570.56520.29441.1890.2235-0.17751.3021-0.06480.826231.962103.079437.1766
65.74960.1823-1.71742.57770.47074.92180.2098-0.2194-0.3726-0.1411-0.0491-0.13690.39170.4543-0.16070.26070.1287-0.0510.10190.02060.1336207.1914119.355955.359
73.71933.26670.05349.6461-4.12244.09020.327-0.03880.1433-0.0927-0.25710.25830.5408-0.4564-0.06990.42860.1283-0.13330.5178-0.17930.2298187.510898.755666.0723
84.3198-3.78531.92466.44480.71752.8347-0.11850.20450.13570.08110.1942-0.62590.09160.3592-0.07570.73070.1270.10250.5980.08390.7744148.553180.311154.2979
97.4541-1.66162.48482.9982-1.00163.1628-0.00760.1361-0.1645-0.1534-0.10360.17040.1775-0.01750.11120.33510.09190.03080.0389-0.03720.2516117.183196.831942.5227
105.797-2.42121.4492.9626-0.65793.53910.27411.1361-0.2754-0.53630.0151-0.0770.17060.3894-0.28920.69150.08670.06440.56550.02870.5485165.198863.287250.2806
111.6557-0.06360.05143.66980.62373.03090.052-0.23930.00050.09940.01110.07120.1921-0.0186-0.06320.12410.1233-0.0440.2183-0.02060.0518165.38964.281592.7885
127.29544.70750.2256.4329-1.14792.20850.0702-0.0527-1.2593-0.7643-0.2591-1.06460.64140.21340.18890.90810.1457-0.01940.8187-0.14370.822205.596964.271275.9074
134.6316-0.7566-0.08373.0342-0.77376.6817-0.0449-0.01370.0456-0.41680.12910.09420.16320.2818-0.08420.68560.12-0.0040.28790.00510.4338201.292986.235476.943
147.7329-0.86990.20091.23090.58662.1786-0.1933-0.6320.16030.0190.0226-0.13330.14760.27420.17070.34930.12710.09020.31940.07540.3379178.107590.4432113.7738
158.30040.52570.85686.36311.60356.49740.02950.54020.3842-0.5538-0.30870.3916-0.1589-0.54960.27920.28560.186-0.12550.3968-0.07460.1439142.929488.178193.1771
166.04831.346-2.22366.1048-4.11155.0338-0.3635-1.6272-1.18320.9640.12130.70880.9128-0.48880.24221.3898-0.24240.2581.39180.13871.1613124.182471.4762108.0996
174.77010.3143-0.37986.9748-1.84275.58050.0618-0.4958-0.40120.4935-0.0314-0.16920.65560.0906-0.03040.61740.0631-0.06040.8142-0.22580.3609162.829129.2775109.7475
182.647-1.7182-0.76645.9145-0.73323.4389-0.0389-0.0039-0.1679-0.1739-0.0665-0.02930.25230.00910.10540.27880.13590.02250.1823-0.03410.037109.986471.756669.3231
196.93440.84350.24647.77280.16956.5132-0.0734-0.3380.26320.43920.0766-0.6164-0.56890.4936-0.00330.23830.105-0.00050.17770.01180.0748105.818296.175273.3644
2010.39611.742-3.29664.1552-1.53171.64180.10590.1821-0.3105-0.0467-0.18470.0870.3561-0.0950.07880.49030.0325-0.03970.2174-0.08380.043381.953695.939773.7187
2111.3815-0.71830.65283.4978-0.37244.3663-0.0527-0.3053-0.29060.09940.14090.18450.1207-0.2935-0.08820.57130.2016-0.07030.1147-0.05880.232457.333994.168781.0044
224.06321.09510.4227.295-2.08468.72680.0768-0.2611-1.4424-0.2515-0.0260.52471.4607-0.9406-0.05081.31950.1447-0.2010.66920.02530.861137.902185.964171.949
235.8935-1.01040.79365.5826-0.15354.782-0.05181.0241.0253-0.4540.02520.0722-0.5913-0.34450.02661.68430.330.07581.04590.27350.570835.7872118.234552.5191
240.3220.0252-0.95580.0086-0.08012.96510.1331-0.0294-0.0099-0.02870.0738-0.0418-0.6285-0.2336-0.20691.6294-0.001-0.0661.5650.01411.5983120.2943131.741124.8442
250.7080.13660.13920.2077-0.70443.04630.1799-0.3546-0.3045-0.00290.04020.00080.0467-0.2139-0.22011.5319-0.0214-0.00821.5618-0.05841.5618118.8462151.520625.8308
260.09170.1029-0.06270.1332-0.07730.0459-0.0406-0.1646-0.20370.025-0.0654-0.13140.01010.03860.1062.6208-0.0424-0.04062.54460.00562.2645104.0109166.371924.3655
270.02030.00180.00210.0005-0.00040.0118-0.0254-0.04990.19930.00980.01930.0254-0.16760.02810.00612.444-0.09690.05522.0425-0.00192.126782.326159.007826.1582
288.4186-2.95881.55566.629-0.52373.2362-0.0230.2440.9509-0.2078-0.29090.5573-0.7087-0.64560.31391.15960.17550.2041.29580.08670.779879.0367130.809737.2767
295.73660.06421.77832.6434-0.45224.86710.2185-0.22530.3594-0.1499-0.04850.1395-0.3657-0.4527-0.170.2550.12830.0620.1052-0.01190.123103.9909114.714855.3741
303.53973.2333-0.00239.77884.13013.99110.2718-0.0157-0.1032-0.0741-0.2278-0.2448-0.51230.4225-0.04410.41560.13380.13310.52220.18540.2267123.5882135.440565.9847
314.5083-4.0557-1.9986.4483-0.53732.9864-0.11580.2093-0.1612-0.00330.16190.6084-0.0569-0.3736-0.0460.74860.1308-0.10590.5855-0.0720.7799162.5911153.781854.305
327.725-1.7836-2.63573.24421.063.2858-0.00120.14120.1893-0.1607-0.1131-0.1825-0.1690.01860.11440.32780.0906-0.02050.03920.0410.2305194.027137.309642.5216
335.8388-2.4615-1.34342.9940.68233.56920.27691.12990.2766-0.54760.01370.0754-0.1477-0.3921-0.29060.69210.0841-0.05030.5596-0.02090.5588145.9687170.835650.2733
341.6469-0.0494-0.07593.658-0.63833.05670.046-0.24820.00310.09790.0107-0.0672-0.19290.0237-0.05660.13190.12650.05190.21690.02980.0488145.8106169.848692.781
357.33024.9561-0.17376.78031.42372.29950.0187-0.1041.2948-0.8271-0.24761.1023-0.6771-0.24270.22890.91890.14120.04780.8060.16620.837105.5852169.85375.9243
364.641-0.76310.17873.06160.87266.5505-0.0534-0.0177-0.0552-0.40540.1266-0.0927-0.1607-0.2871-0.07320.68610.1120.03660.28110.02120.4447109.892147.890476.9598
377.8193-0.8687-0.18721.1961-0.59362.1808-0.1943-0.6333-0.14860.02180.02750.1327-0.1388-0.26840.16690.35460.1328-0.06970.3164-0.06080.3291133.1024143.6874113.7775
388.29310.4846-0.85816.6428-1.6646.48410.00640.5456-0.3886-0.5624-0.2959-0.40920.16540.54510.28950.28040.18910.14150.39640.08650.1462168.2674145.951793.1582
395.73831.34342.51426.22914.13574.6929-0.3932-1.59631.17850.92480.1794-0.7362-0.82180.46870.21381.4459-0.3051-0.24511.4398-0.12761.1602187.0195162.6548108.0666
404.85740.31290.41867.02281.80945.68990.0547-0.49590.4020.5164-0.03040.1765-0.6538-0.0837-0.02440.61860.07410.04050.80890.2140.3408148.2516204.7797109.7236
412.6032-1.71910.78355.91250.69263.4628-0.0361-0.01130.1664-0.1748-0.06420.0314-0.2421-0.0130.10030.27970.1334-0.01630.18320.03880.0365201.2183162.41369.3198
426.98640.9947-0.16147.8021-0.12186.4841-0.0577-0.329-0.28260.44510.0680.60170.5725-0.498-0.01030.2430.10170.00580.1707-0.00450.0721205.34137.993673.4013
4310.41811.67343.32734.10851.48221.67370.10120.18350.2854-0.0381-0.1767-0.0981-0.37650.10080.07550.50060.03110.04070.21780.09210.0454229.2058138.177973.7242
4411.5797-0.6552-0.63123.40660.39974.3156-0.0581-0.32110.27050.07830.1447-0.2-0.12090.2737-0.08670.59380.20510.06960.1140.05730.2135253.8346139.908180.9756
454.18751.0371-0.3827.51571.90718.42450.0838-0.23971.4412-0.2569-0.0112-0.5718-1.41250.9053-0.07271.35990.17040.2010.6646-0.03390.8396273.2678148.048971.8776
465.606-0.8403-0.86035.49120.15264.7032-0.07970.9944-1.0701-0.43620.0471-0.05010.56020.28250.03261.70480.3299-0.07211.0368-0.27030.5896275.2812115.733652.5086
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1ELECTRON MICROSCOPY1A17 - 100
2ELECTRON MICROSCOPY2A101 - 186
3ELECTRON MICROSCOPY3A187 - 275
4ELECTRON MICROSCOPY4A276 - 490
5ELECTRON MICROSCOPY5A497 - 633
6ELECTRON MICROSCOPY6A644 - 786
7ELECTRON MICROSCOPY7A791 - 903
8ELECTRON MICROSCOPY8A933 - 1005
9ELECTRON MICROSCOPY9A1006 - 1222
10ELECTRON MICROSCOPY10A1261 - 1391
11ELECTRON MICROSCOPY11A2241 - 3002
12ELECTRON MICROSCOPY11A2192 - 2228
13ELECTRON MICROSCOPY11A1392 - 1442
14ELECTRON MICROSCOPY12A1443 - 1537
15ELECTRON MICROSCOPY13A1538 - 1677
16ELECTRON MICROSCOPY14A1678 - 2001
17ELECTRON MICROSCOPY15A2002 - 2021
18ELECTRON MICROSCOPY15A2119 - 2191
19ELECTRON MICROSCOPY15A2229 - 2240
20ELECTRON MICROSCOPY16A2022 - 2118
21ELECTRON MICROSCOPY17D8 - 324
22ELECTRON MICROSCOPY18W54 - 270
23ELECTRON MICROSCOPY18W341 - 371
24ELECTRON MICROSCOPY19W271 - 340
25ELECTRON MICROSCOPY19W372 - 406
26ELECTRON MICROSCOPY20W45 - 53
27ELECTRON MICROSCOPY20W407 - 512
28ELECTRON MICROSCOPY20X111 - 118
29ELECTRON MICROSCOPY21W39 - 44
30ELECTRON MICROSCOPY21W513 - 631
31ELECTRON MICROSCOPY21W958 - 970
32ELECTRON MICROSCOPY22W632 - 840
33ELECTRON MICROSCOPY22W950 - 957
34ELECTRON MICROSCOPY23W18 - 38
35ELECTRON MICROSCOPY23W971 - 1331
36ELECTRON MICROSCOPY24B17 - 100
37ELECTRON MICROSCOPY25B101 - 186
38ELECTRON MICROSCOPY26B187 - 275
39ELECTRON MICROSCOPY27B276 - 490
40ELECTRON MICROSCOPY28B497 - 633
41ELECTRON MICROSCOPY29B644 - 786
42ELECTRON MICROSCOPY30B791 - 903
43ELECTRON MICROSCOPY31B933 - 1005
44ELECTRON MICROSCOPY32B1006 - 1222
45ELECTRON MICROSCOPY33B1261 - 1391
46ELECTRON MICROSCOPY34B2241 - 3002
47ELECTRON MICROSCOPY34B2192 - 2228
48ELECTRON MICROSCOPY34B1392 - 1442
49ELECTRON MICROSCOPY35B1443 - 1537
50ELECTRON MICROSCOPY36B1538 - 1677
51ELECTRON MICROSCOPY37B1678 - 2001
52ELECTRON MICROSCOPY38B2002 - 2021
53ELECTRON MICROSCOPY38B2119 - 2191
54ELECTRON MICROSCOPY38B2229 - 2240
55ELECTRON MICROSCOPY39B2022 - 2118
56ELECTRON MICROSCOPY40E8 - 324
57ELECTRON MICROSCOPY41Y54 - 270
58ELECTRON MICROSCOPY41Y341 - 371
59ELECTRON MICROSCOPY42Y271 - 340
60ELECTRON MICROSCOPY42Y372 - 406
61ELECTRON MICROSCOPY43Y45 - 53
62ELECTRON MICROSCOPY43Y407 - 512
63ELECTRON MICROSCOPY43Z111 - 118
64ELECTRON MICROSCOPY44Y39 - 44
65ELECTRON MICROSCOPY44Y513 - 631
66ELECTRON MICROSCOPY44Y958 - 970
67ELECTRON MICROSCOPY45Y632 - 840
68ELECTRON MICROSCOPY45Y950 - 957
69ELECTRON MICROSCOPY46Y18 - 38
70ELECTRON MICROSCOPY46Y971 - 1331

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