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- PDB-5vgz: Conformational Landscape of the p28-Bound Human Proteasome Regula... -

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Basic information

Entry
Database: PDB / ID: 5vgz
TitleConformational Landscape of the p28-Bound Human Proteasome Regulatory Particle
Components
  • (26S proteasome non-ATPase regulatory subunit ...) x 10
  • (26S proteasome regulatory subunit ...) x 6
  • 26S proteasome complex subunit SEM1
KeywordsHYDROLASE / p28 / 26S proteasome / regulatory particle / 19S / gankyrin
Function / homology
Function and homology information


positive regulation of inclusion body assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / meiosis I / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / proteasome accessory complex / integrator complex / proteasome regulatory particle ...positive regulation of inclusion body assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / meiosis I / Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases / proteasome accessory complex / integrator complex / proteasome regulatory particle / positive regulation of proteasomal protein catabolic process / cytosolic proteasome complex / proteasome regulatory particle, lid subcomplex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / negative regulation of programmed cell death / protein K63-linked deubiquitination / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Regulation of ornithine decarboxylase (ODC) / Resolution of D-loop Structures through Holliday Junction Intermediates / Cross-presentation of soluble exogenous antigens (endosomes) / K63-linked deubiquitinase activity / Somitogenesis / Impaired BRCA2 binding to RAD51 / proteasome binding / transcription factor binding / regulation of protein catabolic process / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / blastocyst development / general transcription initiation factor binding / polyubiquitin modification-dependent protein binding / endopeptidase activator activity / protein deubiquitination / proteasome assembly / positive regulation of RNA polymerase II transcription preinitiation complex assembly / mRNA export from nucleus / enzyme regulator activity / regulation of proteasomal protein catabolic process / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / ERAD pathway / inclusion body / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / Asymmetric localization of PCP proteins / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / stem cell differentiation / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / Degradation of AXIN / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / G2/M Checkpoints / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / double-strand break repair via homologous recombination / P-body / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / HDR through Homologous Recombination (HRR) / CDK-mediated phosphorylation and removal of Cdc6 / Metalloprotease DUBs / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / double-strand break repair via nonhomologous end joining / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / cytoplasmic ribonucleoprotein granule / Orc1 removal from chromatin
Similarity search - Function
: / Ubiquitin interaction motif / : / 26S proteasome regulatory subunit RPN7/PSMD6 C-terminal helix / 26S proteasome non-ATPase regulatory subunit Rpn12 / 26S proteasome regulatory subunit, C-terminal / Proteasome regulatory subunit C-terminal / DSS1/SEM1 / 26S proteasome regulatory subunit RPN5, C-terminal domain / : ...: / Ubiquitin interaction motif / : / 26S proteasome regulatory subunit RPN7/PSMD6 C-terminal helix / 26S proteasome non-ATPase regulatory subunit Rpn12 / 26S proteasome regulatory subunit, C-terminal / Proteasome regulatory subunit C-terminal / DSS1/SEM1 / 26S proteasome regulatory subunit RPN5, C-terminal domain / : / : / DSS1/SEM1 family / 26S proteasome regulatory subunit RPN5 C-terminal domain / 26S proteasome subunit RPN2, N-terminal domain / PSD13 N-terminal repeats / DSS1_SEM1 / 26S proteasome regulatory subunit Rpn6, N-terminal / 6S proteasome subunit Rpn6, C-terminal helix domain / 26S proteasome regulatory subunit RPN6 N-terminal domain / 26S proteasome subunit RPN6 C-terminal helix domain / 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunit / 26S Proteasome non-ATPase regulatory subunit 13 / 26S proteasome regulatory subunit RPN2, C-terminal / 26S proteasome regulatory subunit RPN2 C-terminal domain / 26S Proteasome non-ATPase regulatory subunit 7/8 / : / 26S proteasome regulatory subunit 7, OB domain / : / : / PSMD12/CSN4, N-terminal / 26S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1 / 26S proteasome regulatory subunit Rpn7, N-terminal / 26S proteasome subunit RPN7 / 26S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4 / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / Ubiquitin-interacting motif. / PCI/PINT associated module / : / von Willebrand factor type A domain / HEAT repeats / Proteasomal ATPase OB C-terminal domain / Proteasomal ATPase OB C-terminal domain / CSN8/PSMD8/EIF3K / CSN8/PSMD8/EIF3K family / Rpn11/EIF3F, C-terminal / Maintenance of mitochondrial structure and function / : / motif in proteasome subunits, Int-6, Nip-1 and TRIP-15 / PCI domain / Proteasome component (PCI) domain / PCI domain profile. / Ubiquitin interacting motif / Ubiquitin-interacting motif (UIM) domain profile. / Leucine-rich Repeat Variant / JAB1/Mov34/MPN/PAD-1 ubiquitin protease / Leucine-rich Repeat Variant / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / JAB/MPN domain / JAB1/MPN/MOV34 metalloenzyme domain / MPN domain / MPN domain profile. / von Willebrand factor A-like domain superfamily / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / Armadillo-like helical / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase / Mainly Alpha
Similarity search - Domain/homology
26S proteasome non-ATPase regulatory subunit 11 / 26S proteasome non-ATPase regulatory subunit 12 / 26S proteasome non-ATPase regulatory subunit 14 / 26S proteasome non-ATPase regulatory subunit 3 / 26S proteasome regulatory subunit 6A / 26S proteasome regulatory subunit 7 / 26S proteasome regulatory subunit 6B / 26S proteasome non-ATPase regulatory subunit 8 / 26S proteasome non-ATPase regulatory subunit 7 / 26S proteasome non-ATPase regulatory subunit 4 ...26S proteasome non-ATPase regulatory subunit 11 / 26S proteasome non-ATPase regulatory subunit 12 / 26S proteasome non-ATPase regulatory subunit 14 / 26S proteasome non-ATPase regulatory subunit 3 / 26S proteasome regulatory subunit 6A / 26S proteasome regulatory subunit 7 / 26S proteasome regulatory subunit 6B / 26S proteasome non-ATPase regulatory subunit 8 / 26S proteasome non-ATPase regulatory subunit 7 / 26S proteasome non-ATPase regulatory subunit 4 / 26S proteasome complex subunit SEM1 / 26S proteasome regulatory subunit 4 / 26S proteasome regulatory subunit 8 / 26S proteasome regulatory subunit 10B / 26S proteasome non-ATPase regulatory subunit 6 / 26S proteasome non-ATPase regulatory subunit 1 / 26S proteasome non-ATPase regulatory subunit 13
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.5 Å
AuthorsLu, Y. / Wu, J. / Dong, Y. / Chen, S. / Sun, S. / Ma, Y.B. / Ouyang, Q. / Finley, D. / Kirschner, M.W. / Mao, Y.
CitationJournal: Mol Cell / Year: 2017
Title: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.
Authors: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao /
Abstract: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.
History
DepositionApr 12, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 23, 2017Provider: repository / Type: Initial release
Revision 1.1Aug 22, 2018Group: Data collection / Database references / Category: pdbx_related_exp_data_set
Item: _pdbx_related_exp_data_set.data_reference / _pdbx_related_exp_data_set.metadata_reference
Revision 1.2Aug 16, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / refine
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.pdb_format_compatible / _refine.ls_d_res_high / _refine.ls_d_res_low

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Structure visualization

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Assembly

Deposited unit
A: 26S proteasome regulatory subunit 7
B: 26S proteasome regulatory subunit 4
C: 26S proteasome regulatory subunit 8
D: 26S proteasome regulatory subunit 6B
E: 26S proteasome regulatory subunit 10B
F: 26S proteasome regulatory subunit 6A
U: 26S proteasome non-ATPase regulatory subunit 1
V: 26S proteasome non-ATPase regulatory subunit 3
W: 26S proteasome non-ATPase regulatory subunit 12
X: 26S proteasome non-ATPase regulatory subunit 11
Y: 26S proteasome non-ATPase regulatory subunit 6
Z: 26S proteasome non-ATPase regulatory subunit 7
a: 26S proteasome non-ATPase regulatory subunit 13
b: 26S proteasome non-ATPase regulatory subunit 4
c: 26S proteasome non-ATPase regulatory subunit 14
d: 26S proteasome non-ATPase regulatory subunit 8
e: 26S proteasome complex subunit SEM1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)535,26918
Polymers535,20317
Non-polymers651
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area63690 Å2
ΔGint-344 kcal/mol
Surface area233450 Å2

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Components

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26S proteasome regulatory subunit ... , 6 types, 6 molecules ABCDEF

#1: Protein 26S proteasome regulatory subunit 7 / 26S proteasome AAA-ATPase subunit RPT1 / Proteasome 26S subunit ATPase 2 / Protein MSS1


Mass: 9309.589 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC2, MSS1 / Production host: Homo sapiens (human) / References: UniProt: P35998
#2: Protein 26S proteasome regulatory subunit 4 / P26s4 / 26S proteasome AAA-ATPase subunit RPT2 / Proteasome 26S subunit ATPase 1


Mass: 7969.963 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC1 / Production host: Homo sapiens (human) / References: UniProt: P62191
#3: Protein 26S proteasome regulatory subunit 8 / 26S proteasome AAA-ATPase subunit RPT6 / Proteasome 26S subunit ATPase 5 / Proteasome subunit p45 / ...26S proteasome AAA-ATPase subunit RPT6 / Proteasome 26S subunit ATPase 5 / Proteasome subunit p45 / Thyroid hormone receptor-interacting protein 1 / TRIP1 / p45/SUG


Mass: 13603.661 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC5, SUG1 / Production host: Homo sapiens (human) / References: UniProt: P62195
#4: Protein 26S proteasome regulatory subunit 6B / 26S proteasome AAA-ATPase subunit RPT3 / MB67-interacting protein / MIP224 / Proteasome 26S subunit ...26S proteasome AAA-ATPase subunit RPT3 / MB67-interacting protein / MIP224 / Proteasome 26S subunit ATPase 4 / Tat-binding protein 7 / TBP-7


Mass: 12341.005 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC4, MIP224, TBP7 / Production host: Homo sapiens (human) / References: UniProt: P43686
#5: Protein 26S proteasome regulatory subunit 10B / 26S proteasome AAA-ATPase subunit RPT4 / Proteasome 26S subunit ATPase 6 / Proteasome subunit p42


Mass: 12197.259 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC6, SUG2 / Production host: Homo sapiens (human) / References: UniProt: P62333
#6: Protein 26S proteasome regulatory subunit 6A / 26S proteasome AAA-ATPase subunit RPT5 / Proteasome 26S subunit ATPase 3 / Proteasome subunit P50 / ...26S proteasome AAA-ATPase subunit RPT5 / Proteasome 26S subunit ATPase 3 / Proteasome subunit P50 / Tat-binding protein 1 / TBP-1


Mass: 12942.888 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMC3, TBP1 / Production host: Homo sapiens (human) / References: UniProt: P17980

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26S proteasome non-ATPase regulatory subunit ... , 10 types, 10 molecules UVWXYZabcd

#7: Protein 26S proteasome non-ATPase regulatory subunit 1 / 26S proteasome regulatory subunit RPN2 / 26S proteasome regulatory subunit S1 / 26S proteasome subunit p112


Mass: 103755.023 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD1 / Production host: Homo sapiens (human) / References: UniProt: Q99460
#8: Protein 26S proteasome non-ATPase regulatory subunit 3 / 26S proteasome regulatory subunit RPN3 / 26S proteasome regulatory subunit S3 / Proteasome subunit p58


Mass: 55703.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD3 / Production host: Homo sapiens (human) / References: UniProt: O43242
#9: Protein 26S proteasome non-ATPase regulatory subunit 12 / 26S proteasome regulatory subunit RPN5 / 26S proteasome regulatory subunit p55


Mass: 52979.359 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD12 / Production host: Homo sapiens (human) / References: UniProt: O00232
#10: Protein 26S proteasome non-ATPase regulatory subunit 11 / 26S proteasome regulatory subunit RPN6 / 26S proteasome regulatory subunit S9 / 26S proteasome ...26S proteasome regulatory subunit RPN6 / 26S proteasome regulatory subunit S9 / 26S proteasome regulatory subunit p44.5


Mass: 43427.055 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD11 / Production host: Homo sapiens (human) / References: UniProt: O00231
#11: Protein 26S proteasome non-ATPase regulatory subunit 6 / 26S proteasome regulatory subunit RPN7 / 26S proteasome regulatory subunit S10 / Breast cancer- ...26S proteasome regulatory subunit RPN7 / 26S proteasome regulatory subunit S10 / Breast cancer-associated protein SGA-113M / Phosphonoformate immuno-associated protein 4 / Proteasome regulatory particle subunit p44S10 / p42A


Mass: 44336.906 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD6, KIAA0107, PFAAP4 / Production host: Homo sapiens (human) / References: UniProt: Q15008
#12: Protein 26S proteasome non-ATPase regulatory subunit 7 / 26S proteasome regulatory subunit RPN8 / 26S proteasome regulatory subunit S12 / Mov34 protein ...26S proteasome regulatory subunit RPN8 / 26S proteasome regulatory subunit S12 / Mov34 protein homolog / Proteasome subunit p40


Mass: 32382.094 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD7, MOV34L / Production host: Homo sapiens (human) / References: UniProt: P51665
#13: Protein 26S proteasome non-ATPase regulatory subunit 13 / 26S proteasome regulatory subunit RPN9 / 26S proteasome regulatory subunit S11 / 26S proteasome ...26S proteasome regulatory subunit RPN9 / 26S proteasome regulatory subunit S11 / 26S proteasome regulatory subunit p40.5


Mass: 42734.988 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD13 / Production host: Homo sapiens (human) / References: UniProt: Q9UNM6
#14: Protein 26S proteasome non-ATPase regulatory subunit 4 / 26S proteasome regulatory subunit RPN10 / 26S proteasome regulatory subunit S5A / Antisecretory ...26S proteasome regulatory subunit RPN10 / 26S proteasome regulatory subunit S5A / Antisecretory factor 1 / ASF / Multiubiquitin chain-binding protein


Mass: 20866.023 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD4, MCB1 / Production host: Homo sapiens (human) / References: UniProt: P55036
#15: Protein 26S proteasome non-ATPase regulatory subunit 14 / 26S proteasome regulatory subunit RPN11 / 26S proteasome-associated PAD1 homolog 1


Mass: 32329.355 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD14, POH1 / Production host: Homo sapiens (human)
References: UniProt: O00487, Hydrolases; Acting on peptide bonds (peptidases); Omega peptidases
#16: Protein 26S proteasome non-ATPase regulatory subunit 8 / 26S proteasome regulatory subunit RPN12 / 26S proteasome regulatory subunit S14 / p31


Mass: 30039.699 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD8 / Production host: Homo sapiens (human) / References: UniProt: P48556

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Protein / Non-polymers , 2 types, 2 molecules e

#17: Protein 26S proteasome complex subunit SEM1 / 26S proteasome complex subunit DSS1 / Deleted in split hand/split foot protein 1 / Split hand/foot ...26S proteasome complex subunit DSS1 / Deleted in split hand/split foot protein 1 / Split hand/foot deleted protein 1 / Split hand/foot malformation type 1 protein / Sem1


Mass: 8284.611 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEM1, C7orf76, DSS1, SHFDG1, SHFM1 / Production host: Homo sapiens (human) / References: UniProt: P60896
#18: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn

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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: Proteasome regulatory particle / Type: COMPLEX / Entity ID: #1-#17 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
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: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.11.1_2575: / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 117471 / Symmetry type: POINT
RefinementResolution: 4.5→4.5 Å / SU ML: 1.24 / σ(F): 0 / Phase error: 69.72 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.4468 2086 0.32 %
Rwork0.487 --
obs0.4869 652306 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00537363
ELECTRON MICROSCOPYf_angle_d1.05750457
ELECTRON MICROSCOPYf_dihedral_angle_d9.82422980
ELECTRON MICROSCOPYf_chiral_restr0.0585767
ELECTRON MICROSCOPYf_plane_restr0.0076469
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)
12.5332.6116-3.93232.6992-3.97876.3273-0.23430.687-0.715-0.51530.2147-0.60250.09741.66550.13773.5321-1.65623.06286.6832-1.14457.2632150.243379.092114.079
24.1512.9983-4.41572.2696-3.26194.85180.58631.34220.6345-1.56211.088-2.6567-0.46582.1178-1.28193.9703-0.53380.51585.5567-1.46922.9121148.425982.8821126.0707
34.80613.18890.98546.56884.18512.92861.73372.68282.2790.1695-2.34150.0037-1.5783-0.8914-0.94442.0031-0.09161.58412.88730.23692.6923161.5543102.3802131.4274
42.246-1.24722.21897.0714-0.15643.4713-1.76650.68740.82850.8727-0.67450.9509-1.53940.01841.70473.1722-2.57580.96842.3233-0.51062.2971163.5609107.2288133.0947
58.7505-3.28222.95864.9095-4.97055.04590.6105-0.38111.16642.1144-0.7346-0.1694-0.43861.18510.82884.8585-1.93641.43634.4793-2.91384.6905169.351102.476130.5279
60.90740.46061.33223.0418-0.36042.3430.5695-0.0852-0.82760.3520.29430.7080.03510.23290.79141.5192-2.32740.23752.845-1.17513.2178160.6863100.1127131.2639
79.02826.51847.86035.37855.04647.4231-1.805-4.9177-0.88861.49980.88664.46640.90314.15290.38230.97120.69171.82993.8347-0.04174.8076139.609885.6645116.109
83.48510.7914-3.25480.1734-0.73013.0311-0.383-0.23611.08120.4868-0.3418-1.7538-1.0423-0.58331.52263.06460.64620.45094.282-1.60033.5763153.940199.3378112.9653
92.14770.04564.81978.9708-6.1171.9990.7012-1.7871-0.70512.9568-0.2325-3.471-0.1944.8801-0.3292.9927-0.6785-1.56514.331-1.04452.1673163.060291.1412119.2069
105.86191.78923.28471.16120.38362.50820.24430.010.70730.3672-0.307-0.34690.48321.55730.6147-3.25982.78933.4311.0677-1.56871.5187154.638796.8608117.5607
116.21741.3897-0.44523.4716-4.11985.13520.60030.9532-2.0703-1.85790.34880.3128-0.34882.7327-0.7062.0386-1.2579-0.17443.5936-1.76834.1441156.144893.2133109.423
120.5111-0.87890.17571.9542-0.79620.53111.3644-0.49670.7506-2.5832-1.60050.6884-0.69143.3368-0.56861.68310.64050.25481.9585-0.14172.2162148.91295.6922113.836
132.7327-0.2035-0.04810.07630.74674.6923-0.34581.4457-0.2554-1.1515-0.07270.5661-1.26692.03770.1857.19181.39110.46062.7933-1.2181-1.848589.2213110.3355123.7236
144.3766-2.5273-1.32862.3238-2.24669.768-0.4424-0.0172.88561.3987-1.9089-0.1226-0.40942.99280.6579-5.94417.63545.4078-2.7158-4.4922-0.3657135.4465103.6251108.5049
151.50871.33150.32651.08840.36160.58810.2298-1.38961.2320.45120.366-0.1249-1.04860.5226-0.42356.64672.5254-0.27484.0994-3.14792.711579.8325104.7879129.4996
163.53034.0907-0.54834.5703-0.66080.3774-0.72750.20141.0913-0.4494-0.97811.5820.3449-0.92071.30072.9824-0.80051.59672.75180.6460.7782118.286120.0394124.5964
174.77952.4096-2.73411.29-1.82793.8788-0.5260.93690.6931-1.31940.70210.22040.2361-0.49981.29712.2963-2.34750.56391.97333.59722.0054128.7387118.7013115.3269
189.84675.8002-6.52433.4076-3.8974.4419-1.13611.43541.568-2.90420.59222.4021-0.6571-2.26020.03493.74110.0992-0.60984.31341.17831.8542127.2975126.0088117.3845
193.1132-0.144-0.77080.29231.22872.7926-0.6707-1.6369-2.16650.66890.1887-1.22240.33651.9832-0.43962.621-0.56163.40766.82391.60352.7845162.4434125.4882177.3484
204.2653-4.98845.56739.5426-4.22538.4727-0.4786-1.08230.6164-0.54861.2096-1.3085-0.6066-0.1655-0.6831-1.3842-2.39660.55872.16391.48730.4142138.852131.2482128.8914
214.22810.9956-0.40264.37061.05032.0445-0.6662-2.09911.32361.60371.8261.3646-1.27032.6776-0.67320.6828-0.09572.28722.4721-1.63791.3384136.2542138.9121137.7634
225.4863-0.32973.22525.33333.2355.5037-1.3858-1.88231.44781.44330.8250.7646-1.62381.43570.68820.7698-0.18291.77413.19530.16340.7863143.4496131.8152136.059
233.6807-2.53311.14971.9849-0.76710.3574-0.7531-3.63871.8851.24461.40731.70751.2887-2.0999-1.07153.2488-1.5163.31236.00360.54135.9402155.9925116.6259170.697
247.836-0.3444-0.16480.2540.84452.9451.0655-1.5938-0.37560.57850.07640.7543-1.20080.4001-0.60950.4950.19321.18644.4326-0.42963.6934158.2188117.7798136.6528
259.78831.61060.51823.2184-3.72895.0223-2.7281-1.546.3063-2.63933.4037-2.0994-9.7369-0.0153-1.50183.97950.11030.99674.37031.35244.2466149.7418136.0578145.8994
262.66053.60110.81951.99322.00639.6622-1.3980.53690.61771.7771-2.31033.60551.4567-3.08243.5668-0.33910.2431-1.14964.1869-0.48063.8394152.7176124.3003132.3915
270.5180.265-0.5192.23191.17311.4994-2.6848-0.59793.16023.1028-1.3528-7.24351.09758.12614.61891.99030.20150.51625.82730.30945.3369160.3012126.9751147.5506
284.47765.82437.66547.58039.9771.99980.57831.86843.17622.33780.5884-3.61843.49672.9225-0.94992.7660.45661.87515.2469-0.57935.3646161.9567122.9227137.8063
296.1534-5.8158-2.59566.29810.31416.78381.3948-0.6832-1.1744-0.37730.6891.63013.7363-3.5667-1.95551.49680.0571.93181.04692.40591.902150.3361116.1211139.1934
302.0571-1.9547-1.42944.59394.26997.28722.0408-1.09192.77390.64210.4855-1.079-2.27252.2094-2.52626.1918-2.2619-0.76482.68750.03515.4985166.0059120.5692140.2388
315.57581.64672.33442.06180.48928.78670.5085-0.44851.88070.45661.32631.2762-1.45251.19440.09616.36740.47293.98162.56251.8242-0.190643.5688128.7298136.4377
321.0017-0.14641.2291.99280.96684.84580.73581.17610.3165-1.0302-0.0859-0.6248-0.74571.3575-0.10791.74561.25736.17841.2543-3.1247-2.339255.4582103.7226137.3038
331.957-1.2641-1.64321.03461.53121.8091-0.8367-1.0952-1.06150.21170.005-0.36531.84040.177-0.82070.07523.7946.24945.4899-3.885-1.677168.826677.6437138.8319
340.4926-0.70170.24581.17560.11450.63260.725-0.2834-1.1265-0.2483-0.06290.2440.3259-0.87075.59092.38567.5978-0.69745.7733-4.61651.709699.752966.4436133.1864
350.1065-1.17120.1392.37960.78082.41940.6166-0.3742-2.5012.1471-0.17211.5699-0.3329-0.20330.34487.68426.5638-1.5940.7262-10.0041-4.243498.992483.7585134.9433
363.75242.5017-1.66774.0283-1.66631.18170.4145-0.4863-2.5364-0.0397-0.36670.39610.56110.1281-0.27684.28944.8661-2.80287.6461-2.9775.178978.800561.8632121.0287
372.18721.21270.3972.38081.17942.78690.8155-2.2761-0.2687-2.35630.0569-3.61620.74710.23081.32265.37850.70370.19428.2391-1.78638.919467.9268120.185191.1665
383.7846-1.44811.16392.1676-1.86551.58542.96037.329-8.4454-4.0794-3.62632.20125.91564.30810.65052.6944-9.39273.7184-3.13581.80030.185761.894132.3021108.0312
396.2237-3.7764-0.61166.8437-1.23692.5579-2.7193-0.59371.03894.8471.5171-3.3651-4.20792.15640.09350.5204-1.7335-0.85873.37560.3468-0.389573.0566160.7126127.7076
400.79010.66950.66399.32835.69033.60610.47761.1396-3.7022-2.4075-0.2625-2.50372.41951.3898-1.98299.01952.14670.62988.32872.27978.5593194.029187.9706137.7977
418.53455.75650.50765.8807-1.41091.59011.77140.4855-1.11672.7559-0.0996-6.19962.207-0.5174-2.49729.69513.6922.31535.45360.75297.7317178.9063191.871143.5872
420.8215-0.07790.26320.10190.0530.2767-0.15310.3066-0.52010.2557-1.3133-0.4321.8069-1.0153-0.67246.23021.66885.83389.33083.32063.2624161.4751183.4712146.9982
433.4791-1.64483.25235.0371-0.48033.24890.68121.01720.2501-1.6645-2.9815-0.62330.0604-1.1271-0.7521-1.74252.30824.54694.7722-2.8775.1586138.6577177.7356165.9574
447.63970.0807-0.11933.04180.93893.7598-0.5827-1.03922.43281.47571.45351.24710.11642.56282.02242.05092.8275-2.01065.94860.67518.1087117.9344181.0921157.4514
455.50472.85550.9651.85170.31313.2337-0.3394-0.13090.3939-0.0679-0.96151.0612-0.85630.1301-0.07031.27260.5771-2.81045.8706-0.54245.9787107.8497170.3321147.8532
460.2578-0.83871.42585.1321-5.30397.06350.01760.0611-0.52131.898-0.6638-1.545-0.64821.0322-0.15632.73560.5768-2.45584.144-4.19348.0877110.4776139.2303163.0153
470.0450.14560.11291.2246-0.72892.5418-0.41870.16351.37330.25270.5307-1.3444-0.79231.2113-1.58975.09714.62992.87528.6315-1.60979.1945137.2547212.465880.6089
480.1976-0.06660.30260.0387-0.01140.80861.30550.75151.812-0.98450.2246-1.7624-0.03341.73521.33614.61796.65652.76016.7482-2.66828.8377129.2136191.508490.8664
493.41011.0668-1.60055.1441-2.55531.55470.948-0.8292-0.1288-0.891-0.0456-1.16930.5940.33980.88992.41874.99823.11916.4382-3.87934.9726131.2071193.0543119.276
501.6211-0.5398-0.59524.28972.39874.82920.5893-0.42850.08170.30580.64890.3581-0.7257-0.44472.2135-0.4325-3.98014.261.92826.05310.7968109.3413180.9885132.0342
517.2615-3.46310.84824.33082.20382.5918-0.86973.35212.0867-0.12110.3961-0.95090.5727-0.06191.96260.9997-0.35082.47932.3990.59141.564695.338141.757113.9738
526.0217-3.2012-5.18092.07432.73684.76722.57730.0286-2.3462-1.34750.287-3.42572.42480.5185-0.45778.43345.74471.03248.88-1.73827.435190.9381173.43571.6664
530.57440.1668-0.98910.5491-0.89492.34892.39462.46180.4411-3.243-0.6426-2.18362.70151.19682.0321.70745.4696-0.9015.6319-4.92484.5438101.3278165.054990.8174
541.2945-1.9704-1.63864.9279-2.86410.04420.7506-2.6787-0.5564.62771.8473-1.5328-0.7612-0.8948-0.4516-11.918313.97612.8093-4.4521-9.384-7.132791.5841172.7287116.7431
551.1876-0.56350.25080.1035-0.0385-0.04760.4205-0.4424-1.27561.0066-0.6109-0.5651-0.2595-0.8652-1.9308-1.64832.8589-7.41261.831-5.24285.3694128.5602116.9209167.3609
564.85992.88724.96267.08674.66336.0365-0.84110.09511.64860.8075-0.75910.66611.62291.99980.80263.38680.7673-3.8044.953-3.22535.0288119.9416124.9914160.4696
572.44951.60114.36381.30062.11526.4977-1.8877-0.33723.89982.15660.0051-1.9806-2.1856-1.3212-0.68360.5084-1.14011.09840.0801-1.2946.247899.0465135.7741145.709
582.4913-0.6125-0.68212.4125-1.29821.50783.70171.5475-2.96331.67920.1745-1.63831.30670.3068-0.05266.0913.4432-1.46936.81850.06257.022144.38139.414204.2671
592.8923-1.59210.42951.6891-0.32620.2296-0.3989-0.0620.1739-0.47930.67560.54070.39561.0620.25860.11380.2096-1.51326.07133.1796-0.2149119.1359151.9935192.8358
603.362-0.7536-0.30765.19724.4233.7014-4.30333.7142-1.6156-2.4157-2.4673.8766-0.56460.0645-0.5352-0.5137-4.1766-1.25660.05541.57735.9451102.3685156.5874172.2503
614.04011.83932.46572.16580.91398.22610.64491.3004-2.78251.07850.0342-1.6472-0.12750.7218-1.24655.1813.4464-0.38363.49690.47754.0845143.5604110.6349194.88
623.9299-0.1506-0.33722.78860.47152.21470.2830.6586-0.49660.45050.3263-0.73341.21531.0215-0.84510.82213.7716-1.00973.0533-3.35872.3326144.457106.7544187.9441
631.2453-0.3312-0.20822.07290.48110.71111.22530.69690.50910.01860.5962-0.63960.26040.1873-0.3040.33045.00690.28112.0963-3.39512.4702137.3383107.5722185.6215
643.00843.11992.69028.314-1.95976.8097-1.715-0.83841.27321.73321.7023.2735-2.71630.4620.33123.46330.74360.16554.8491-2.4783.3382124.6045108.1326198.7889
652.6524-3.61284.58174.9288-5.88149.99690.6606-2.44463.884-0.7716-1.4401-2.5370.0206-2.09240.02475.05763.8767-1.5355.5683-2.29164.8551132.8428102.2676201.5348
664.897-0.9524-0.87262.89982.99113.3221-0.8725-0.41071.23290.25821.5202-0.1292-0.20711.31350.34314.16011.1478-3.16494.6427-0.95384.3966146.981102.5594202.5978
671.0283-0.46270.63241.75020.27870.4895-0.4768-0.5687-0.7920.02660.30491.1007-0.3251-1.12720.6182-1.06250.954-0.81073.0671-1.924.5094126.9772101.3719146.463
681.72222.11830.2032.62020.12010.4184-0.0878-0.2004-0.81250.3985-0.10311.15080.2556-0.73731.44070.55174.350.16463.9902-1.00673.8799130.812399.0902150.1537
691.0251-1.695-1.45212.6152.17974.95210.8156-0.63730.19692.56011.3351-3.07020.55321.0053-0.3648-5.9911-2.204-2.3303-1.4765-0.40931.7358139.0966101.4026151.1474
702.8740.3041-0.20372.9451.59911.12231.04921.1469-1.5414-1.36020.7550.0323-0.2346-0.6049-0.548-12.188211.57333.2381-2.3096-5.0868-4.3087130.650693.6114138.5484
717.364-4.8226-5.34223.15983.96426.67232.17091.8470.794-1.154-1.04430.22640.1425-0.3223-0.76711.5032-0.5495-0.23130.83240.39920.7349127.135697.2671134.7213
724.5364-5.0852.9745.7566-2.84076.9753-2.131-0.43142.5099-1.38120.3342.7983-1.16090.17080.76865.08470.4565-3.29648.1682-3.10637.1032113.0583116.8123152.0439
732.96535.0371-4.22278.9738-7.32436.10021.24960.46451.256-1.02390.1114-1.0618-1.02310.0818-0.92364.1010.64451.06343.6312-0.045510.1676107.7241137.5814148.7199
742.8439-4.0095-0.23945.64120.38822.83751.03652.9312-0.8564-1.9542-0.6142-0.6249-0.40011.7252-1.19793.84670.43713.49316.39840.60424.1735106.2374139.8059118.6349
752.6906-1.38780.98450.9833-1.07673.2150.32141.3262-0.187-1.1876-0.68690.58530.61730.541-0.7841.00482.6731-0.4230.83691.33924.8992102.5351133.6274129.793
763.5528-4.413-3.41895.59134.3423.35821.408-0.6293-0.72543.5427-0.75160.3918-0.33610.3299-0.64952.9296-0.33221.36485.24721.24342.965118.7379149.2345133.1451
779.8516-2.43435.59284.6287-0.53633.34240.5903-1.3639-4.10141.4447-0.4182.2423-1.5793-1.1147-0.20013.3486-0.31371.48843.4163-0.15642.289927.4517142.545130.956
785.6545-0.26282.27053.25321.90032.18220.3418-0.96810.57040.33451.2427-0.3052-1.3850.7763-0.23176.38714.08213.21594.93891.06314.668137.9133149.0414128.676
791.09020.2657-0.5861.4906-0.24620.6833-0.3839-0.6446-0.3748-0.5888-0.6831-0.73391.081-0.10361.60943.4093-1.91131.35553.35834.59750.879848.4113158.6645125.0667
802.30023.7233-1.2658.5289-3.06723.844-0.71540.45070.5977-1.20320.34872.47470.5367-1.05720.12241.8663-1.80840.66780.8405-0.76040.600645.5358167.08136.8091
816.93062.1194-4.13058.7659-2.76922.66330.32360.78741.15971.7298-0.0416-3.5859-0.23530.2352-0.5099-0.3343-0.46481.14090.76570.63753.225758.0717171.5564150.0385
824.72381.86851.70962.7335-0.25815.9935-0.2261-1.6295-1.4487-1.3556-1.7248-4.0293.43374.28932.31945.4592-0.808-0.6764.58622.29116.230275.7147163.537152.6245
834.36131.67291.6060.64960.70241.84920.00150.754-0.6392-0.27130.22220.78040.2479-0.3136-0.87641.21632.0603-2.7851.851-0.61054.67490.1853133.6101139.8243
841.9971-0.17963.1030.0024-0.060.944-1.98562.48114.5878-2.98660.342-0.1178-0.66973.47590.46588.1175-2.87291.38575.36511.38374.583762.7975146.841299.7616
853.091.24042.65222.3452-0.06082.97290.6649-3.17440.6468-0.47461.62591.97571.0699-4.833-2.04446.8252-1.13861.85759.1430.86998.301171.3515162.868291.5966
862.9402-1.24551.74660.5769-0.81871.16290.7352.1202-0.7611-1.5952-0.584-0.31430.4367-0.005-0.26866.73332.94640.91267.1699-1.80533.915883.1029163.129398.8409
877.1408-2.7590.32757.021-3.96632.50163.13890.8675-1.4806-0.740.58122.68333.53611.0988-3.94296.8851.3858-0.42246.8724-0.97662.743179.3805174.2192108.2507
882.8999-0.3389-3.83342.055-0.60385.61351.1072-0.56150.89480.1453-0.3125-1.0477-1.53041.6739-0.37553.3351-1.51610.6155.4132.43364.20683.5571193.5303114.5986
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1ELECTRON MICROSCOPY1chain 'A' and (resid 73 through 83 )
2ELECTRON MICROSCOPY2chain 'A' and (resid 84 through 88 )
3ELECTRON MICROSCOPY3chain 'A' and (resid 89 through 109 )
4ELECTRON MICROSCOPY4chain 'A' and (resid 110 through 130 )
5ELECTRON MICROSCOPY5chain 'A' and (resid 131 through 143 )
6ELECTRON MICROSCOPY6chain 'A' and (resid 144 through 155 )
7ELECTRON MICROSCOPY7chain 'B' and (resid 93 through 106 )
8ELECTRON MICROSCOPY8chain 'B' and (resid 107 through 114 )
9ELECTRON MICROSCOPY9chain 'B' and (resid 115 through 121 )
10ELECTRON MICROSCOPY10chain 'B' and (resid 122 through 139 )
11ELECTRON MICROSCOPY11chain 'B' and (resid 140 through 153 )
12ELECTRON MICROSCOPY12chain 'B' and (resid 154 through 165 )
13ELECTRON MICROSCOPY13chain 'C' and (resid 11 through 67 )
14ELECTRON MICROSCOPY14chain 'C' and (resid 68 through 128 )
15ELECTRON MICROSCOPY15chain 'D' and (resid 39 through 65 )
16ELECTRON MICROSCOPY16chain 'D' and (resid 66 through 99 )
17ELECTRON MICROSCOPY17chain 'D' and (resid 100 through 120 )
18ELECTRON MICROSCOPY18chain 'D' and (resid 121 through 145 )
19ELECTRON MICROSCOPY19chain 'E' and (resid 11 through 51 )
20ELECTRON MICROSCOPY20chain 'E' and (resid 52 through 81 )
21ELECTRON MICROSCOPY21chain 'E' and (resid 82 through 96 )
22ELECTRON MICROSCOPY22chain 'E' and (resid 97 through 114 )
23ELECTRON MICROSCOPY23chain 'F' and (resid 53 through 84 )
24ELECTRON MICROSCOPY24chain 'F' and (resid 85 through 94 )
25ELECTRON MICROSCOPY25chain 'F' and (resid 95 through 121 )
26ELECTRON MICROSCOPY26chain 'F' and (resid 122 through 134 )
27ELECTRON MICROSCOPY27chain 'F' and (resid 135 through 144 )
28ELECTRON MICROSCOPY28chain 'F' and (resid 145 through 154 )
29ELECTRON MICROSCOPY29chain 'F' and (resid 155 through 159 )
30ELECTRON MICROSCOPY30chain 'F' and (resid 160 through 167 )
31ELECTRON MICROSCOPY31chain 'U' and (resid 1 through 71 )
32ELECTRON MICROSCOPY32chain 'U' and (resid 72 through 172 )
33ELECTRON MICROSCOPY33chain 'U' and (resid 173 through 254 )
34ELECTRON MICROSCOPY34chain 'U' and (resid 255 through 426 )
35ELECTRON MICROSCOPY35chain 'U' and (resid 427 through 838 )
36ELECTRON MICROSCOPY36chain 'U' and (resid 839 through 935 )
37ELECTRON MICROSCOPY37chain 'V' and (resid 18 through 104 )
38ELECTRON MICROSCOPY38chain 'V' and (resid 105 through 371 )
39ELECTRON MICROSCOPY39chain 'V' and (resid 372 through 505 )
40ELECTRON MICROSCOPY40chain 'W' and (resid 1 through 93 )
41ELECTRON MICROSCOPY41chain 'W' and (resid 94 through 134 )
42ELECTRON MICROSCOPY42chain 'W' and (resid 135 through 221 )
43ELECTRON MICROSCOPY43chain 'W' and (resid 222 through 343 )
44ELECTRON MICROSCOPY44chain 'W' and (resid 344 through 399 )
45ELECTRON MICROSCOPY45chain 'W' and (resid 400 through 423 )
46ELECTRON MICROSCOPY46chain 'W' and (resid 424 through 456 )
47ELECTRON MICROSCOPY47chain 'X' and (resid 38 through 81 )
48ELECTRON MICROSCOPY48chain 'X' and (resid 82 through 220 )
49ELECTRON MICROSCOPY49chain 'X' and (resid 221 through 317 )
50ELECTRON MICROSCOPY50chain 'X' and (resid 318 through 393 )
51ELECTRON MICROSCOPY51chain 'X' and (resid 394 through 422 )
52ELECTRON MICROSCOPY52chain 'Y' and (resid 12 through 113 )
53ELECTRON MICROSCOPY53chain 'Y' and (resid 114 through 245 )
54ELECTRON MICROSCOPY54chain 'Y' and (resid 246 through 389 )
55ELECTRON MICROSCOPY55chain 'Z' and (resid 5 through 115 )
56ELECTRON MICROSCOPY56chain 'Z' and (resid 116 through 185 )
57ELECTRON MICROSCOPY57chain 'Z' and (resid 186 through 290 )
58ELECTRON MICROSCOPY58chain 'a' and (resid 3 through 149 )
59ELECTRON MICROSCOPY59chain 'a' and (resid 150 through 242 )
60ELECTRON MICROSCOPY60chain 'a' and (resid 243 through 376 )
61ELECTRON MICROSCOPY61chain 'b' and (resid 1 through 24 )
62ELECTRON MICROSCOPY62chain 'b' and (resid 25 through 62 )
63ELECTRON MICROSCOPY63chain 'b' and (resid 63 through 113 )
64ELECTRON MICROSCOPY64chain 'b' and (resid 114 through 133 )
65ELECTRON MICROSCOPY65chain 'b' and (resid 134 through 169 )
66ELECTRON MICROSCOPY66chain 'b' and (resid 170 through 191 )
67ELECTRON MICROSCOPY67chain 'c' and (resid 24 through 47 )
68ELECTRON MICROSCOPY68chain 'c' and (resid 48 through 74 )
69ELECTRON MICROSCOPY69chain 'c' and (resid 75 through 125 )
70ELECTRON MICROSCOPY70chain 'c' and (resid 126 through 185 )
71ELECTRON MICROSCOPY71chain 'c' and (resid 186 through 210 )
72ELECTRON MICROSCOPY72chain 'c' and (resid 211 through 225 )
73ELECTRON MICROSCOPY73chain 'c' and (resid 226 through 243 )
74ELECTRON MICROSCOPY74chain 'c' and (resid 244 through 273 )
75ELECTRON MICROSCOPY75chain 'c' and (resid 274 through 310 )
76ELECTRON MICROSCOPY76chain 'd' and (resid 1 through 15 )
77ELECTRON MICROSCOPY77chain 'd' and (resid 16 through 64 )
78ELECTRON MICROSCOPY78chain 'd' and (resid 65 through 108 )
79ELECTRON MICROSCOPY79chain 'd' and (resid 109 through 145 )
80ELECTRON MICROSCOPY80chain 'd' and (resid 146 through 182 )
81ELECTRON MICROSCOPY81chain 'd' and (resid 183 through 218 )
82ELECTRON MICROSCOPY82chain 'd' and (resid 219 through 236 )
83ELECTRON MICROSCOPY83chain 'd' and (resid 237 through 257 )
84ELECTRON MICROSCOPY84chain 'e' and (resid 1 through 19 )
85ELECTRON MICROSCOPY85chain 'e' and (resid 20 through 32 )
86ELECTRON MICROSCOPY86chain 'e' and (resid 33 through 38 )
87ELECTRON MICROSCOPY87chain 'e' and (resid 39 through 62 )
88ELECTRON MICROSCOPY88chain 'e' and (resid 63 through 70 )

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