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- EMDB-22481: Composite cryo-EM density map of radial spoke 2 stalk, IDAc, and ... -

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Basic information

Entry
Database: EMDB / ID: EMD-22481
TitleComposite cryo-EM density map of radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule
Map data
Sample
  • Complex: Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule
    • Protein or peptide: x 19 types
  • Ligand: x 4 types
Keywordscilia / native / complex / microtubule / mechanoregulation / STRUCTURAL PROTEIN
Function / homology
Function and homology information


regulation of cilium movement / inner dynein arm / axonemal dynein complex assembly / epithelial cilium movement involved in determination of left/right asymmetry / inner dynein arm assembly / cilium-dependent cell motility / cilium movement involved in cell motility / 9+2 motile cilium / cilium movement / motile cilium assembly ...regulation of cilium movement / inner dynein arm / axonemal dynein complex assembly / epithelial cilium movement involved in determination of left/right asymmetry / inner dynein arm assembly / cilium-dependent cell motility / cilium movement involved in cell motility / 9+2 motile cilium / cilium movement / motile cilium assembly / dynein heavy chain binding / axoneme assembly / axonemal dynein complex / flagellated sperm motility / dynein complex / cytoplasmic dynein complex / ciliary plasm / motile cilium / dynein intermediate chain binding / heart looping / axoneme / microtubule-based process / cilium assembly / centriole / GTPase activator activity / acrosomal vesicle / filopodium / cell projection / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / small GTPase binding / cilium / microtubule cytoskeleton organization / mitotic cell cycle / microtubule binding / microtubule / cytoskeleton / hydrolase activity / GTPase activity / calcium ion binding / GTP binding / Golgi apparatus / ATP binding / membrane / metal ion binding / cytoplasm
Similarity search - Function
Axonemal dynein light chain / Dynein regulatory complex protein 1, C-terminal / Axonemal dynein light chain / Sperm tail C-terminal domain / Radial spoke protein 14 / Cilia- and flagella-associated protein 91 / CFAP91 domain / Coiled-coil domain-containing protein 39 / Coiled-coil domain-containing protein 40 / Cilia- and flagella-associated protein 91 ...Axonemal dynein light chain / Dynein regulatory complex protein 1, C-terminal / Axonemal dynein light chain / Sperm tail C-terminal domain / Radial spoke protein 14 / Cilia- and flagella-associated protein 91 / CFAP91 domain / Coiled-coil domain-containing protein 39 / Coiled-coil domain-containing protein 40 / Cilia- and flagella-associated protein 91 / IQ and ubiquitin-like domain-containing protein / Growth arrest-specific protein 8 domain / Growth arrest-specific protein 8 / Dynein regulatory complex protein 1/2, N-terminal / Dynein regulatory complex protein / Growth-arrest specific micro-tubule binding / Sperm tail / Radial spoke 3 / Radial spoke protein 3 / : / Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases. / Dynein light chain, type 1/2, conserved site / Dynein light chain type 1 signature. / cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain / Regulatory subunit of type II PKA R-subunit / RIIalpha, Regulatory subunit portion of type II PKA R-subunit / MORN motif / MORN repeat / Dynein light chain type 1 / Dynein light chain, type 1/2 / Dynein light chain superfamily / Dynein light chain type 1 / Leucine rich repeat, ribonuclease inhibitor type / EF hand / IQ calmodulin-binding motif / Leucine Rich repeat / Short calmodulin-binding motif containing conserved Ile and Gln residues. / IQ motif profile. / IQ motif, EF-hand binding site / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Actin / Actin family / Actin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Leucine-rich repeat / EF-hand domain pair / Leucine-rich repeat domain superfamily / EF-hand, calcium binding motif / ATPase, nucleotide binding domain / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / Armadillo-like helical / EF-hand domain pair / Armadillo-type fold
Similarity search - Domain/homology
Flagellar-associated protein 172 / Flagellar-associated protein 59 / IQ and ubiquitin-like domain-containing protein / Flagellar associated protein / MORN repeat-containing protein 3 / Cilia- and flagella-associated protein 91 / EF-hand domain-containing protein / Uncharacterized protein / Dynein regulatory complex subunit 2 / Tubulin beta-1/beta-2 chain ...Flagellar-associated protein 172 / Flagellar-associated protein 59 / IQ and ubiquitin-like domain-containing protein / Flagellar associated protein / MORN repeat-containing protein 3 / Cilia- and flagella-associated protein 91 / EF-hand domain-containing protein / Uncharacterized protein / Dynein regulatory complex subunit 2 / Tubulin beta-1/beta-2 chain / Tubulin alpha-1 chain / Dynein regulatory complex protein 1 / Actin / Radial spoke protein 11 / Radial spike protein 8 / Dynein 8 kDa light chain, flagellar outer arm / 28 kDa inner dynein arm light chain, axonemal / Dynein regulatory complex subunit 4
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsGui M / Ma M / Sze-Tu E / Wang X / Koh F / Zhong E / Berger B / Davis J / Dutcher S / Zhang R / Brown A
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Nat Struct Mol Biol / Year: 2021
Title: Structures of radial spokes and associated complexes important for ciliary motility.
Authors: Miao Gui / Meisheng Ma / Erica Sze-Tu / Xiangli Wang / Fujiet Koh / Ellen D Zhong / Bonnie Berger / Joseph H Davis / Susan K Dutcher / Rui Zhang / Alan Brown /
Abstract: In motile cilia, a mechanoregulatory network is responsible for converting the action of thousands of dynein motors bound to doublet microtubules into a single propulsive waveform. Here, we use two ...In motile cilia, a mechanoregulatory network is responsible for converting the action of thousands of dynein motors bound to doublet microtubules into a single propulsive waveform. Here, we use two complementary cryo-EM strategies to determine structures of the major mechanoregulators that bind ciliary doublet microtubules in Chlamydomonas reinhardtii. We determine structures of isolated radial spoke RS1 and the microtubule-bound RS1, RS2 and the nexin-dynein regulatory complex (N-DRC). From these structures, we identify and build atomic models for 30 proteins, including 23 radial-spoke subunits. We reveal how mechanoregulatory complexes dock to doublet microtubules with regular 96-nm periodicity and communicate with one another. Additionally, we observe a direct and dynamically coupled association between RS2 and the dynein motor inner dynein arm subform c (IDAc), providing a molecular basis for the control of motor activity by mechanical signals. These structures advance our understanding of the role of mechanoregulation in defining the ciliary waveform.
History
DepositionAug 19, 2020-
Header (metadata) releaseDec 16, 2020-
Map releaseDec 16, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.018
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.018
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7ju4
  • Surface level: 0.018
  • Imaged by UCSF Chimera
  • Download
  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7ju4
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22481.png

Downloads & links

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Map

FileDownload / File: emd_22481.map.gz / Format: CCP4 / Size: 2.1 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.403 Å
Density
Contour LevelBy AUTHOR: 0.018 / Movie #1: 0.018
Minimum - Maximum0.0 - 0.17338881
Average (Standard dev.)0.000104659746 (±0.0013935497)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions832832832
Spacing832832832
CellA=B=C: 1167.296 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.4031.4031.403
M x/y/z832832832
origin x/y/z0.0000.0000.000
length x/y/z1167.2961167.2961167.296
α/β/γ90.00090.00090.000
start NX/NY/NZ1081340
NX/NY/NZ13584349
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS832832832
D min/max/mean0.0000.1730.000

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Supplemental data

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Mask #1

Fileemd_22481_msk_1.map
Projections & Slices
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Mask #2

Fileemd_22481_msk_2.map
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Mask #3

Fileemd_22481_msk_3.map
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Mask #4

Fileemd_22481_msk_4.map
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Additional map: #1

Fileemd_22481_additional_1.map
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Additional map: #3

Fileemd_22481_additional_2.map
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Additional map: #4

Fileemd_22481_additional_3.map
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Additional map: #2

Fileemd_22481_additional_4.map
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Sample components

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Entire : Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with do...

EntireName: Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule
Components
  • Complex: Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule
    • Protein or peptide: Dynein regulatory complex subunit 4
    • Protein or peptide: Dynein regulatory complex protein 1
    • Protein or peptide: Dynein regulatory complex subunit 2
    • Protein or peptide: Unknown protein
    • Protein or peptide: Tubulin beta
    • Protein or peptide: Tubulin alpha
    • Protein or peptide: Flagellar-associated protein 59
    • Protein or peptide: Flagellar-associated protein 172
    • Protein or peptide: Radial spoke protein 3
    • Protein or peptide: Radial spoke protein 7
    • Protein or peptide: Radial spoke protein 11
    • Protein or peptide: Dynein 8 kDa light chain, flagellar outer arm
    • Protein or peptide: Radial spoke protein 15
    • Protein or peptide: FAP207
    • Protein or peptide: Radial spike protein 8
    • Protein or peptide: FAP253
    • Protein or peptide: Actin
    • Protein or peptide: 28 kDa inner dynein arm light chain, axonemal
    • Protein or peptide: CFAP91 domain-containing protein
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with do...

SupramoleculeName: Complex of radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#19
Source (natural)Organism: Chlamydomonas reinhardtii (plant)

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Macromolecule #1: Dynein regulatory complex subunit 4

MacromoleculeName: Dynein regulatory complex subunit 4 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 55.207887 KDa
SequenceString: MAPKKKGTKK ESKKDAVATG DIEGASVEEL NQKIGTLEKE KNKEEEYRNY MQLERDKINA FWEITKKDLE DRRAELRNKD REMEEMEER HQVEIKVYKQ KVKHLLYEHQ NNITTLKSDG ELALKLQQDE YRKREGDLGK DKRNLKLELK EQELAHQDII R QLKLEHAK ...String:
MAPKKKGTKK ESKKDAVATG DIEGASVEEL NQKIGTLEKE KNKEEEYRNY MQLERDKINA FWEITKKDLE DRRAELRNKD REMEEMEER HQVEIKVYKQ KVKHLLYEHQ NNITTLKSDG ELALKLQQDE YRKREGDLGK DKRNLKLELK EQELAHQDII R QLKLEHAK EITKLRQEFE QQAKDLQSKY EKKMKMLRDD MELRRKQEIH EIEERKNTHI NELMKKHERA FAEIKNYYND IT HNNLDLI KTLKEDVAEM KRREAANEKL MYEIAQDNKK LSEPLSRALK EVELLRQQLA NYDKDKLSLA QTKARLLNAE RQI KNLEWE NEVLSQRFSK VQTERDELYG KFEASIYDVQ QKTGLKSALL EKKVEALGEA LEMKEAQLAE VLTAANLDPG TLAA INQRL EEVLDNKNQI IKALQYDVAK VSKAHNDLIR VYEAKLTEFG IPVDELGFRP LVTNTSTGPA GLVVGA

UniProtKB: Dynein regulatory complex subunit 4

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Macromolecule #2: Dynein regulatory complex protein 1

MacromoleculeName: Dynein regulatory complex protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 79.454133 KDa
SequenceString: MDELQSQTER EARILARRKR IQERLAALRE GDHGGGKEGE NKEEIGKGKQ QIIESKRRLM RVKYRTDQDV SSVRVAGDDR ENQHRIQEE QTRQDLRAKL LAEAEQSARQ NAAVAMRWAD LFSIEVPQDL YNEIESQRQA CERIIASKDK LIGEIKGELK K KDDEFVKT ...String:
MDELQSQTER EARILARRKR IQERLAALRE GDHGGGKEGE NKEEIGKGKQ QIIESKRRLM RVKYRTDQDV SSVRVAGDDR ENQHRIQEE QTRQDLRAKL LAEAEQSARQ NAAVAMRWAD LFSIEVPQDL YNEIESQRQA CERIIASKDK LIGEIKGELK K KDDEFVKT LKRQAEDIDT LLQYMSRQFV EVQNAYKEEL DEIENAFLQE RSDLLESNRR EMQELFDKRS RLEQDFMDRY LA AVEAYQS QLEGHRQMDA EEYHILKIRL ETDIQNLEQH LEAMRATYQL NTEKLEYNYR VLKEREKENT QTIESQKKKL SRQ RDILSS LKQRYAETDR RYRDDNMKLT DEYKRITEQF KDLQSKFRHF ELVDTKKYKE VWGMKEADVA ALVRQLLQAD KVLH EQQLG WDWRPPDDAV FAPVHGDAGS GGGAAAAATG GAAGGAAAAG GVGPNGEEES EEDAAARVRE AELAERLRDG RNWGA LGLL CDEAGFLIDI KARNMIERLP KDEQGQVKAE AILRSLGIAD GSAFDALLEA LSADSNIELR AKGMVAPQGR GMAEEK SDR GGTAVLVHPD EAVRRLKAFV EVYGTGPSRG PGGGGGGGGG MSGPMRVQGA MRRAAEREQE FWSRMTHVIS DKHTRVW GA LEKQLEKYLA LLQERAGSLR DVESLQHQNN ELRALLNQYL SSRINDELQI PPTQII

UniProtKB: Dynein regulatory complex protein 1

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Macromolecule #3: Dynein regulatory complex subunit 2

MacromoleculeName: Dynein regulatory complex subunit 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 64.986242 KDa
SequenceString: MVKAGKKVKG ASKVRENETE EEKKIRLEME ALAADEAERK AQEAARVALR ERQLREQRYA HLNGIKIHNQ WRKIMRMAKV EELRREIEI LSQNHEREVD RKDAIMQMLD RDLEEAEEQY SLAVRSHMLV VDNLLDLQYQ RMRALEAEFA ADLKALEDEF E TERTEIVN ...String:
MVKAGKKVKG ASKVRENETE EEKKIRLEME ALAADEAERK AQEAARVALR ERQLREQRYA HLNGIKIHNQ WRKIMRMAKV EELRREIEI LSQNHEREVD RKDAIMQMLD RDLEEAEEQY SLAVRSHMLV VDNLLDLQYQ RMRALEAEFA ADLKALEDEF E TERTEIVN AHTRQRKDMG DMIAAMEGEF ADAEAELRQE YEAQREEIKN RNSEEYNVLK IQLEGIIEEL EKSFELAHRA YL ESTEHRT NTFRTLTKDD AKAALKIERQ MRKLVRLQEA LQHWRTKIAT NGREWEERNR ALRNEKEIMA RHYAKLKSSM DAF RAGQAE RLKQLSLASS GAMETLRGKL AVAENVLKLA ELARKYETEQ EKVLPFWNPA QAVPSGEQGD EEAAAQAEAE AAAL EPSAA ELGELGLRAS MPEDSSKEAP GPSKSSAGPG KPKFSSYGLD PSSGSEVDEW DYLNCFFRRY NKALLDKTAI DKEKS RLER ENADLRSILK QYLDGISVND DVLNNPVNPL LVVNNRLQIT LTERNKARAA AMAQRAAAAT GAGLSVTGQG AGGGGQ KQL VEVQVVSRVS

UniProtKB: Dynein regulatory complex subunit 2

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Macromolecule #4: Unknown protein

MacromoleculeName: Unknown protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 6.145567 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #5: Tubulin beta

MacromoleculeName: Tubulin beta / type: protein_or_peptide / ID: 5 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 49.665809 KDa
SequenceString: MREIVHIQGG QCGNQIGAKF WEVVSDEHGI DPTGTYHGDS DLQLERINVY FNEATGGRYV PRAILMDLEP GTMDSVRSGP YGQIFRPDN FVFGQTGAGN NWAKGHYTEG AELIDSVLDV VRKEAESCDC LQGFQVCHSL GGGTGSGMGT LLISKIREEY P DRMMLTFS ...String:
MREIVHIQGG QCGNQIGAKF WEVVSDEHGI DPTGTYHGDS DLQLERINVY FNEATGGRYV PRAILMDLEP GTMDSVRSGP YGQIFRPDN FVFGQTGAGN NWAKGHYTEG AELIDSVLDV VRKEAESCDC LQGFQVCHSL GGGTGSGMGT LLISKIREEY P DRMMLTFS VVPSPKVSDT VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLT TPTFGDLNHL ISAVMSGITC CL RFPGQLN ADLRKLAVNL IPFPRLHFFM VGFTPLTSRG SQQYRALTVP ELTQQMWDAK NMMCAADPRH GRYLTASALF RGR MSTKEV DEQMLNVQNK NSSYFVEWIP NNVKSSVCDI PPKGLKMSAT FIGNSTAIQE MFKRVSEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDASAEEEGE FEGEEEEA

UniProtKB: Tubulin beta-1/beta-2 chain

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Macromolecule #6: Tubulin alpha

MacromoleculeName: Tubulin alpha / type: protein_or_peptide / ID: 6 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 49.638008 KDa
SequenceString: MREVISIHIG QAGIQVGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK HVPRCIFLDL EPTVVDEVRT GTYRQLFHP EQLISGKEDA ANNFARGHYT IGKEIVDLAL DRIRKLADNC TGLQGFLVFN AVGGGTGSGL GSLLLERLSV D YGKKSKLG ...String:
MREVISIHIG QAGIQVGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK HVPRCIFLDL EPTVVDEVRT GTYRQLFHP EQLISGKEDA ANNFARGHYT IGKEIVDLAL DRIRKLADNC TGLQGFLVFN AVGGGTGSGL GSLLLERLSV D YGKKSKLG FTVYPSPQVS TAVVEPYNSV LSTHSLLEHT DVAVMLDNEA IYDICRRSLD IERPTYTNLN RLIAQVISSL TA SLRFDGA LNVDITEFQT NLVPYPRIHF MLSSYAPIIS AEKAYHEQLS VAEITNAAFE PASMMVKCDP RHGKYMACCL MYR GDVVPK DVNASVATIK TKRTIQFVDW CPTGFKCGIN YQPPTVVPGG DLAKVQRAVC MISNSTAIGE IFSRLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDL AALEKDFEEV GAESAEGAGE GEGEEY

UniProtKB: Tubulin alpha-1 chain

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Macromolecule #7: Flagellar-associated protein 59

MacromoleculeName: Flagellar-associated protein 59 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 105.504469 KDa
SequenceString: MANIDPYRTE EELVEDDEEV DMSFLPPFAK GTENEVLYVE NARMERRLER TERALETNMD RLHIMDEHLK NVQQELKYTQ TRVEAKNKE IESEKHLNAM AEREMGRLKK DIGKMEAERQ ELADKINGLQ NQIYKNNEKL DQFKMLMNWN QEELEQWALA E RQKAEDNA ...String:
MANIDPYRTE EELVEDDEEV DMSFLPPFAK GTENEVLYVE NARMERRLER TERALETNMD RLHIMDEHLK NVQQELKYTQ TRVEAKNKE IESEKHLNAM AEREMGRLKK DIGKMEAERQ ELADKINGLQ NQIYKNNEKL DQFKMLMNWN QEELEQWALA E RQKAEDNA ALEKYRHADD GKVKELTLAL ERVSKQVVGR KEELEAEVVE TQAAQIQLDK AAEDFRKLHV ERQDLIRQWE EA VEAMRHR DAAIAAASEQ FAMQKDVLRE RKRELDAQAR FLENETLNTK EADARVAYYE REVGKQRDVL AREQARTEEL NNQ VELVKA TLSKAATELA QRTVENKQAR EDLDAKRQKL DAARKRFVVL KRKLENEFGN LDSMEAKASE LEAMRRGEEA RLKA ILKEH ELLKKEQYKR SQVLFDLRQK ERELISEISG GQGQNKNLAA RIHALDEQVV RQQELLYNVE FQLQQMERKV ARAGG VRSE EETRALNARI EKLTAILEGV NAEYSMLLEQ VKRAEDDLLA ARRANTSLRA DRAKLDETIS TLKLENDMVS RQVKGS VEA REKALVDHDV LALEVKRLRD ILAAHADEVF SLENRKQQLA LSMEERKQEV EVHRDGLRAE LRLLREDVHR ITLELKE RL LRCEKLQAKF EIISAKHRGS GEDDGEERTQ AYYVIKAAQE REALQREGDD LDGRIRVAEK EVAALEATLA QLMAVNTN F AASYKKVGSK EAFEERAALR DKLDKAYDKL KARRADEAAI AGDIQVSEAR LSNLGQEQRS LQALVDDMTR RKAEAQRQL DEQREKLGRA LGRTDKLRQK LGLANSPQGA DVELAEVRDV TRAMLLELKA LALANPGAMI AEACEAAGIR LPSGGSNPPS LGGSRPGSA RSQTSLGSVR SARSVASQQR GGMGGSPAVR TIQLGA

UniProtKB: Flagellar-associated protein 59

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Macromolecule #8: Flagellar-associated protein 172

MacromoleculeName: Flagellar-associated protein 172 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 101.385719 KDa
SequenceString: MADPMDQPST SDPVDNQIFG EQGGLRPDHP LLRRAQEALK VQFEANRTRL QEELREKANA LKQAKARREA LGVELYGFQQ NLAKLQLNL ETTHQNYQVI NRARQQCEDQ LNQLKQQLSL EEGDTKGERS RVEKFQLEMD RLGATLKQVE EYNEAMKGEI A VTRRAAYA ...String:
MADPMDQPST SDPVDNQIFG EQGGLRPDHP LLRRAQEALK VQFEANRTRL QEELREKANA LKQAKARREA LGVELYGFQQ NLAKLQLNL ETTHQNYQVI NRARQQCEDQ LNQLKQQLSL EEGDTKGERS RVEKFQLEMD RLGATLKQVE EYNEAMKGEI A VTRRAAYA AEEAVQKLEK QKMEQDFRID TLQDNLKGTQ QQLALVSAQL EAQKRETRAA LETLAEAEAE MENVHFEKKQ LV AQWKSSL LAIQKRDEAL SAIQDGMREQ QQQELSLVLE IEGYKKDVVR EQLKHESLTA VVRKVEGDAV FVQKQIEGAQ ERQ ARLQEI LAKLAKSLEH TEAEVLRVNS EKKALQGEAD AVDRAITKVA AEGRAIEEEM LSALSDQTTA EKATSKTAAD TQEL RKRIR AEELAVVETE NELAKLQVDI LNTEAHNSRL GETLGLLDEE LRDKGRTIEK YELEIKRRND EIEKKTREID ILNRR FERM LEQRGTGEET GPLEATIKNL GREIDTKGSE SKELQRRWIG CQQELVGLQN ENGGLTETLA RLRAEHTVLF QKKRRL EQQ LEGQGKAIKG LTSAMGRLHV DLTRVNGLIA ANSAARQALA EDNFNLEGRI MGDLRAMEEE AARLNSQIEE GRGAKRD TL AEIVEAERQI MLWERKIQLE KEMQEVLDPT VGQDVVAEMK KEIHRMTLRH TELMRLQEKL VSDMEKALTK REIISVKG R ATAAKSKSST PAGSATASSR ASPSASVASS TLTRNQLDRA TTDLAKSIKE TEREIVATEQ RLGALEQQRS AVSAAVAAA DGACLQLRGA EEALRLEAVS AVNARYGLLL ATARAQRTTK RLEDLEAGRY RPVVEDAAAV GEELGRAQDK LGRVVALLEG LRQAAPHLA GELDKVLCHV ADVRA

UniProtKB: Flagellar-associated protein 172

+
Macromolecule #9: Radial spoke protein 3

MacromoleculeName: Radial spoke protein 3 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 56.856688 KDa
SequenceString: MVQAKAQQQL YTHAAEPKAV QQRRAKYRED ETTQTLPTAN IMFDRRVVRG NTYAARILPA DATQTQTKGP SPASTKKRTT RTLPPRTPE AVDGRRHIDI QTDVYLEELT DTVPEADTST QTDAFLDRPP TPLFVPQKTG TDAITQIENG DLFDFDFEVE P ILEVLVGK ...String:
MVQAKAQQQL YTHAAEPKAV QQRRAKYRED ETTQTLPTAN IMFDRRVVRG NTYAARILPA DATQTQTKGP SPASTKKRTT RTLPPRTPE AVDGRRHIDI QTDVYLEELT DTVPEADTST QTDAFLDRPP TPLFVPQKTG TDAITQIENG DLFDFDFEVE P ILEVLVGK VLEQGLMEVL EEEELAAMRA HQEHFEQIRN AELVATQRME AAERRKLEEK ERRMQQERER VERERVVRQK VA ASAFARG YLSGIVNTVF DRLVSSGYIY DPVMREVETA FMPWLKEQAI GYLARGVVAR RVVDKLVEDA AAALAANRST LAD KAASTA ATVDAWAERQ AKMEAELQGK ELEAVRRRPT FVLRELKPAV ASADAVEAAA AELTAQAEEA ANAKWEADKA EAAE KARAE AEAAAEEQKA LLEELAATAA AEAEERGEEP PAEPPSLPDG VEPVDVEAEV AKAVEAVPKP PVKEVTDIDI LSYMM DKGA ITKDAIIQAL AVHALGDKAY TNHPAFAEAE GA

UniProtKB: Uncharacterized protein

+
Macromolecule #10: Radial spoke protein 7

MacromoleculeName: Radial spoke protein 7 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 54.781898 KDa
SequenceString: MSSTYQKPIT IPGDFPAILK AFTREILRAQ PSNIYEFGAR YFSGLQGQAE PEGLGRAAPV EPASTSHAAT SKATDVEETA VMFDIAALT PAELEPILMK LFIEADADRS GFLDRHEFTA VLRNANLKLS DRQIRQILAE ADENDDDVIQ YKEFLPIMVD I LQSIKAKE ...String:
MSSTYQKPIT IPGDFPAILK AFTREILRAQ PSNIYEFGAR YFSGLQGQAE PEGLGRAAPV EPASTSHAAT SKATDVEETA VMFDIAALT PAELEPILMK LFIEADADRS GFLDRHEFTA VLRNANLKLS DRQIRQILAE ADENDDDVIQ YKEFLPIMVD I LQSIKAKE QAKAMMHGVE TMVRTEVETM LLHGLPQEEL QALMLKVFKK ADADGSGQLN RHEFKEALKA AELGLTRKDI NL ILSHIDV DRDGLVSYEE FIPVCFQVLV ERFKDEIVVN DILGNADELQ QMLLGAFRDA DPDNTGLLSQ RQVKSIFKEL SYK ALGLTT LQMVSLISQA PTTPDGMVQY IQFVPQAASI IRSMYDVETM KGRMHAIKAV AEAGGIAALG ALDLDQLRGV LEQA FQRVD TEGAGQLTLP QVTQVLDGLN SLAPDANLAL SDQHMKAMFA AIDADESGTV DWTELVNFIC DALEHIEREA YVANM RDGG AGGAGEAEAS PGDEEA

UniProtKB: EF-hand domain-containing protein

+
Macromolecule #11: Radial spoke protein 11

MacromoleculeName: Radial spoke protein 11 / type: protein_or_peptide / ID: 11 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 21.504635 KDa
SequenceString: MDVEPIFCAE QIVIPHNLAD ILKAYTKEVI RRQPTDLIAF SAKYFTNLAN VASGVSNSSA PAKEQLRQVY TRGGSGGATL TESQVTGLC QQAGIADAVV AKVMEVGAFT PAAVDLSKFV FLCLAMSCED FNRVCMGVFD VFSDNGSLPA QDLLTLIAHL G PDMDPEVT ...String:
MDVEPIFCAE QIVIPHNLAD ILKAYTKEVI RRQPTDLIAF SAKYFTNLAN VASGVSNSSA PAKEQLRQVY TRGGSGGATL TESQVTGLC QQAGIADAVV AKVMEVGAFT PAAVDLSKFV FLCLAMSCED FNRVCMGVFD VFSDNGSLPA QDLLTLIAHL G PDMDPEVT PAFLDAVAAE LPAGGGAVTY MELCEAPSLK PKLGLS

UniProtKB: Radial spoke protein 11

+
Macromolecule #12: Dynein 8 kDa light chain, flagellar outer arm

MacromoleculeName: Dynein 8 kDa light chain, flagellar outer arm / type: protein_or_peptide / ID: 12 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 10.336775 KDa
SequenceString:
MASGSSKAVI KNADMSEEMQ ADAVDCATQA LEKYNIEKDI AAYIKKEFDR KHNPTWHCIV GRNFGSYVTH ETKHFIYFYL GQVAILLFK SG

UniProtKB: Dynein 8 kDa light chain, flagellar outer arm

+
Macromolecule #13: Radial spoke protein 15

MacromoleculeName: Radial spoke protein 15 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 35.302625 KDa
SequenceString: MQVFALCEAL YEYSGLAVLR LPYNFLNDMA AQAVARLMQV NPGLQLLDLT GNEVTDKGAA AITEVLAKPE AGLKALILRH NPIGDTGAL AVADMLRSNR SLTLLDLADC HVAVKGLIGL ANALTAPEGN RSLQVLDLED AQLAAPQDST YQHMSRMLAT N TTLTELSL ...String:
MQVFALCEAL YEYSGLAVLR LPYNFLNDMA AQAVARLMQV NPGLQLLDLT GNEVTDKGAA AITEVLAKPE AGLKALILRH NPIGDTGAL AVADMLRSNR SLTLLDLADC HVAVKGLIGL ANALTAPEGN RSLQVLDLED AQLAAPQDST YQHMSRMLAT N TTLTELSL AKCRLVDSQL ELLTTYGFAR SSARWSSLSL RANRLSPFSG PTLERLLALP ALCRLQRLTL ASNSLGNDGA SA LARVLPT ACPDIRELDL RSNGIGDVGL LALAAALPLV NSLELLLLWG NSFSPASSRA VAEALAAPAL RRLRSDLRPY VVD GEVALA LQEVE

UniProtKB: Flagellar associated protein

+
Macromolecule #14: FAP207

MacromoleculeName: FAP207 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 28.41841 KDa
SequenceString: MPPNIPGTLT AESLRRKQGD QLWKTSDQKA QKEGPHHTVY WTTGERYQGS WKDNKKHGKG TVIYKNSDKY EGDWANDMRH GLGTLWLYR DGKYVVRYNG EWRADQPTGH GTFFADNGDT YEGEWLNGRR HGKGRAVYGG RPVDGFGGDV YEGYFENDVK C GPGTMMYA ...String:
MPPNIPGTLT AESLRRKQGD QLWKTSDQKA QKEGPHHTVY WTTGERYQGS WKDNKKHGKG TVIYKNSDKY EGDWANDMRH GLGTLWLYR DGKYVVRYNG EWRADQPTGH GTFFADNGDT YEGEWLNGRR HGKGRAVYGG RPVDGFGGDV YEGYFENDVK C GPGTMMYA NGDVYEGLWA ADKKNGTGTY FYMSKGKRFD GVWADGAIKC GTYSEIHAPP PGTPGALPPC ELRNPDKVLA EA TMEASEA ATEAAARGL

UniProtKB: MORN repeat-containing protein 3

+
Macromolecule #15: Radial spike protein 8

MacromoleculeName: Radial spike protein 8 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 40.537438 KDa
SequenceString: MQSHSSRHVV SEHLKDLHPD LSEPFPKHVI EDEVAEAHGR RAIPKLVAVL ALPELPDDQR AHALRVLNGL LSTQEHKTNA VAEGAAPPL CQLASQCRDD EVRRLSCSAL ASLGQVMAGR NGIVAAGGLP VLTEALQTTP EQAAAALKSF AASNDGAAQL N LERAAIVP ...String:
MQSHSSRHVV SEHLKDLHPD LSEPFPKHVI EDEVAEAHGR RAIPKLVAVL ALPELPDDQR AHALRVLNGL LSTQEHKTNA VAEGAAPPL CQLASQCRDD EVRRLSCSAL ASLGQVMAGR NGIVAAGGLP VLTEALQTTP EQAAAALKSF AASNDGAAQL N LERAAIVP ALVTLLSQPT DPAFTLTAFS NALSTLEGMT RTDDGVLAAL DGGVPACLVA LARRGLEGDL KFEGRLMELL QL VATCLEQ ICHHADGKAA CRQAEAHKVL AELLTLQHRE IIKHAAAALM GLAVEKESKV NVMLYAGVSL VRLMRGSDAE LAA NARDTV AAAAEHLEAR RTAEMLLSME ERELLLWRGP PPETPPDYRY HVDLPKFTPQ AK

UniProtKB: Radial spike protein 8

+
Macromolecule #16: FAP253

MacromoleculeName: FAP253 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 75.037945 KDa
SequenceString: MSDPEAEQGE QGYEESPEEP GPGSEAPSPS RIDNGLDTII DIDPQTQHAE EGSNTAYESE QPDVISSYTG GQQEEDGEQA GNGAIDETT EEAAGEADDG GKASGFAVEV DAGTDAAAEG DLEPEPEPER PASASGEPQP TASTSRPASG AAARPASARP T SARPGSAA ...String:
MSDPEAEQGE QGYEESPEEP GPGSEAPSPS RIDNGLDTII DIDPQTQHAE EGSNTAYESE QPDVISSYTG GQQEEDGEQA GNGAIDETT EEAAGEADDG GKASGFAVEV DAGTDAAAEG DLEPEPEPER PASASGEPQP TASTSRPASG AAARPASARP T SARPGSAA PRQPSASGGS RPGSGHPVNL APDSVGLAQQ QQQKSQIEVG AQAYEARGSS RPQSGGDAYG QAEEASAAAA AG RPSTSQS GSRPPPSREG VAVVPSIPED QPLAVPIHIE RYIAPGLKAI EVEVAQGPGM PHRLVRVLLD YTQCDAKPYL GGF RNKRTG AVYHHGATQT PRAPKYSEAD RKLSRETQTV KIKQHSQQTV REQATQMARP GVLLDNDYDK EVTPGRYQTA DERD EIVLR STLRIQRWVR GWLGRKRAAY LRGKKMEREA FLRDQEARAQ SEAEEHRRRE IQRRMHPRTA ADFEVLYNEL EAWRL QETR KIKEAGLAKE QEQQVLQQLL HKETKLLQTI DRLKINANQE NKEARIQHTL NEMSKPKKFA LRNGGKVDVH TPFTTR AKE LQQLYNGLNL PLLTVDERLD VLLHVKWTVK EFDCDLTREL VDLIDREADL LNRGRNPKML EGLRKRISSL FLNFIET PE FNPEAVRFQI VPMDFEAYLY EQVGKATAKA GTSVGTRTLS

UniProtKB: IQ and ubiquitin-like domain-containing protein

+
Macromolecule #17: Actin

MacromoleculeName: Actin / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 41.881984 KDa
SequenceString: MADEGEVSAL VCDNGSGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDSYVGDEA QSKRGILTLR YPIEHGIVTN WDDMEKIWH HTFFNELRVA PEEHPVLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHTVPIY ...String:
MADEGEVSAL VCDNGSGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDSYVGDEA QSKRGILTLR YPIEHGIVTN WDDMEKIWH HTFFNELRVA PEEHPVLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLDSGD G VTHTVPIY EGYALPHAIL RLDLAGRDLT DYLMKILMER GYSFTTTAER EIVRDIKEKL CYVALDFEQE MATALSSSAL EK TYELPDG QMITIGNERF RCPEVLFNPN MIGMEAVGIH DTTFNSIMKC DVDIRKDLYN NIVLSGGTTM FPGIADRMSK EIT ALAPSA MKIKVVAPPE RKYSVWIGGS ILASLSTFQQ MWIAKSEYDE SGPSIVHRKC F

UniProtKB: Actin

+
Macromolecule #18: 28 kDa inner dynein arm light chain, axonemal

MacromoleculeName: 28 kDa inner dynein arm light chain, axonemal / type: protein_or_peptide / ID: 18 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 28.691717 KDa
SequenceString: MIPPLSSLVR YDNPVLVSTS KDKGKGAKGT PGKKGALPPV EQKPGLTQTE DILNSILPPR EWTEDGQLWV QYVSSTPATR LDVINLQEK LDQQLQQRQA RETGICPIRE ELYAQTFDEL IRQVTINCAE RGLLLLRVRD EMRMTIAAYQ TLYESAVAFG I RKALQTEQ ...String:
MIPPLSSLVR YDNPVLVSTS KDKGKGAKGT PGKKGALPPV EQKPGLTQTE DILNSILPPR EWTEDGQLWV QYVSSTPATR LDVINLQEK LDQQLQQRQA RETGICPIRE ELYAQTFDEL IRQVTINCAE RGLLLLRVRD EMRMTIAAYQ TLYESAVAFG I RKALQTEQ GKSEMESRIT QLEGDVKDLE RQVQEWKFKC EAIEKRESER REVEAKKHKD EVAYLENYAK QLKQQLETFL VP AKKGAPG APAAAT

UniProtKB: 28 kDa inner dynein arm light chain, axonemal

+
Macromolecule #19: CFAP91 domain-containing protein

MacromoleculeName: CFAP91 domain-containing protein / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 134.440578 KDa
SequenceString: MAQPQRPYDA LYDPNFTVAG PRDHYRQQTM AGGFNIERAP VYNNFFSELP HHPPSTLRLK NADRVPAFVD RNYRPAANDP NDTRQRSDA LAVSGPNRPK YFRRPMLAAA EIHIKQAPPS QLPPLPSHQD LNATAPAAMG GAGGLGEPRS KTIGTQSDYR E NEAQTAPW ...String:
MAQPQRPYDA LYDPNFTVAG PRDHYRQQTM AGGFNIERAP VYNNFFSELP HHPPSTLRLK NADRVPAFVD RNYRPAANDP NDTRQRSDA LAVSGPNRPK YFRRPMLAAA EIHIKQAPPS QLPPLPSHQD LNATAPAAMG GAGGLGEPRS KTIGTQSDYR E NEAQTAPW EPGYVLPAPG ALTAKQAALM RRYHTDVPEV LQLKDLAFPD GLPAGLQEVT RIDKMRAKRA FEASLPPIDD VA RLPLRQR MIEEWEAKEW EEREQEILSI QDKRLELLDN ALQVREEELD DENRLRVEAR KEAMLAGRAG KFADVQATRI KTM RQLIEN RKYVEKHRKL HKPTIVERYA NYGSGTYAPL QREGRFPESK PLGKEIETEG YAPVTLKGVV DLESFLPSRL LNPR VAAPQ KPARLDYHQR KEAAVQRDLK AINDLLDTAK GTAGRGFGDC WPAPLQDDGG AGMGNGTLGR ATSTVGKGTL GAGGS AGGA APGGASMALL GGPSTAAASA MGPLASGVSG SPSRRVVRAI ERPPTPELPQ PPAVTAPQHA AVVLLQRLLR GRAAQN IMY EGRVRRQELI DELRLEEVVS ADGTKIDGQP IRRPEHRDTA TLRIDALVGS AVAEVAAILA ETDPERRETL LAGLDVS RA HATAAAVAAA AADINASARA EAEEAAATAM AEAAAAAAAA AAAAAAAEDG GAEGAAESAA EAAAAAEAAA SAAEEAYA G AVAAAAAPAR AAALNLEALG ISPEEAEEAA VRIQAAFKGH KARKEVAAMR ARGEMLRNIM ANGDEAKVVT CQAAIRGHL ARKRVRQLRA SQAGNEGFAG APSASPEPAA PLPALAENQD QQEPQPQPQP SSSSGALDLA DYDDHHVAAV TRIQAAQRGR IARKRAAAM RTELEEQLAT AAALVATSAA SEGTRLASGR SEPNSEGRSD GGSARGGASR APPPTAAVNP DAFQDQYTAE Q EAAVIKIQ AFGRGMIARK RVGRLKGRSS EEGAGDVLVV APEPSANFGG QGEAAAEASA AEAQQQEEQE LWPSVKALPG VA QAVAARM AHEPTLTEVR PEGEAAAAAE GEGEGVEQSE AGPAPEVEAD LEPEAQEEGA EGEPQPEGEG APADPAAEAE FSL AGGGFA EGDGGAAAQG EASAAMLGGE PSLAVGGSRE GEQQLEADAE AEAEAEAEAE AGAEAEASAQ AGAEAEAEAG VEAE AEASA GAEASVGAGA EGDAEAETEA GAQAEPGPEA EAEAEAGAEA EAENGAEAEA RLGGEEEGFR EGEGQGGAAA GEAGP GGEL AEGEGEAGEG EAAE

UniProtKB: Cilia- and flagella-associated protein 91

+
Macromolecule #20: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 20 / Number of copies: 14 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

+
Macromolecule #21: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 21 / Number of copies: 14 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

+
Macromolecule #22: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 22 / Number of copies: 14 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #23: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 23 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

-
Sample preparation

BufferpH: 7.4
GridPretreatment - Type: GLOW DISCHARGE / Details: unspecified
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-30 / Average exposure time: 9.0 sec. / Average electron dose: 38.9 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: OTHER
Details: Initial model was extracted from the doublet microtubule attached density in our dataset
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 202168
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)

-
Atomic model buiding 1

RefinementSpace: REAL
Output model

PDB-7ju4:
Radial spoke 2 stalk, IDAc, and N-DRC attached with doublet microtubule

+
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