EMDB-17873: Composite structure of Dynein-Dynactin-JIP3-LIS1

Basic information

Entry

Database: EMDB / ID: EMD-17873

• Title: Composite structure of Dynein-Dynactin-JIP3-LIS1
• Map data: Composite map of Dynein-Dynactin-JIP3-LIS1 filtered to 10 angstrom resolution

Sample

• Complex: Composite structure of Dynein-Dynactin-JIP3-LIS1
  • Complex: Dynactin subunits
    • Protein or peptide: x 11 types
  • Complex: Dynein and JIP3
    • Protein or peptide: x 8 types
• Ligand: x 5 types

• Keywords: Dynein / AAA-Atpase / p150 / LIS1 / MOTOR PROTEIN / Dynactin / JIP3

Function / homology

Function:

intracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / ameboidal-type cell migration / microtubule cytoskeleton organization involved in establishment of planar polarity / establishment of planar polarity of embryonic epithelium / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / UCH proteinases / negative regulation of DNA strand resection involved in replication fork processing / 1-alkyl-2-acetylglycerophosphocholine esterase complex / RHOF GTPase cycle / Regulation of CDH1 Function / Formation of the dystrophin-glycoprotein complex (DGC) / Gap junction degradation / Formation of annular gap junctions / secretory vesicle / Clathrin-mediated endocytosis / dynactin complex / centriolar subdistal appendage / corpus callosum morphogenesis / negative regulation of phosphorylation / maintenance of centrosome location / centriole-centriole cohesion / visual behavior / intraciliary retrograde transport / platelet activating factor metabolic process / positive regulation of neuromuscular junction development / radial glia-guided pyramidal neuron migration / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / microtubule anchoring at centrosome / establishment of centrosome localization / acrosome assembly / cerebral cortex neuron differentiation / Recruitment of mitotic centrosome proteins and complexes / nuclear membrane disassembly / central region of growth cone / F-actin capping protein complex / WASH complex / anterograde axonal protein transport / microtubule sliding / dynein light chain binding / transport along microtubule / ventral spinal cord development / dynein heavy chain binding / motile cilium assembly / Activation of BIM and translocation to mitochondria / positive regulation of cytokine-mediated signaling pathway / microtubule organizing center organization / positive regulation of embryonic development / layer formation in cerebral cortex / retromer complex / cytoskeleton-dependent cytokinesis / interneuron migration / dynein complex / astral microtubule / auditory receptor cell development / microtubule plus-end / cortical microtubule organization / cellular response to cytochalasin B / Intraflagellar transport / positive regulation of microtubule nucleation / myeloid leukocyte migration / MAP kinase scaffold activity / reelin-mediated signaling pathway / positive regulation of intracellular transport / regulation of transepithelial transport / regulation of metaphase plate congression / positive regulation of spindle assembly / JUN kinase binding / positive regulation of dendritic spine morphogenesis / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / melanosome transport / osteoclast development / protein localization to adherens junction / negative regulation of nitric oxide biosynthetic process / establishment of spindle localization / regulation of G protein-coupled receptor signaling pathway / barbed-end actin filament capping / dense body / stereocilium / Neutrophil degranulation / Tat protein binding / microtubule plus-end binding / brain morphogenesis / coronary vasculature development

Domain/homology:

JNK-interacting protein, leucine zipper II / JNK-interacting protein 3/4 / JNK-interacting protein leucine zipper II / WD40 repeated domain / RH1 domain / RH2 domain / RILP homology 1 domain / RH1 domain profile. / RH2 domain profile. / Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / : / : / PAC1 LisH domain / Dynamitin / Dynamitin / Dynactin subunit 6 / : / Dynein associated protein / Dynein associated protein / Dynein 1 light intermediate chain / Dynein light chain Tctex-1 like / Dynactin subunit 5 / Tctex-1-like superfamily / Tctex-1 family / Dynein light chain roadblock-type 1/2 / Dynein family light intermediate chain / Dynein light intermediate chain (DLIC) / Cytoplasmic dynein 1 intermediate chain 1/2 / Cytoplasmic dynein 1 intermediate chain 2 / F-actin-capping protein subunit beta / Dynein regulator LIS1 / F-actin capping protein, beta subunit, conserved site / LIS1, N-terminal / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Dynein light chain, type 1/2, conserved site / Dynein light chain type 1 signature. / Dynein light chain, type 1/2 / Dynein light chain type 1 / Dynein light chain type 1 / Dynein light chain superfamily / : / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Lissencephaly type-1-like homology motif / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / LIS1 homology (LisH) motif profile. / LIS1 homology motif / : / Dynein heavy chain, ATPase lid domain / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / P-loop containing dynein motor region / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Trimeric LpxA-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site

Component:

Dynactin subunit 5 / Dynactin subunit 1 / Dynactin subunit 4 / Dynactin subunit 2 / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 6 / Dynactin subunit 3 / Alpha-centractin / Actin-related protein 10 / Cytoplasmic dynein 1 light intermediate chain 2 / Platelet-activating factor acetylhydrolase IB subunit beta / Dynein light chain 1, cytoplasmic / Dynein light chain Tctex-type 1 / Cytoplasmic dynein 1 intermediate chain 2 / Cytoplasmic dynein 1 heavy chain 1 / Actin, cytoplasmic 1 / Dynein light chain roadblock-type 1 / C-Jun-amino-terminal kinase-interacting protein 3

• Biological species: Sus scrofa (pig) / Homo sapiens (human)
• Method: single particle reconstruction / cryo EM / Resolution: 10.0 Å
• Authors: Singh K / Lau CK / Manigrasso G / Gassmann R / Carter AP

Funding support

United Kingdom, European Union, 3 items

Organization	Grant number	Country
Wellcome Trust	210711/Z/18/Z	United Kingdom
Medical Research Council (MRC, United Kingdom)	MC_UP_A025_1011	United Kingdom
European Molecular Biology Organization (EMBO)	ALTF 197-2021	European Union

• Citation: Journal: Science / Year: 2024; Title: Molecular mechanism of dynein-dynactin complex assembly by LIS1.; Authors: Kashish Singh / Clinton K Lau / Giulia Manigrasso / José B Gama / Reto Gassmann / Andrew P Carter / ; Abstract: Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation.

History

Deposition	Jul 14, 2023	-
Header (metadata) release	Mar 27, 2024	-
Map release	Mar 27, 2024	-
Update	Apr 10, 2024	-
Current status	Apr 10, 2024	Processing site: PDBe / Status: Released

Map

• File: Download / File: emd_17873.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Composite map of Dynein-Dynactin-JIP3-LIS1 filtered to 10 angstrom resolution
• Voxel size: X=Y=Z: 1.059 Å

Density

Contour Level	By AUTHOR: 0.0134
Minimum - Maximum	-0.015466937 - 0.111484736
Average (Standard dev.)	0.0017092265 (±0.0043441495)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 640 640 640 Spacing 640 640 640
Cell	A=B=C: 677.76 Å α=β=γ: 90.0 °

Supplemental data

Sample components

Entire : Composite structure of Dynein-Dynactin-JIP3-LIS1

• Entire: Name: Composite structure of Dynein-Dynactin-JIP3-LIS1

Components

• Complex: Composite structure of Dynein-Dynactin-JIP3-LIS1
  • Complex: Dynactin subunits
    • Protein or peptide: ARP1 actin related protein 1 homolog A
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Dynactin subunit 2
    • Protein or peptide: Dynactin subunit 3
    • Protein or peptide: Dynactin subunit 1
    • Protein or peptide: Capping protein (Actin filament) muscle Z-line, alpha 1
    • Protein or peptide: F-actin-capping protein subunit beta
    • Protein or peptide: Arp11
    • Protein or peptide: Dynactin 6
    • Protein or peptide: Dynactin subunit 5
    • Protein or peptide: Dynactin subunit 4
  • Complex: Dynein and JIP3
    • Protein or peptide: Cytoplasmic dynein 1 intermediate chain 2
    • Protein or peptide: Cytoplasmic dynein 1 light intermediate chain 2
    • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1
    • Protein or peptide: C-Jun-amino-terminal kinase-interacting protein 3
    • Protein or peptide: Dynein light chain roadblock-type 1
    • Protein or peptide: Platelet-activating factor acetylhydrolase IB subunit beta
    • Protein or peptide: Dynein light chain 1, cytoplasmic
    • Protein or peptide: Dynein light chain Tctex-type 1
• Ligand: ADENOSINE-5'-DIPHOSPHATE
• Ligand: ADENOSINE-5'-TRIPHOSPHATE
• Ligand: ZINC ION
• Ligand: MAGNESIUM ION
• Ligand: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

Supramolecule #1: Composite structure of Dynein-Dynactin-JIP3-LIS1

• Supramolecule: Name: Composite structure of Dynein-Dynactin-JIP3-LIS1 / type: complex / ID: 1 / Parent: 0 ; Macromolecule list: #2-#3, #7-#9, #5-#6, #17, #12, #15, #19, #16, #1, #4, #10-#11, #13-#14, #18

Supramolecule #2: Dynactin subunits

• Supramolecule: Name: Dynactin subunits / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2-#3, #7-#9, #5-#6, #4, #10-#11, #13
• Source (natural): Organism: Sus scrofa (pig)

Supramolecule #3: Dynein and JIP3

• Supramolecule: Name: Dynein and JIP3 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #16-#17, #15, #12, #19, #1, #14, #18
• Source (natural): Organism: Homo sapiens (human)

Macromolecule #1: Platelet-activating factor acetylhydrolase IB subunit beta

• Macromolecule: Name: Platelet-activating factor acetylhydrolase IB subunit beta; type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 46.709984 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR LQKKVMELES KLNEAKEEFT SGGPLGQKR DPKEWIPRPP EKYALSGHRS PVTRVIFHPV FSVMVSASED ATIKVWDYET GDFERTLKGH TDSVQDISFD H SGKLLASC SADMTIKLWD FQGFECIRTM HGHDHNVSSV AIMPNGDHIV SASRDKTIKM WEVQTGYCVK TFTGHREWVR MV RPNQDGT LIASCSNDQT VRVWVVATKE CKAELREHEH VVECISWAPE SSYSSISEAT GSETKKSGKP GPFLLSGSRD KTI KMWDVS TGMCLMTLVG HDNWVRGVLF HSGGKFILSC ADDKTLRVWD YKNKRCMKTL NAHEHFVTSL DFHKTAPYVV TGSV DQTVK VWECR

UniProtKB: Platelet-activating factor acetylhydrolase IB subunit beta

Macromolecule #2: ARP1 actin related protein 1 homolog A

• Macromolecule: Name: ARP1 actin related protein 1 homolog A / type: protein_or_peptide / ID: 2 / Number of copies: 8 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 42.670688 KDa

Sequence

String:

MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV PIYEGFAMPH SIMRIDIAGR DVSRFLRLYL RKEGYDFHSS SEFEIVKAIK ERACYLSINP QKDETLETEK AQ YYLPDGS TIEIGPSRFR APELLFRPDL IGEESEGIHE VLVFAIQKSD MDLRRTLFSN IVLSGGSTLF KGFGDRLLSE VKK LAPKDV KIRISAPQER LYSTWIGGSI LASLDTFKKM WVSKKEYEED GARSIHRKTF

UniProtKB: Alpha-centractin

Macromolecule #3: Actin, cytoplasmic 1

• Macromolecule: Name: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 41.78266 KDa

Sequence

String:

MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

Macromolecule #4: Arp11

• Macromolecule: Name: Arp11 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 46.250785 KDa

Sequence

String:

MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKKAGMPK PIKVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VVIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG KALHKELETQ LLEQCTVDTG AAKEQSLPSV MGSIPEGVLE DIKVRTCFVS DLTRGLKIQA AKFNIDGNTE RP SPPPNVD YPLDGEKILH VLGSIRDSVV EILFEQDNEE KSVATLILDS LMQCPIDTRK QLAENLVIIG GTSMLPGFLH RLL AEIRYL VEKPKYKKTL GTKTFRIHTP PAKANCVAWL GGAIFGALQD ILGSRSVSKE YYNQTGRIPD WCSLNNPPLE MVFD VGKSQ PPLMKRAFST EK

UniProtKB: Actin-related protein 10

Macromolecule #5: Capping protein (Actin filament) muscle Z-line, alpha 1

• Macromolecule: Name: Capping protein (Actin filament) muscle Z-line, alpha 1; type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 33.059848 KDa

Sequence

String:

MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEVDGSLKS WRESCDSALR AYVKDHYSNG FCTVYAKNID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPTAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSVTV SNEAQTAKEF IKIIEHAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

UniProtKB: F-actin-capping protein subunit alpha-1

Macromolecule #6: F-actin-capping protein subunit beta

• Macromolecule: Name: F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 30.669768 KDa

Sequence

String:

MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK LTSTVMLWLQ TNKSGSGTMN LGGSLTRQME KDETVSDCSP HIANIGRLVE DMENKIRSTL NEIYFGKTKD IV NGLRSVQ TFADKSKQEA LKNDLVEALK RKQQC

UniProtKB: F-actin-capping protein subunit beta

Macromolecule #7: Dynactin subunit 2

• Macromolecule: Name: Dynactin subunit 2 / type: protein_or_peptide / ID: 7 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 44.704414 KDa

Sequence

String:

MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELEEL TSTSVEHIIV NPNAAYDKFK DKRVGTKGLD FSDRIGKTKR TGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKMTVKES ATEEKLTPVV LAKQLAALKQ QLVASHLEKL L GPDAAINL TDPDGALAKR LLLQLEATKN TKGAGSGGKT TSGSPPDSSL VTYELHSRPE QDKFSQAAKV AELEKRLTEL EA TVRCDQD AQNPLSAGLQ GACLMETVEL LQAKVSALDL AVLDQVEARL QSVLGKVNEI AKHKASVEDA DTQSKVHQLY ETI QRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAC SLKDNATLLT QVQTTMRENL STVEGNFANI DERM KKLGK

UniProtKB: Dynactin subunit 2

Macromolecule #8: Dynactin subunit 3

• Macromolecule: Name: Dynactin subunit 3 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 21.192477 KDa

Sequence

String:

MAGVTDVQRL QARLEELERW VYGPGGSRGS RKVADGLVKV QVALGNIASK RERVKILYKK IEDLIKYLDP EYMDRIAIPD ASKLQFILA EEQFILSQVA LLEQVEALVP MLDSAHIKAV PEHAARLQRL AQIHIQQQDQ CVEITEESKA LLEEYNKTTM L LSKQFVQW DELLCQLEAA KQVKPAEE

UniProtKB: Dynactin subunit 3

Macromolecule #9: Dynactin subunit 1

• Macromolecule: Name: Dynactin subunit 1 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 142.015484 KDa

Sequence

String:

MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLRR EGTDSNAKTS KLRGPKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG PSGSASAGEL SSSEPSTPAQ TPLAAPIIPT PALTSPGAAP PLPSPSKEEE GLRAQVRDLE EKLETLRLKR AE DKAKLKE LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK EARKEAKEAL EAKERYMEEM ADTADAIEMA TLDKEMAEER AES LQQEVE ALKERVDELT TDLEILKAEI EEKGSDGAAS SYQLKQLEEQ NARLKDALVR MRDLSSSEKQ EHVKLQKLME KKNQ ELEVV RQQRERLQEE LSQAESTIDE LKEQVDAALG AEEMVEMLTD RNLNLEEKVR ELRETVGDLE AMNEMNDELQ ENARE TELE LREQLDMAGA RVREAQKRVE AAQETVADYQ QTIKKYRQLT AHLQDVNREL TNQQEASVER QQQPPPETFD FKIKFA ETK AHAKAIEMEL RQMEVAQANR HMSLLTAFMP DSFLRPGGDH DCVLVLLLMP RLICKAELIR KQAQEKFDLS ENCSERP GL RGAAGEQLSF AAGLVYSLSL LQATLHRYEH ALSQCSVDVY KKVGSLYPEM SAHERSLDFL IELLHKDQLD ETVNVEPL T KAIKYYQHLY SIHLAEQPED STMQLADHIK FTQSALDCMS VEVGRLRAFL QGGQEASDIA LLLRDLETSC SDIRQFCKK IRRRMPGTDA PGIPAALAFG AQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGT PSSSPYECL RQSCNILIST MNKLATAMQE GEYDAERPPS KPPPVELRAA ALRAEITDAE GLGLKLEDRE TVIKELKKSL K IKGEELSE ANVRLSLLEK KLDSAAKDAD ERIEKVQTRL EETQALLRKK EKEFEETMDA LQADIDQLEA EKAELKQRLN SQ SKRTIEG IRGPPPSGIA TLVSGIAGEE QQRGGAPGQA PGIVPGPGLV KDSPLLLQQI SAMRLHISQL QHENSVLKGA QMK ASLAAL PPLHVAKLSL PPHEGPGSEL AAGALYRKTN QLLETLNQLS THTHVVDITR SSPAAKSPSA QLLEQVTQLK SLSD TIEKL KDEVLKETVS QRPGATVPTD FATFPSSAFL RAKEEQQDDT VYMGKVTFSC AAGLGQRHRL VLTQEQLHQL HDRLI S

UniProtKB: Dynactin subunit 1

Macromolecule #10: Dynactin 6

• Macromolecule: Name: Dynactin 6 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 20.70391 KDa

Sequence

String:

MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIVI GEGNLIEEQA LIINAHPDNI TPDAEDSEPK PMIIGTNNV FEVGCYSQAM KMGDNNVIES KAYVGRNVIL TSGCIIGACC NLNTFEVIPE NTVIYGADCL RRVQTERPQP Q TLQLDFLM KILPNYHHLK KTMKGSSTPV KN

UniProtKB: Dynactin subunit 6

Macromolecule #11: Dynactin subunit 5

• Macromolecule: Name: Dynactin subunit 5 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 20.150533 KDa

Sequence

String:

MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGD HVFIEEDCVV NAAQIGSYVH VGKNCVIGRR CVLKDCCKIL DNTVLPPETV VPPFTVFSGC PGLFSGELPE C TQELMIDV TKSYYQKFLP LTQV

UniProtKB: Dynactin subunit 5

Macromolecule #12: C-Jun-amino-terminal kinase-interacting protein 3

• Macromolecule: Name: C-Jun-amino-terminal kinase-interacting protein 3 / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 65.975398 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

SNIEFLKMME IQMDEGGGVV VYQDDYCSGS VMSERVSGLA GSIYREFERL IHCYDEEVVK ELMPLVVNVL ENLDSVLSEN QEHEVELEL LREDNEQLLT QYEREKALRR QAEEKFIEFE DALEQEKKEL QIQVEHYEFQ TRQLELKAKN YADQISRLEE R ESEMKKEY NALHQRHTEM IQTYVEHIER SKMQQVGGNS QTESSLPGRR KERPTSLNVF PLADGTVRAQ IGGKLVPAGD HW HLSDLGQ LQSSSSYQCP QDEMSESGQS SAAATPSTTG TKSNTPTSSV PSAAVTPLNE SLQPLGDYGV GSKNSKRARE KRD SRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDMCPETRL DRTGSSPTQG IVNKAFGINT DSLYHELSTA GSEV IGDVD EGADLLGEFS VRDDFFGMGK EVGNLLLENS QLLETKNALN VVKNDLIAKV DQLSGEQEVL RGELEAAKQA KVKLE NRIK ELEEELKRVK SEAIIARREP KEEAEDVSSY LCTESDKIPM AQRRRFTRVE MARVLMERNQ YKERLMELQE AVRWTE MIR ASREGSGSGR WSHPQFEK

UniProtKB: C-Jun-amino-terminal kinase-interacting protein 3

Macromolecule #13: Dynactin subunit 4

• Macromolecule: Name: Dynactin subunit 4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 52.920434 KDa

Sequence

String:

MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTAVKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPDHP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA RRRNYMPLAF SQHTIHVVDK YGLGTRLQRP RAGTTITALA GLSLKEGEDQ KEIKIEPAQA VDEVEPLPED YY TRPVNLT EVTTLQQRLL QPDFQPICAS QLYPRHKHLL IKRSLRCRQC EHNLSKPEFN PTSIKFKIQL VAVNYIPEVR IMS IPNLRY MKESQVLLTL TNPVENLTHV TLLECEEGDP DDTNSTAKVS VPPTELVLAG KDAAAEYDEL AEPQDFPDDP DVVA FRKAN KVGVFIKVTP QREEGDVTVC FKLKHDFKNL AAPIRPVEEA DPGAEVSWLT QHVELSLGPL LP

UniProtKB: Dynactin subunit 4

Macromolecule #14: Dynein light chain 1, cytoplasmic

• Macromolecule: Name: Dynein light chain 1, cytoplasmic / type: protein_or_peptide / ID: 14 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 10.381899 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG

UniProtKB: Dynein light chain 1, cytoplasmic

Macromolecule #15: Cytoplasmic dynein 1 heavy chain 1

• Macromolecule: Name: Cytoplasmic dynein 1 heavy chain 1 / type: protein_or_peptide / ID: 15 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 533.055125 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVG DEGEEEKEFI SYNINIDIHY GVKSNSLAFI KRTPVIDADK PVSSQLRVLT LSEDSPYETL HSFISNAVAP F FKSYIRES GKADRDGDKM APSVEKKIAE LEMGLLHLQQ NIEIPEISLP IHPMITNVAK QCYERGEKPK VTDFGDKVED PT FLNQLQS GVNRWIREIQ KVTKLDRDPA SGTALQEISF WLNLERALYR IQEKRESPEV LLTLDILKHG KRFHATVSFD TDT GLKQAL ETVNDYNPLM KDFPLNDLLS ATELDKIRQA LVAIFTHLRK IRNTKYPIQR ALRLVEAISR DLSSQLLKVL GTRK LMHVA YEEFEKVMVA CFEVFQTWDD EYEKLQVLLR DIVKRKREEN LKMVWRINPA HRKLQARLDQ MRKFRRQHEQ LRAVI VRVL RPQVTAVAQQ NQGEVPEPQD MKVAEVLFDA ADANAIEEVN LAYENVKEVD GLDVSKEGTE AWEAAMKRYD ERIDRV ETR ITARLRDQLG TAKNANEMFR IFSRFNALFV RPHIRGAIRE YQTQLIQRVK DDIESLHDKF KVQYPQSQAC KMSHVRD LP PVSGSIIWAK QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTI E STRVRGRTGN VLKLKVNFLP EIITLSKEVR NLKWLGFRVP LAIVNKAHQA NQLYPFAISL IESVRTYERT CEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLN LHSYSNLPIW VNKLDMEIER ILGVRLQAGL RAWTQVLLGQ AEDKAEVDMD TDAPQVSHKP GGEPKIKNVV H ELRITNQV IYLNPPIEEC RYKLYQEMFA WKMVVLSLPR IQSQRYQVGV HYELTEEEKF YRNALTRMPD GPVALEESYS AV MGIVSEV EQYVKVWLQY QCLWDMQAEN IYNRLGEDLN KWQALLVQIR KARGTFDNAE TKKEFGPVVI DYGKVQSKVN LKY DSWHKE VLSKFGQMLG SNMTEFHSQI SKSRQELEQH SVDTASTSDA VTFITYVQSL KRKIKQFEKQ VELYRNGQRL LEKQ RFQFP PSWLYIDNIE GEWGAFNDIM RRKDSAIQQQ VANLQMKIVQ EDRAVESRTT DLLTDWEKTK PVTGNLRPEE ALQAL TIYE GKFGRLKDDR EKCAKAKEAL ELTDTGLLSG SEERVQVALE ELQDLKGVWS ELSKVWEQID QMKEQPWVSV QPRKLR QNL DALLNQLKSF PARLRQYASY EFVQRLLKGY MKINMLVIEL KSEALKDRHW KQLMKRLHVN WVVSELTLGQ IWDVDLQ KN EAIVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN SVSAMKLSPY YKVFEEDA L SWEDKLNRIM ALFDVWIDVQ RRWVYLEGIF TGSADIKHLL PVETQEFQSI STEFLALMKK VSKSPLVMDV LNIQGVQRS LERLADLLGE IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE GEEVMFKTP VSITEHPKIN EWLTLVEKEM RVTLAKLLAE SVTEVEIFGK ATSIDPNTYI TWIDKYQAQL VVLSAQIAWS E NVETALSS MGGGGDAAPL HSVLSNVEVT LNVLADSVLM EQPPLRRRKL EHLITELVHQ RDVTRSLIKS KIDNAKSFEW LS QMRFYFD PKQTDVLQQL SIQMANAKFN YGFEYLGVQD KLVQTPLTDR CYLTMTQALE ARLGGSPFGP AGTGKTESVK ALG HQLGRF VLVFNCDETF DFQAMGRIFV GLCQVGAWGC FDEFNRLEER MLSAVSQQVQ CIQEALREHS NPNYDKTSAP ITCE LLNKQ VKVSPDMAIF ITMNPGYAGR SNLPDNLKKL FRSLAMTKPD RQLIAQVMLY SQGFRTAEVL ANKIVPFFKL CDEQL SSQS HYDFGLRALK SVLVSAGNVK RERIQKIKRE KEERGEAVDE GEIAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSL LSD VFPGVQYHRG EMTALREELK KVCQEMYLTY GDGEEVGGMW VEKVLQLYQI TQINHGLMMV GPSGSGKSMA WRVLLKA LE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDSVR GELQKRQWIV FDGDVDPEWV ENLNSVLD D NKLLTLPNGE RLSLPPNVRI MFEVQDLKYA TLATVSRCGM VWFSEDVLST DMIFNNFLAR LRSIPLDEGE DEAQRRRKG KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQIEQLERY IQRYLVYAIL WSLSGDSRLK MRAELGEYIR RITTVPLPTA PNIPIIDYEV SISGEWSPWQ AKVPQIEVET H KVAAPDVV VPTLDTVRHE ALLYTWLAEH KPLVLCGPPG SGKTMTLFSA LRALPDMEVV GLNFSSATTP ELLLKTFDHY CE YRRTPNG VVLAPVQLGK WLVLFCDEIN LPDMDKYGTQ RVISFIRQMV EHGGFYRTSD QTWVKLERIQ FVGACNPPTD PGR KPLSHR FLRHVPVVYV DYPGPASLTQ IYGTFNRAML RLIPSLRTYA EPLTAAMVEF YTMSQERFTQ DTQPHYIYSP REMT RWVRG IFEALRPLET LPVEGLIRIW AHEALRLFQD RLVEDEERRW TDENIDTVAL KHFPNIDREK AMSRPILYSN WLSKD YIPV DQEELRDYVK ARLKVFYEEE LDVPLVLFNE VLDHVLRIDR IFRQPQGHLL LIGVSGAGKT TLSRFVAWMN GLSVYQ IKV HRKYTGEDFD EDLRTVLRRS GCKNEKIAFI MDESNVLDSG FLERMNTLLA NGEVPGLFEG DEYATLMTQC KEGAQKE GL MLDSHEELYK WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNY I VPDYMPVVYD KLPQPPSHRE AIVNSCVFVH QTLHQANARL AKRGGRTMAI TPRHYLDFIN HYANLFHEKR SELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAV IEAQNAVKSI KKQHLVEVRS MANPPAAVKL ALESICLLLG ESTTDWKQIR SIIMRENFIP TIVNFSAEEI S DAIREKMK KNYMSNPSYN YEIVNRASLA CGPMVKWAIA QLNYADMLKR VEPLRNELQK LEDDAKDNQQ KANEVEQMIR DL EASIARY KEEYAVLISE AQAIKADLAA VEAKVNRSTA LLKSLSAERE RWEKTSETFK NQMSTIAGDC LLSAAFIAYA GYF DQQMRQ NLFTTWSHHL QQANIQFRTD IARTEYLSNA DERLRWQASS LPADDLCTEN AIMLKRFNRY PLIIDPSGQA TEFI MNEYK DRKITRTSFL DDAFRKNLES ALRFGNPLLV QDVESYDPVL NPVLNREVRR TGGRVLITLG DQDIDLSPSF VIFLS TRDP TVEFPPDLCS RVTFVNFTVT RSSLQSQCLN EVLKAERPDV DEKRSDLLKL QGEFQLRLRQ LEKSLLQALN EVKGRI LDD DTIITTLENL KREAAEVTRK VEETDIVMQE VETVSQQYLP LSTACSSIYF TMESLKQIHF LYQYSLQFFL DIYHNVL YE NPNLKGVTDH TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD AEFQHFLRGN EIVLSAGS T PRIQGLTVEQ AEAVVRLSCL PAFKDLIAKV QADEQFGIWL DSSSPEQTVP YLWSEETPAT PIGQAIHRLL LIQAFRPDR LLAMAHMFVS TNLGESFMSI MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVK SGRWVMLKNV HLAPGWLMQL EKKLHSLQPH ACFRLFLTME INPKVPVNLL RAGRIFVFEP PPGVKANMLR T FSSIPVSR ICKSPNERAR LYFLLAWFHA IIQERLRYAP LGWSKKYEFG ESDLRSACDT VDTWLDDTAK GRQNISPDKI PW SALKTLM AQSIYGGRVD NEFDQRLLNT FLERLFTTRS FDSEFKLACK VDGHKDIQMP DGIRREEFVQ WVELLPDTQT PSW LGLPNN AERVLLTTQG VDMISKMLKM QMLEDEDDLA YAETEKKTRT DSTSDGRPAW MRTLHTTASN WLHLIPQTLS HLKR TVENI KDPLFRFFER EVKMGAKLLQ DVRQDLADVV QVCEGKKKQT NYLRTLINEL VKGILPRSWS HYTVPAGMTV IQWVS DFSE RIKQLQNISL AAASGGAKEL KNIHVCLGGL FVPEAYITAT RQYVAQANSW SLEELCLEVN VTTSQGATLD ACSFGV TGL KLQGATCNNN KLSLSNAIST ALPLTQLRWV KQTNTEKKAS VVTLPVYLNF TRADLIFTVD FEIATKEDPR SFYERGV AV LCTE

UniProtKB: Cytoplasmic dynein 1 heavy chain 1

Macromolecule #16: Cytoplasmic dynein 1 intermediate chain 2

• Macromolecule: Name: Cytoplasmic dynein 1 intermediate chain 2 / type: protein_or_peptide / ID: 16 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 68.442141 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA EALLQSMGLT PESPIVPPPM SPSSKSVST PSEAGSQDSG DGAVGSRRGP IKLGMAKITQ VDFPPREIVT YTKETQTPVM AQPKEDEEED DDVVAPKPPI E PEEEKTLK KDEENDSKAP PHELTEEEKQ QILHSEEFLS FFDHSTRIVE RALSEQINIF FDYSGRDLED KEGEIQAGAK LS LNRQFFD ERWSKHRVVS CLDWSSQYPE LLVASYNNNE DAPHEPDGVA LVWNMKYKKT TPEYVFHCQS AVMSATFAKF HPN LVVGGT YSGQIVLWDN RSNKRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLISIS TDGKICSWSL DMLSHPQDSM ELVH KQSKA VAVTSMSFPV GDVNNFVVGS EEGSVYTACR HGSKAGISEM FEGHQGPITG IHCHAAVGAV DFSHLFVTSS FDWTV KLWS TKNNKPLYSF EDNAGYVYDV MWSPTHPALF ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIA VGD SEGQIVIYDV GEQIAVPRND EWARFGRTLA EINANRADAE EEAATRIPA

UniProtKB: Cytoplasmic dynein 1 intermediate chain 2

Macromolecule #17: Cytoplasmic dynein 1 light intermediate chain 2

• Macromolecule: Name: Cytoplasmic dynein 1 light intermediate chain 2 / type: protein_or_peptide / ID: 17 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 54.173156 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF GEDGSGKTTL MTKLQGAEHG KKGRGLEYL YLSVHDEDRD DHTRCNVWIL DGDLYHKGLL KFAVSAESLP ETLVIFVADM SRPWTVMESL QKWASVLREH I DKMKIPPE KMRELERKFV KDFQDYMEPE EGCQGSPQRR GPLTSGSDEE NVALPLGDNV LTHNLGIPVL VVCTKCDAVS VL EKEHDYR DEHLDFIQSH LRRFCLQYGA ALIYTSVKEE KNLDLLYKYI VHKTYGFHFT TPALVVEKDA VFIPAGWDNE KKI AILHEN FTTVKPEDAY EDFIVKPPVR KLVHDKELAA EDEQVFLMKQ QSLLAKQPAT PTRASESPAR GPSGSPRTQG RGGP ASVPS SSPGTSVKKP DPNIKNNAAS EGVLASFFNS LLSKKTGSPG SPGAGGVQST AKKSGQKTVL SNVQEELDRM TRKPD SMVT NSSTENEA

UniProtKB: Cytoplasmic dynein 1 light intermediate chain 2

Macromolecule #18: Dynein light chain Tctex-type 1

• Macromolecule: Name: Dynein light chain Tctex-type 1 / type: protein_or_peptide / ID: 18 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 12.461996 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MEDYQAAEET AFVVDEVSNI VKEAIESAIG GNAYQHSKVN QWTTNVVEQT LSQLTKLGKP FKYIVTCVIM QKNGAGLHTA SSCFWDSST DGSCTVRWEN KTMYCIVSAF GLSI

UniProtKB: Dynein light chain Tctex-type 1

Macromolecule #19: Dynein light chain roadblock-type 1

• Macromolecule: Name: Dynein light chain roadblock-type 1 / type: protein_or_peptide / ID: 19 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 10.934576 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI DPQNDLTFLR IRSKKNEIMV APDKDYFLI VIQNPTE

UniProtKB: Dynein light chain roadblock-type 1

Macromolecule #20: ADENOSINE-5'-DIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 20 / Number of copies: 16 / Formula: ADP
• Molecular weight: Theoretical: 427.201 Da

Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Macromolecule #21: ADENOSINE-5'-TRIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 21 / Number of copies: 6 / Formula: ATP
• Molecular weight: Theoretical: 507.181 Da

Chemical component information

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

Macromolecule #22: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 22 / Number of copies: 3 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Macromolecule #23: MAGNESIUM ION

• Macromolecule: Name: MAGNESIUM ION / type: ligand / ID: 23 / Number of copies: 6 / Formula: MG
• Molecular weight: Theoretical: 24.305 Da

Macromolecule #24: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

• Macromolecule: Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 24 / Number of copies: 4 / Formula: ANP
• Molecular weight: Theoretical: 506.196 Da

Chemical component information

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Buffer: pH: 7.2
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: FEI TITAN KRIOS
• Image recording: Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 53.0 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.5 µm
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• Startup model: Type of model: INSILICO MODEL
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 10.0 Å / Resolution method: OTHER / Number images used: 700290
• Initial angle assignment: Type: ANGULAR RECONSTITUTION
• Final angle assignment: Type: ANGULAR RECONSTITUTION

Atomic model buiding 1

Initial model

PDB ID:

7z8g

Chain - Source name: PDB / Chain - Initial model type: experimental model

• Software: Name: UCSF Chimera

Output model

PDB-8ptk:
Composite structure of Dynein-Dynactin-JIP3-LIS1