EMDB-29014: Engineered human dynein motor domain in the microtubule-unbound s...

Basic information

Entry

Database: EMDB / ID: EMD-29014

• Title: Engineered human dynein motor domain in the microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1)
• Map data: Unsharpened map of engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1 region)

Sample

• Complex: Engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi
  • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase
  • Protein or peptide: Platelet-activating factor acetylhydrolase IB subunit beta,Platelet-activating factor acetylhydrolase IB subunit beta,human LIS1 protein with a SNAP tag
• Ligand: ADENOSINE-5'-DIPHOSPHATE

• Keywords: Dynein / motor domain / microtubule-unbound / MOTOR PROTEIN / LIS1

Function / homology

Function:

corpus callosum morphogenesis / microtubule cytoskeleton organization involved in establishment of planar polarity / ameboidal-type cell migration / establishment of planar polarity of embryonic epithelium / 1-alkyl-2-acetylglycerophosphocholine esterase complex / maintenance of centrosome location / selenocysteine biosynthetic process / platelet activating factor metabolic process / radial glia-guided pyramidal neuron migration / acrosome assembly / central region of growth cone / serine-tRNA ligase / serine-tRNA ligase activity / seryl-tRNA aminoacylation / cerebral cortex neuron differentiation / establishment of centrosome localization / microtubule sliding / positive regulation of embryonic development / positive regulation of cytokine-mediated signaling pathway / microtubule organizing center organization / interneuron migration / layer formation in cerebral cortex / auditory receptor cell development / nuclear membrane disassembly / astral microtubule / positive regulation of dendritic spine morphogenesis / positive regulation of intracellular transport / cortical microtubule organization / myeloid leukocyte migration / reelin-mediated signaling pathway / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of spindle assembly / stereocilium / osteoclast development / microtubule plus-end binding / brain morphogenesis / vesicle transport along microtubule / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / retrograde axonal transport / kinesin complex / negative regulation of JNK cascade / minus-end-directed microtubule motor activity / P-body assembly / microtubule associated complex / dynein light intermediate chain binding / cytoplasmic dynein complex / motile cilium / stem cell division / dynein intermediate chain binding / nuclear migration / dynein complex binding / cell leading edge / transmission of nerve impulse / germ cell development / establishment of mitotic spindle orientation / dynactin binding / cochlea development / protein secretion / neuromuscular process controlling balance / neuroblast proliferation / positive regulation of axon extension / microtubule-based process / phospholipase binding / lipid catabolic process / cytoplasmic microtubule / COPI-mediated anterograde transport / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / JNK cascade / cytoplasmic microtubule organization / axon cytoplasm / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / stress granule assembly / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / positive regulation of mitotic cell cycle / regulation of microtubule cytoskeleton organization / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / regulation of mitotic spindle organization / Resolution of Sister Chromatid Cohesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / adult locomotory behavior / AURKA Activation by TPX2 / hippocampus development / mitotic spindle organization / filopodium / phosphoprotein binding / RHO GTPases Activate Formins / modulation of chemical synaptic transmission / cerebral cortex development / kinetochore / microtubule cytoskeleton organization / Schaffer collateral - CA1 synapse / neuron migration / HCMV Early Events

Domain/homology:

: / : / PAC1 LisH domain / Serine-tRNA synthetase, type1, N-terminal / Seryl-tRNA synthetase N-terminal domain / Dynein regulator LIS1 / LIS1, N-terminal / Serine-tRNA ligase, type1 / Serine-tRNA ligase catalytic core domain / Serine-tRNA synthetase, type1, N-terminal domain superfamily / Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm / Lissencephaly type-1-like homology motif / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / LIS1 homology (LisH) motif profile. / LIS1 homology motif / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) / tRNA synthetase class II core domain (G, H, P, S and T) / : / Dynein heavy chain, ATPase lid domain / P-loop containing dynein motor region / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / 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 / Aminoacyl-tRNA synthetase, class II / Aminoacyl-transfer RNA synthetases class-II family profile. / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / WD domain, G-beta repeat / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase

Component:

Platelet-activating factor acetylhydrolase IB subunit beta / Cytoplasmic dynein 1 heavy chain 1 / Serine--tRNA ligase

• Biological species: Homo sapiens (human)
• Method: single particle reconstruction / cryo EM / Resolution: 3.3 Å
• Authors: Ton W / Wang Y / Chai P

Funding support

United States, 3 items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R35GM139483	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R35GM142959	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	S10OD023603	United States

• Citation: Journal: Nat Struct Mol Biol / Year: 2023; Title: Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.; Authors: William D Ton / Yue Wang / Pengxin Chai / Cisloynny Beauchamp-Perez / Nicholas T Flint / Lindsay G Lammers / Hao Xiong / Kai Zhang / Steven M Markus / ; Abstract: The lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 binding is required for dynein activity, its unbinding prior to initiation of cargo transport is equally important, since preventing dissociation leads to dynein dysfunction. To understand whether and how dynein-LIS1 binding is modulated, we engineered dynein mutants locked in a microtubule-bound (MT-B) or microtubule-unbound (MT-U) state. Whereas the MT-B mutant exhibits low LIS1 affinity, the MT-U mutant binds LIS1 with high affinity, and as a consequence remains almost irreversibly associated with microtubule plus-ends. We find that a monomeric motor domain is sufficient to exhibit these opposing LIS1 affinities, and that this is evolutionarily conserved between yeast and humans. Three cryo-EM structures of human dynein with and without LIS1 reveal microtubule-binding induced conformational changes responsible for this regulation. Our work reveals key biochemical and structural insight into LIS1-mediated dynein activation.

History

Deposition	Dec 4, 2022	-
Header (metadata) release	Jun 21, 2023	-
Map release	Jun 21, 2023	-
Update	Nov 15, 2023	-
Current status	Nov 15, 2023	Processing site: RCSB / Status: Released

Map

• File: Download / File: emd_29014.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Unsharpened map of engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1 region)
• Voxel size: X=Y=Z: 1.149 Å

Density

Contour Level	By AUTHOR: 0.3
Minimum - Maximum	-0.50581324 - 1.1052208
Average (Standard dev.)	-0.0002358953 (±0.026874704)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 360 360 360 Spacing 360 360 360
Cell	A=B=C: 413.64 Å α=β=γ: 90.0 °

Supplemental data

Mask #1

• File: emd_29014_msk_1.map

Half map: Half map A of engineered human dynein motor...

• File: emd_29014_half_map_1.map
• Annotation: Half map A of engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1 region)

Half map: Half map B of engineered human dynein motor...

• File: emd_29014_half_map_2.map
• Annotation: Half map B of engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1 region)

Sample components

Entire : Engineered human dynein motor domain in microtubule-unbound state...

• Entire: Name: Engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi

Components

• Complex: Engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi
  • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase
  • Protein or peptide: Platelet-activating factor acetylhydrolase IB subunit beta,Platelet-activating factor acetylhydrolase IB subunit beta,human LIS1 protein with a SNAP tag
• Ligand: ADENOSINE-5'-DIPHOSPHATE

Supramolecule #1: Engineered human dynein motor domain in microtubule-unbound state...

• Supramolecule: Name: Engineered human dynein motor domain in microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi; type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 490 KDa

Macromolecule #1: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase

• Macromolecule: Name: Cytoplasmic dynein 1 heavy chain 1,Serine--tRNA ligase; type: protein_or_peptide / ID: 1 ; Details: residues 1458-3277 of dynein followed by residues 30-96 of serine-tRNA ligase, followed by residues 3412-4646 of dynein; Number of copies: 1 / Enantiomer: LEVO / EC number: serine-tRNA ligase
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 357.459125 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

GSALEEFLKQ IREVWNTYEL DLVNYQNKCR LIRGWDDLFN KVKEHINSVS AMKLSPYYKV FEEDALSWED KLNRIMALFD VWIDVQRRW VYLEGIFTGS ADIKHLLPVE TQRFQSISTE FLALMKKVSK SPLVMDVLNI QGVQRSLERL ADLLGKIQKA L GEYLERER SSFPRFYFVG DEDLLEIIGN SKNVAKLQKH FKKMFAGVSS IILNEDNSVV LGISSREGEE VMFKTPVSIT EH PKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL SAQIAWSENV ETALSSMGGG GDA APLHSV LSNVEVTLNV LADSVLMEQP PLRRRKLEHL ITELVHQRDV TRSLIKSKID NAKSFEWLSQ MRFYFDPKQT DVLQ QLSIQ MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL GGSPFGPAGT GKTESVKALG HQLGRFVLVF NCDET FDFQ AMGRIFVGLC QVGAWGCFDE FNRLEERMLS AVSQQVQCIQ EALREHSNPN YDKTSAPITC ELLNKQVKVS PDMAIF ITM NPGYAGRSNL PDNLKKLFRS LAMTKPDRQL IAQVMLYSQG FRTAEVLANK IVPFFKLCDE QLSSQSHYDF GLRALKS VL VSAGNVKRER IQKIKREKEE RGEAVDEGEI AENLPEQEIL IQSVCETMVP KLVAEDIPLL FSLLSDVFPG VQYHRGEM T ALREELKKVC QEMYLTYGDG EEVGGMWVEK VLQLYQITQI NHGLMMVGPS GSGKSMAWRV LLKALERLEG VEGVAHIID PKAISKDHLY GTLDPNTREW TDGLFTHVLR KIIDSVRGEL QKRQWIVFDG DVDPEWVENL NSVLDDNKLL TLPNGERLSL PPNVRIMFE VQDLKYATLA TVSRCGMVWF SEDVLSTDMI FNNFLARLRS IPLDEGEDEA QRRRKGKEDE GEEAASPMLQ I QRDAATIM QPYFTSNGLV TKALEHAFQL EHIMDLTRLR CLGSLFSMLH QACRNVAQYN ANHPDFPMQI EQLERYIQRY LV YAILWSL SGDSRLKMRA ELGEYIRRIT TVPLPTAPNI PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTV RHEALL YTWLAEHKPL VLCGPPGSGK TMTLFSALRA LPDMEVVGLN FSSATTPELL LKTFDHYCEY RRTPNGVVLA PVQL GKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVY VDYP GPASLTQIYG TFNRAMLRLI PSLRTYAEPL TAAMVEFYTM SQERFTQDTQ PHYIYSPREM TRWVRGIFEA LRPLET LPV EGLIRIWAHE ALRLFQDRLV EDEERRWTDE NIDTVALKHF PNIDREKAMS RPILYSNWLS KDYIPVDQEE LRDYVKA RL KVFYEEELDV PLVLFNEVLD HVLRIDRIFR QPQGHLLLIG VSGAGKTTLS RFVAWMNGLS VYQIKVHRKY TGEDFDED L RTVLRRSGCK NEKIAFIMDE SNVLDSGFLE RMNTLLANGE VPGLFEGDEY ATLMTQCKEG AQKEGLMLDS HEELYKWFT SQVIRNLHVV FTMNPSSEGL KDRAATSPAL FNRCVLNWFG DWSTEALYQV GKEFTSKMDL EKPNYIVPDY MPVVYDKLPQ PPSHREAIV NSCVFVHQTL HQANARLAKR GGRTMAITPR HYLDFINHYA NLFHEKRSEL EEQQMHLNVG LRKIKETVDQ V EELRRDLR IKSQELEVKN AAANDKLKKM VKDQQEAEKK KVMSQEIQEQ LHKQQEVIAD KQMSLLALDQ EVQELKKRLQ EV QTERNQV AKRVPKAPPE EKEALIARGR ALGEEAKRLE EALREKEAQL EALRNELQKL EDDAKDNQQK ANEVEQMIRD LEA SIARYK EEYAVLISEA QAIKADLAAV EAKVNRSTAL LKSLSAERER WEKTSETFKN QMSTIAGDCL LSAAFIAYAG YFDQ QMRQN LFTTWSHHLQ QANIQFRTDI ARTEYLSNAD ERLRWQASSL PADDLCTENA IMLKRFNRYP LIIDPSGQAT EFIMN EYKD RKITRTSFLD DAFRKNLESA LRFGNPLLVQ DVESYDPVLN PVLNREVRRT GGRVLITLGD QDIDLSPSFV IFLSTR DPT VEFPPDLCSR VTFVNFTVTR SSLQSQCLNE VLKAERPDVD EKRSDLLKLQ GEFQLRLRQL EKSLLQALNE VKGRILD DD TIITTLENLK REAAEVTRKV EETDIVMQEV ETVSQQYLPL STACSSIYFT MESLKQIHFL YQYSLQFFLD IYHNVLYE N PNLKGVTDHT QRLSIITKDL FQVAFNRVAR GMLHQDHITF AMLLARIKLK GTVGEPTYDA EFQHFLRGNE IVLSAGSTP RIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD SSSPEQTVPY LWSEETPATP IGQAIHRLLL IQAFRPDRLL AMAHMFVST NLGESFMSIM EQPLDLTHIV GTEVKPNTPV LMCSVPGYDA SGHVEDLAAE QNTQITSIAI GSAEGFNQAD K AINTAVKS GRWVMLKNVH LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR AGRIFVFEPP PGVKANMLRT FS SIPVSRI CKSPNERARL YFLLAWFHAI IQERLRYAPL GWSKKYEFGE SDLRSACDTV DTWLDDTAKG RQNISPDKIP WSA LKTLMA QSIYGGRVDN EFDQRLLNTF LERLFTTRSF DSEFKLACKV DGHKDIQMPD GIRREEFVQW VELLPDTQTP SWLG LPNNA ERVLLTTQGV DMISKMLKMQ MLEDEDDLAY AETEKKTRTD STSDGRPAWM RTLHTTASNW LHLIPQTLSH LKRTV ENIK DPLFRFFERE VKMGAKLLQD VRQDLADVVQ VCEGKKKQTN YLRTLINELV KGILPRSWSH YTVPAGMTVI QWVSDF SER IKQLQNISLA AASGGAKELK NIHVCLGGLF VPEAYITATR QYVAQANSWS LEELCLEVNV TTSQGATLDA CSFGVTG LK LQGATCNNNK LSLSNAISTA LPLTQLRWVK QTNTEKKASV VTLPVYLNFT RADLIFTVDF EIATKEDPRS FYERGVAV L CTEEF

UniProtKB: Cytoplasmic dynein 1 heavy chain 1, Serine--tRNA ligase, Cytoplasmic dynein 1 heavy chain 1

Macromolecule #2: Platelet-activating factor acetylhydrolase IB subunit beta,Platel...

• Macromolecule: Name: Platelet-activating factor acetylhydrolase IB subunit beta,Platelet-activating factor acetylhydrolase IB subunit beta,human LIS1 protein with a SNAP tag; type: protein_or_peptide / ID: 2 ; Details: SNAP tag present on C-terminus,SNAP tag present on C-terminus; Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 66.423547 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

GSVLSQRQRD ELNRAIADYL RSNGYEEAYS VFKKEAELDV NEELDKKYAG LLEKKWTSVI RLQKKVMELE SKLNEAKEEF TSGGPLGQK RDPKEWIPRP PEKYALSGHR SPVTRVIFHP VFSVMVSASE DATIKVWDYE TGDFERTLKG HTDSVQDISF D HSGKLLAS CSADMTIKLW DFQGFECIRT MHGHDHNVSS VAIMPNGDHI VSASRDKTIK MWEVQTGYCV KTFTGHREWV RM VRPNQDG TLIASCSNDQ TVRVWVVATK ECKAELREHE HVVECISWAP ESSYSSISEA TGSETKKSGK PGPFLLSGSR DKT IKMWDV STGMCLMTLV GHDNWVRGVL FHSGGKFILS CADDKTLRVW DYKNKRCMKT LNAHEHFVTS LDFHKTAPYV VTGS VDQTV KVWECRGAGA GADKDCEMKR TTLDSPLGKL ELSGCEQGLH RIIFLGKGTS AADAVEVPAP AAVLGGPEPL MQATA WLNA YFHQPEAIEE FPVPALHHPV FQQESFTRQV LWKLLKVVKF GEVISYSHLA ALAGNPAATA AVKTALSGNP VPILIP CHR VVQGDLDVGG YEGGLAVKEW LLAHEGHRLG KPGLG

UniProtKB: Platelet-activating factor acetylhydrolase IB subunit beta

Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 2 / Formula: ADP
• Molecular weight: Theoretical: 427.201 Da

Chemical component information

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

Experimental details

Structure determination

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

Sample preparation

• Concentration: 0.5 mg/mL
• Buffer: pH: 7.4 ; Details: 50 mM Tris pH 7.4, 150 mM potassium acetate, 2 mM magnesium acetate, 1 mM EGTA, 1 mM DTT, and 0.1 mM Mg-ATP
• Grid: Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS / Support film - Film thickness: 1 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR
• Vitrification: Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

Electron microscopy

• Microscope: FEI TITAN KRIOS
• Image recording: Film or detector model: GATAN K3 (6k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 40.0 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: C2 aperture diameter: 100.0 µm / Calibrated defocus max: 3.0 µm / Calibrated defocus min: 1.2 µm / Calibrated magnification: 105000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000
• Sample stage: Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• Startup model: Type of model: NONE / Details: Ab-initio model was generated in cryoSPARC.
• Final reconstruction: Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3) / Number images used: 53572
• Initial angle assignment: Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)
• Final angle assignment: Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)

Atomic model buiding 1

• Refinement: Space: REAL / Protocol: RIGID BODY FIT

Output model

PDB-8fdu:
Engineered human dynein motor domain in the microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1)