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- EMDB-11969: A 3.7-angstrom structure of Yarrowia lipolytica complex I with an... -

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Basic information

Entry
Database: EMDB / ID: EMD-11969
TitleA 3.7-angstrom structure of Yarrowia lipolytica complex I with an R121M mutation in NUCM.
Map dataFinal map globally sharpened with RELION postprocess
Sample
  • Complex: Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxidoreductase) with NUCM R121M mutation
    • Protein or peptide: x 39 types
  • Protein or peptide: x 3 types
  • Ligand: x 10 types
Function / homology
Function and homology information


NADH dehydrogenase / respiratory chain complex I / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding ...NADH dehydrogenase / respiratory chain complex I / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / respirasome / respiratory electron transport chain / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / fatty acid biosynthetic process / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / oxidoreductase activity / mitochondrion / membrane / metal ion binding
Similarity search - Function
NADH dehydrogenase [ubiquinone] (complex I), 21kDa subunit, fungi / NADH-ubiquinone oxidoreductase, 21kDa subunit, C-terminal, fungi / NADH-ubiquinone oxidoreductase 9.5kDa subunit / C-terminal of NADH-ubiquinone oxidoreductase 21 kDa subunit / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / Soluble ligand binding domain / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 ...NADH dehydrogenase [ubiquinone] (complex I), 21kDa subunit, fungi / NADH-ubiquinone oxidoreductase, 21kDa subunit, C-terminal, fungi / NADH-ubiquinone oxidoreductase 9.5kDa subunit / C-terminal of NADH-ubiquinone oxidoreductase 21 kDa subunit / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / Soluble ligand binding domain / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / SLBB domain / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / GRIM-19 / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / GRIM-19 protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NDUFA6, LYR domain / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NDUFB9, LYR domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH dehydrogenase, subunit C / NADH ubiquinone oxidoreductase, F subunit / Complex 1 LYR protein domain / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH-quinone oxidoreductase, chain M/4 / Complex 1 protein (LYR family) / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / CHCH / NuoE domain / CHCH domain / NADH:ubiquinone oxidoreductase / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2.
Similarity search - Domain/homology
Complex 1 LYR protein domain-containing protein / Uncharacterized protein / Uncharacterized protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / Uncharacterized protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Uncharacterized protein / Acyl carrier protein ...Complex 1 LYR protein domain-containing protein / Uncharacterized protein / Uncharacterized protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / Uncharacterized protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Uncharacterized protein / Acyl carrier protein / Uncharacterized protein / Uncharacterized protein / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit-domain-containing protein / Uncharacterized protein / Thioredoxin-like protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / Acyl carrier protein / Uncharacterized protein / Zinc finger CHCC-type domain-containing protein / NAD-dependent epimerase/dehydratase domain-containing protein / NADH dehydrogenase 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase / ETC complex I subunit conserved region-domain-containing protein / Uncharacterized protein / Uncharacterized protein / NUWM protein / NUVM protein / Subunit NUKM of protein NADH:Ubiquinone oxidoreductase / Subunit NUIM of protein NADH:Ubiquinone oxidoreductase / Subunit NUHM of protein NADH:Ubiquinone oxidoreductase / NUGM protein / NUCM protein / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NUAM protein / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 3 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 6 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 4L
Similarity search - Component
Biological speciesYarrowia lipolytica (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsHirst J / Grba D
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_U105663141 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UU_00015/2 United Kingdom
CitationJournal: J Biol Chem / Year: 2021
Title: A conserved arginine residue is critical for stabilizing the N2 FeS cluster in mitochondrial complex I.
Authors: Mikhail A Hameedi / Daniel N Grba / Katherine H Richardson / Andrew J Y Jones / Wei Song / Maxie M Roessler / John J Wright / Judy Hirst /
Abstract: Respiratory complex I (NADH:ubiquinone oxidoreductase), the first enzyme of the electron-transport chain, captures the free energy released by NADH oxidation and ubiquinone reduction to translocate ...Respiratory complex I (NADH:ubiquinone oxidoreductase), the first enzyme of the electron-transport chain, captures the free energy released by NADH oxidation and ubiquinone reduction to translocate protons across an energy-transducing membrane and drive ATP synthesis during oxidative phosphorylation. The cofactor that transfers the electrons directly to ubiquinone is an iron-sulfur cluster (N2) located in the NDUFS2/NUCM subunit. A nearby arginine residue (R121), which forms part of the second coordination sphere of the N2 cluster, is known to be posttranslationally dimethylated but its functional and structural significance are not known. Here, we show that mutations of this arginine residue (R121M/K) abolish the quinone-reductase activity, concomitant with disappearance of the N2 signature from the electron paramagnetic resonance (EPR) spectrum. Analysis of the cryo-EM structure of NDUFS2-R121M complex I at 3.7 Å resolution identified the absence of the cubane N2 cluster as the cause of the dysfunction, within an otherwise intact enzyme. The mutation further induced localized disorder in nearby elements of the quinone-binding site, consistent with the close connections between the cluster and substrate-binding regions. Our results demonstrate that R121 is required for the formation and/or stability of the N2 cluster and highlight the importance of structural analyses for mechanistic interpretation of biochemical and spectroscopic data on complex I variants.
History
DepositionNov 20, 2020-
Header (metadata) releaseMar 10, 2021-
Map releaseMar 10, 2021-
UpdateDec 7, 2022-
Current statusDec 7, 2022Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7b0n
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11969.png

Downloads & links

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Map

FileDownload / File: emd_11969.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal map globally sharpened with RELION postprocess
Voxel sizeX=Y=Z: 1.05 Å
Density
Contour LevelBy AUTHOR: 0.04 / Movie #1: 0.04
Minimum - Maximum-0.08990855 - 0.27803996
Average (Standard dev.)8.117691e-05 (±0.0066138864)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 472.49997 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.051.051.05
M x/y/z450450450
origin x/y/z0.0000.0000.000
length x/y/z472.500472.500472.500
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS450450450
D min/max/mean-0.0900.2780.000

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Supplemental data

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Mask #1

Fileemd_11969_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1

Fileemd_11969_half_map_1.map
AnnotationHalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2

Fileemd_11969_half_map_2.map
AnnotationHalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxid...

EntireName: Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxidoreductase) with NUCM R121M mutation
Components
  • Complex: Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxidoreductase) with NUCM R121M mutation
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4L
    • Protein or peptide: Subunit NUXM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Epimerase domain-containing protein
    • Protein or peptide: Subunit NUYM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: zf-CHCC domain-containing protein
    • Protein or peptide: Subunit NI8M of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUKM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: Subunit NUFM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NB4M of protein NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUPM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Complex I-B14.7
    • Protein or peptide: GRIM-19
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
    • Protein or peptide: subunit NI9M of protein NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUZM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: NUGM protein
    • Protein or peptide: subunit NEBM of protein NADH:Ubiquinone Oxidoreductase (Complex I) [Yarrowia lipolytica]
    • Protein or peptide: Subunit NIPM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit N7BM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NESM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: subunit NUNM of protein NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUUM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUVM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NB2M of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NIAM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NB5M of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: NUCM protein
    • Protein or peptide: Subunit NI2M of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NB8M of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NIDM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUHM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUBM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: Subunit NUAM of NADH:Ubiquinone Oxidoreductase (Complex I)
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: Subunit NUIM of protein NADH:Ubiquinone Oxidoreductase (Complex I)
  • Protein or peptide: NADH-ubiquinone oxidoreductase chain 5
  • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
  • Protein or peptide: NADH dehydrogenase subunit 2
  • Ligand: DIUNDECYL PHOSPHATIDYL CHOLINE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: CARDIOLIPIN
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: ZINC ION
  • Ligand: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
  • Ligand: DODECYL-BETA-D-MALTOSIDE

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Supramolecule #1: Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxid...

SupramoleculeName: Yarrowia lipolytica mitochondrial complex I (NADH:Ubiquinone oxidoreductase) with NUCM R121M mutation
type: complex / ID: 1 / Parent: 0
Macromolecule list: #1, #10-#11, #15-#19, #2, #20-#29, #3, #30-#39, #4, #40-#42, #5-#9
Source (natural)Organism: Yarrowia lipolytica (yeast)

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Macromolecule #1: NADH-ubiquinone oxidoreductase chain 3

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 14.506339 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
(FME)NTFIIFIIL IPIVGFALLA VNILLAVYKP YNEKLGAFEC GLTSFNQTRL AFNAAFILVA ILFLPFDLEI STLLPY VMS IYLVSNYGFT IVLLFLLILI IGFVYEINTN ALKINKHNKP NTDSLIYKL

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Macromolecule #2: Subunit NUKM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUKM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 23.455176 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLRSQIGRLA LRPTLVPATV IPQTRAYSAP AGTPRVSSSS MPTDFPLPSQ QKPNSAVDYT LTTLDAVANW ARQGSFWPVT FGLACCAVE MMHVSAPRYD QDRLGIIFRA SPRQSDIMIV AGTLTNKMAP VLRQVYDQMP EPRWVISMGS CANGGGYYHF S YSVVRGCD ...String:
MLRSQIGRLA LRPTLVPATV IPQTRAYSAP AGTPRVSSSS MPTDFPLPSQ QKPNSAVDYT LTTLDAVANW ARQGSFWPVT FGLACCAVE MMHVSAPRYD QDRLGIIFRA SPRQSDIMIV AGTLTNKMAP VLRQVYDQMP EPRWVISMGS CANGGGYYHF S YSVVRGCD RIVPVDVYVP GCPPTSEALM YGVFQLQRKM RNTKITRMWY RK

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Macromolecule #3: NUGM protein

MacromoleculeName: NUGM protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 33.64491 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLSRFARIGS MGIRPVAAAR ATFVTSARAA QAAPSWENIK DIRLDPKVHV DEVYEPIVNP ADRYLQHVSD LHQYAKYIMA ALPKYIQGF SVWKDELTLH VAPSAVIPVT TFLRDNTSTQ YKSIIDITAV DYPSRENRFE VVYNFLSVRH NSRIRLKTYA T EVTPVPSI ...String:
MLSRFARIGS MGIRPVAAAR ATFVTSARAA QAAPSWENIK DIRLDPKVHV DEVYEPIVNP ADRYLQHVSD LHQYAKYIMA ALPKYIQGF SVWKDELTLH VAPSAVIPVT TFLRDNTSTQ YKSIIDITAV DYPSRENRFE VVYNFLSVRH NSRIRLKTYA T EVTPVPSI TCLYEGANWF EREAYDMYGV FFEGHPDLRR IMTDYGFEGH PLRKDFPLTG YTEVRWDEEK RRVVYEPLEL TQ AFRNFSA GSTAWEPVGP GRDDRPDSFK LPTPKPEEKE GDKKAAAAAA HHHHHH

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Macromolecule #4: NUCM protein

MacromoleculeName: NUCM protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 52.468906 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLRSAAARAV RAVRPRLSAR YMATTALPQD PIPSGALGQK VPHVDESHQD LLFRTSHMVE DLETYDEDSP INTSDANTRI RAFTINFGP QHPAAHGVLR LILELSGEEI IRSDPHVGLL HMGTEKLIEY KTYMQALPYF DRLDYVSMMT NEQVFSLAVE K LLNVEVPL ...String:
MLRSAAARAV RAVRPRLSAR YMATTALPQD PIPSGALGQK VPHVDESHQD LLFRTSHMVE DLETYDEDSP INTSDANTRI RAFTINFGP QHPAAHGVLR LILELSGEEI IRSDPHVGLL HMGTEKLIEY KTYMQALPYF DRLDYVSMMT NEQVFSLAVE K LLNVEVPL RGKYIRTMFG EITRVLNHLM SVCSHAMDVG ALTPFLWGFE EREKLMEFYE RVSGARLHAA YVRPGGVSQD LP AGLLDDI YMWATQFGDR LDEIEELLTD NRIWKLRTVN IGTVTAQDAL NLGLSGPMLR GSGIPFDIRK NAPYDAYDKV DFD VPVGMN GDCYDRYLIR MAEFRQSLRI IEQCCNDMPA GAVKVEDFKI NSPPRNLMKE DMEALIHHFL LYTKGYSVPP GETY TAIEA PKGEMGVYVV SDGSERPYKC KIRAPGFAHL GAFDHIARGH FLPDAVAIIG TMDLVFGEVD R

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Macromolecule #5: Subunit NUHM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUHM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 27.247402 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLRLIRPRLA ALARPTTRAP QALNARTHIV SVHRNTENNN PSIPFEFSPE NMKRAEEVIA KYPPQYKKAA VMPLLDIGQR QLGYTSISV MNYVAKLLEM PPMRVYEVAT FYTMYNRTPM GRYHLQICTT TPCQLCGSDG IMEAVQNTLN IKPGETTKDN L FTLSEVEC ...String:
MLRLIRPRLA ALARPTTRAP QALNARTHIV SVHRNTENNN PSIPFEFSPE NMKRAEEVIA KYPPQYKKAA VMPLLDIGQR QLGYTSISV MNYVAKLLEM PPMRVYEVAT FYTMYNRTPM GRYHLQICTT TPCQLCGSDG IMEAVQNTLN IKPGETTKDN L FTLSEVEC LGACVNAPMM AINDDYYEDL TPEGTVKLLE DCKAGKMPTP GPENHVRRDC EPASGQKVLL SKEPHNVADF LQ EGI

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Macromolecule #6: Subunit NUBM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUBM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 53.829508 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLRTTLHKRG LARLSRGFAT TQDATPKARQ YGGLKDQDRI FQNLYDNYGW DLASARKQGD WYKTKELILK GDTWIIDEIK KSGLRGRGG AGFPSGLKWS FMNPPGWEKN EGPRYLVVNA DEGEPGTCKD REIMRKDPHK LVEGCLLAGR AMNATAAYIY I RGEFYNEA ...String:
MLRTTLHKRG LARLSRGFAT TQDATPKARQ YGGLKDQDRI FQNLYDNYGW DLASARKQGD WYKTKELILK GDTWIIDEIK KSGLRGRGG AGFPSGLKWS FMNPPGWEKN EGPRYLVVNA DEGEPGTCKD REIMRKDPHK LVEGCLLAGR AMNATAAYIY I RGEFYNEA AVLQTAINEA YAAGLIGKDA CGSGYDFDVY IHRGMGAYVC GEETSLIESL EGKAGKPRLK PPFPAGVGLF GR PSTVTNV ETVAVAPTIL RRGGDWFASF GRERNSGTKL FCISGNVNEP CTVEEEMSIP LRELLEKHCG GIKGGWDNLL GVI PGGCSV PILPKNICED VLMDFDALKD VQSGLGTAAV IVINKQQDVI RAIQRFAAFY KHESCGQCTP CREGTTWLLK AMDR FRTGQ AKEREIDMLY ELTKDIEGHT ICALGDAAAW PIQGLIRNFR PEMETRMKKF HDEVGAVSVG GWMKDARVEK GKVVG APLP GVHH

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Macromolecule #7: Subunit NUAM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUAM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 79.088078 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLSRNLSKFA RAGLIRPATT STHTRLFSVS ARRLAEIELT IDGHKVSIEA GSALIQACEK AGVTVPRYCY HDKLAIAGNC RMCLVDVER APKPVASCAY PVAPGMVVRT DTERVKQARE NVMEMMLQNH PLDCPVCDQG GECDLQDQSM RYGRDRGRFT E ITGKRSTE ...String:
MLSRNLSKFA RAGLIRPATT STHTRLFSVS ARRLAEIELT IDGHKVSIEA GSALIQACEK AGVTVPRYCY HDKLAIAGNC RMCLVDVER APKPVASCAY PVAPGMVVRT DTERVKQARE NVMEMMLQNH PLDCPVCDQG GECDLQDQSM RYGRDRGRFT E ITGKRSTE DKNIGPLVKT SMNRCIHCTR CVRFANDIAG APELGSSGRG NDMQIGTYLE KNLNTELSGN VIDLCPVGAL TN KPYAFRA RPWELKKTES IDVMDAVGSN IRIDSKGVEV MRVIPRVHED VNEEWINDKS RFACDGLKTQ RLTTPLIRVG DKF VNATWD DALSTIAKAY QQKAPKGDEF KAVAGALVEV ESMVALKDMT NALGSENTTT DTPNGNSAPA HGITFRSNYL FNSS IAGIE DADAILLVGT NPRREAAVMN ARIRKAWLRQ ELEIASVGPT LDATFDVAEL GNTHADLEKA LSGEFGEVLK NAKNP LIIV GSGITDREDA GAFFNTIGKF VESTPSVLNE NWNGYNVLQR SASRAGAYDI GFTPSDEASK TTPKMVWLLG ADEVAA SDI PADAFVVYQG HNGDVGAQFA DVVLPGAAYT EKAGTYVNTE GRSQISRAAT GPPGGAREDW KILRAVSEYL GVALPYE DA YEVRDRLAEI SPSLVRYDLV EPTVFGDVAV QHSLVGPNGS VTPSSAPLTE TIENFYMTDS ISRSSPTMAK SSIAFNKD N KKNQAFA

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Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 8
Details: ligands (PLC)(3PE)(3PE) are not in the polypeptide sequence (FME) is at the start of the polypeptide sequence
Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 38.389277 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: (FME)IINIVEILI FLVCVLFSVA YLTVAERKTL AYMQRRLGPN FVGYYGLLQA FADAVKLLLK EIVLPKESNY IILVIS PLI TLITALIGWV VIPLGPGITL GELNLGILFS LAIGSLGVFG SLLSGWSSNS KYSLLGSIRS TAQLISYELI LTSIFII II MFVSSLNITT ...String:
(FME)IINIVEILI FLVCVLFSVA YLTVAERKTL AYMQRRLGPN FVGYYGLLQA FADAVKLLLK EIVLPKESNY IILVIS PLI TLITALIGWV VIPLGPGITL GELNLGILFS LAIGSLGVFG SLLSGWSSNS KYSLLGSIRS TAQLISYELI LTSIFII II MFVSSLNITT IIETQRVVWY CIPLLPLLLI FFIASVAETA RPPFDLTESE SELVAGYFTE YSGSPFVFFF LAEYSNII L ISAFNGYLLL GGYLSFNYSY LFNILFNDYS YVSFLFEGLI NSSAYAIKLV FLMFSFIWVR AAFPRFTYDN LINFCWIIL LPLLFGIFLI IPSTLYIFDS FPTLI

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Macromolecule #9: Subunit NUIM of protein NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUIM of protein NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 9
Details: Ligands (SF4)(SF4) are not in the polypeptide sequence
Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 21.890789 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: SAINIYAGGS AAAAPPAGFR IHRPATWEES EEGALSKATK YFLLAEMFRG LYVVLEQFFR APYTIYYPFE KGPVSPRFRG EHALRRYPS GEERCIACKL CEAICPALAI TIDAEERIDG SRRTTKYDID MTKCIYCGYC QESCPVDAIV ETPNVEYATE T REELLYNK ...String:
SAINIYAGGS AAAAPPAGFR IHRPATWEES EEGALSKATK YFLLAEMFRG LYVVLEQFFR APYTIYYPFE KGPVSPRFRG EHALRRYPS GEERCIACKL CEAICPALAI TIDAEERIDG SRRTTKYDID MTKCIYCGYC QESCPVDAIV ETPNVEYATE T REELLYNK EKLLANGDKW ELELQYALDA DAPYR

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Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 10 / Details: (FME) is in the polypeptide sequence / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 20.793111 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
(FME)MYLTYYFIE ITIFLAILCT IFIISAKNPM VSILYMIALF VIAAMYLYLI GLGIFSLLYI MIYIGAIAVL FLFIIT LLD INSTELSVKS NIRDLPLVLI SLIVLTISGL MIYSNDSILI NKLLEAFGND YNTIITQDWF NIENTTLLTT IGNVLLT NN AFILLVLAIV LLLGIIGPIS ITMKHKE

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Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / type: protein_or_peptide / ID: 11 / Details: (FME) is in the polypeptide sequence / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 9.84386 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
(FME)FIGTIILVL SFLGFVFNRR NIILAFICLE TMLLGINLIL LRNSVLFDDI SGSLFAIVII ILAGVESAIG LSLLVS YYR LRGVINSYGI

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Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 12
Details: ligands (PLC)(3PE)(3PE)(3PE)(3PE) are not in the polypeptide sequence (FME) is in the polypeptide sequence
Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 73.768703 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: (FME)YNAISLIII LPCISWLFPL FFGRQLGYVF VTRMTSTLII ITTLITYYYF YQLLGNNNPI NLELFNYLNI DYLDIN YNF EIDALTITML LAITTISSMV HIYSIGYMET DPHQVRFFSL LSMFTFWMII LVTGSNYFVL FVGWEFIGVT SYLLISF WV TRLQAMKSAL ...String:
(FME)YNAISLIII LPCISWLFPL FFGRQLGYVF VTRMTSTLII ITTLITYYYF YQLLGNNNPI NLELFNYLNI DYLDIN YNF EIDALTITML LAITTISSMV HIYSIGYMET DPHQVRFFSL LSMFTFWMII LVTGSNYFVL FVGWEFIGVT SYLLISF WV TRLQAMKSAL SAVLMNRFGD AFFVLGLCVI AYVFGTLNYS TIFATAYLIN TDLLVLIMLA LFIAAMAKSA QFGLHNWL T LAMEGPTPVS SLLHAATLVT AGIYLLLRSA NILEYTPTVL FIILWIGALT TLSAGLIAIC SNDLKRIIAL STMSQLGMM TIAIGLSAYN LALFHLLGHA FFKALLFMSA GSIIHSILNE SQDIRTYGGL LSYLPYTYIC ITIASLSLMA MPGLTGYYTK DIIIESTYG SYSISNYVVY WIAYLSAVLT CVYSMKILYL TFYSNPNNNT ITYYNAHESN IYITLPMFIL AIFAMFAGWI L KDIYLGVG TDFVGTHILP NNFSYFDTEF SITQFYKLLP LISAILVSIL IVVLNEFFAI VFNLNNKYIN TVYSIFNQKL VS DQILNHF IIFKGLVTSG NIAHHVDKGS LYRLGPVGIN RLLNKASYNV INLSSNTRSS LSMNSMLILI TIVSLLLLVL VMN VNFIIV IPVLISILYI LFS

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13
Details: ligands (CDL)(PLC)(PLC)(3PE)(LMT)(3PE) are not in the polypeptide sequence (FME) is in the polypeptide sequence
Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 54.534652 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: (FME)FLTSILLSS LYLFNRILAW QGNVKHFYLF ASNLLLLFIV VLYINFNTFS NSFQFNFELF NSLNPFGLSN SDISNG LLF GIDGLSLTFI LLTVLLIPLT LLGNWYNINF NSNLYYTLVL AIGLVILLNF WALDYISFYI LFEATLPLLF ILIHIYG SS DSERASFYVL ...String:
(FME)FLTSILLSS LYLFNRILAW QGNVKHFYLF ASNLLLLFIV VLYINFNTFS NSFQFNFELF NSLNPFGLSN SDISNG LLF GIDGLSLTFI LLTVLLIPLT LLGNWYNINF NSNLYYTLVL AIGLVILLNF WALDYISFYI LFEATLPLLF ILIHIYG SS DSERASFYVL MFTLSGSLFM LLSIVVISIV LNTTNFINHN LFVLSLDLQT IIWLGLFIAI MVKTPLFPIH VWLPVVHS E SPLAGSMILA GLILKLALYA ILRLLLPLLC EAQILYTPMI YIISLLTIIL TSLATLRQID LKVIIAYSSI SHMGIAILG VCSNTSLGIY GSIVLGVAHG FVSPALFLIV GGILYDRYHI RIVNYYKGLT TYMPQLATYI IILSFANIGT PLTGNFTGEF LSLQGGFIR NPIIGGISCI SVLLAAIYQL KLTNKLTGGI SSIYMHRTND VTIREKFIMN ILIISTLIIG ICPQIMYNLL Y WTVNNYIY II

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Macromolecule #14: NADH dehydrogenase subunit 2

MacromoleculeName: NADH dehydrogenase subunit 2 / type: protein_or_peptide / ID: 14
Details: ligands (PLC)(PLC)(3PE) are not in the polypeptide sequence (FME) is in the polypeptide sequence
Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 53.381367 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: (FME)LILAIISLI TFVSMSKLSD NRAIIRLINI YLILVLVLDS FLYLLFLNNQ TYTVMGELLI FNSFTFYIDM LIYFIM IVI SSLYGYNLYN NNLYKTLFEP KKELIILFLI NILGALLIVH SNDFITLFVA IELQSYSIYL ITAIYNSSYK ASKASML YF FMGGILSILI ...String:
(FME)LILAIISLI TFVSMSKLSD NRAIIRLINI YLILVLVLDS FLYLLFLNNQ TYTVMGELLI FNSFTFYIDM LIYFIM IVI SSLYGYNLYN NNLYKTLFEP KKELIILFLI NILGALLIVH SNDFITLFVA IELQSYSIYL ITAIYNSSYK ASKASML YF FMGGILSILI AYSINTYYSV LNSYTLHSLD SLIINTLDLN LILIALSLGL LFKIGIAPLH KWLISIYENT PILITIYI S LIPKISILSY LVLSNISINS LVISILAILT LLVGSVGGLL QIKIKRLLAF SGLTNAGYMM LLLLLNNNEF SYLYYITQY SISHLAIFMI IIFSIYYINY INNQYNPIIY VNQLKGLIHD NAYLVLSMAI VVFSFIGIPP LLGFFGKLNI LMSILNNGYY FISIVLIVA SLISALYYLY LLNVSIQDKN NILINSNETV SSVLSYILSS LIILITFGFI YNSLIIDIFN VYFN

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Macromolecule #15: Subunit NUXM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUXM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 15 / Details: (CDL) is not in the polypeptide sequence / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 18.588209 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MSSSTPLVKT SVNYSYGDYP LIDADPHFKR VVGYMRPSDY GVIGLATAAL PAGICFAEWL DPVKGKFARP SVKFLRVATM LGFAVGFGA AYARSSLRFF GVTENAREYK KDEAQMAARK AAGLEPYGTS SLTPELQEIA AKNSAHSIAG LFIFPWFNFV N HPYHGREQ K

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Macromolecule #16: Epimerase domain-containing protein

MacromoleculeName: Epimerase domain-containing protein / type: protein_or_peptide / ID: 16 / Details: (NDP) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 40.488949 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MNSFENLAQD VNITRSGKTL IAKGTGGRSS RTGYTATVFG ANGFLGSYLT AKLAKHGTTV VVPYREEMAK RHLKVTGDLG VVNFLEMDL RNLESIDEAV RHSDIVVNLI GREYETKNFN YYDVHVEGAR RIAEAVKKHN IARYIHVSAF NAEIDSPSEF N HTKGLGEQ ...String:
MNSFENLAQD VNITRSGKTL IAKGTGGRSS RTGYTATVFG ANGFLGSYLT AKLAKHGTTV VVPYREEMAK RHLKVTGDLG VVNFLEMDL RNLESIDEAV RHSDIVVNLI GREYETKNFN YYDVHVEGAR RIAEAVKKHN IARYIHVSAF NAEIDSPSEF N HTKGLGEQ VTKDIVPWAT IVRPAPMFGR EDKWFLDRMA RSPCLVSANK FQETSNPVHV IDVAAALERI CFDDSTVAQT FE LYGPQKF TQKQIIDMVS ETLRKEVRHI ELPKALYQAY TKATQAIWWP TYSPDQVERQ FLSQKIDPSA KTFNDLDLTP MEL PDLMFK LIRPYRVNTF QHDVSQLENK EKTFVHILD

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Macromolecule #17: Subunit NUYM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUYM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 18.65608 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MLSRSLRQLS QPSVRSFATS ARLLQKKDVP EVGVNLDNVP AHEIVSGAPA ELSRNRVVRI YQQAKPATQS GEYGTFAWRL DWDIVDVAN RWENDLIGWQ SSGDYMQATQ MKFTSKESAI KFANKQGWDF YIQEPHHRKF RVKQYANNFV HSYGKLKHIR T K

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Macromolecule #18: zf-CHCC domain-containing protein

MacromoleculeName: zf-CHCC domain-containing protein / type: protein_or_peptide / ID: 18 / Details: (ZN) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 13.133609 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
KSIISYNGNT IEIPEEYTKQ APNRDSTWAP AQASKTEIYK NNMVRFEQKD LSKQPMPYAG IELIAQQPVR FVHGNTAVCD GANHNGPGA QGHPKIFINV DAPGSHACQY CGTRYEKEH

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Macromolecule #19: Subunit NI8M of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NI8M of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 9.621051 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MSAALREIRF HLCQNGSSSA PLRQFVKNQI GAFQKANPST KVLVREANGV KPIVFARFDH GHESKIGLDV SSEKEVAERV KSLIEAK

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Macromolecule #20: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 20 / Details: (EHZ) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 8.821807 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
RPDAEKRIAA VLESFDKISN PAAITPTASF AKDLNLDSLD TVEVVVAIEE EFGIEIPDKE ADEIKSVNQA VEYILAQPDA K

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Macromolecule #21: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 21 / Details: (EHZ) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 9.533592 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
SSAHVLTKDM IQERIVALLE SFDKVNDAKN ITATANLTSD LGLDSLDVVE VVMAIEEEFG LEIPDHDADE IKTVQQAIDY VSAQPAAV

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Macromolecule #22: Subunit NUFM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUFM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 16.65792 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MRYTQLLRNV SKGVQKSGQS VLVQMREGTP IGLTGIYQHP NPRPALIALY EATLKELQDK HPKDSVYRQS IENLTAHRKQ IVEDNEVSE VIENKIGAGL IEEVVIQAHE ELELAKKMSE WKPWEELEEK PLEDQWVYFN KKGVE

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Macromolecule #23: Subunit NB4M of protein NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NB4M of protein NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 14.778818 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MAIIATAFAE TVKFSGSKQE LQKRTLALYR QFLRGAPTFA DLYEVQFSIP TIRTKIRQEF ERHRFVDDLS IQNVLYAKGH MEYQECINF WKQQAQFLKY FPEEDDIQGR HQPSNFVDKF LKNRA

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Macromolecule #24: Subunit NUPM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUPM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 19.355197 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MPREAAAHWV PFEDKANMPD NVPDVVEVGA TSAPLLSASY FIGAKCKPYN DDFMLCREES QGSGAIDCLK EGRRVTRCAV SVIEDINKS CLDEFRLHWQ CLEQNNHQLS GCRKAEALLN KCVFTKLNLE KKIPGLRPDE EPVFLKKDPW IKPAVDDFKS V RAYAEAKK NGTL

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Macromolecule #25: Complex I-B14.7

MacromoleculeName: Complex I-B14.7 / type: protein_or_peptide / ID: 25 / Details: (LMT) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 18.966498 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
HFHPYNTLGL ATQSAMVGLG AGVVAAAARN SLATGPRNIL TTFSKSGGVV TIFTGASIAY VFTYCSAANL RERKDGWNHM WAGAATGAV LGARTKLVPA FIGWTVLCGA ACGLFGWTGA RFNADRKASL EQSPKGFVQE DAHQTFWEVV HRRPLSLTVE Q LGEGRGIN AVPIATATEA PN

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Macromolecule #26: GRIM-19

MacromoleculeName: GRIM-19 / type: protein_or_peptide / ID: 26
Details: ligands (CDL)(3PE) are not in the polypeptide chain
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 13.981233 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
PSVGQDLPPV GGYEPVQWRR NLPARGFRPL VYLAALCGIC GYGFYRALGG IQERRELKRE KLWARIYLMP LLQAEEDRQT VRRSIAQLE REKEIMKGTG FDVDKSVYND GKFHAPALMI PPK

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Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 27 / Details: Ligand (CDL) is not in the polypeptide chain / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 9.675043 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
AIPFEALLPY GIIFGLLTAG GGAMQVLHVY RNGGVRDRFA IDQWDSQMME RDLRLNGGQG RKQVDQATAP EAFKHNHVWK SERPLI

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Macromolecule #28: subunit NI9M of protein NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: subunit NI9M of protein NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 28
Details: ligands (CDL)(3PE)(3PE) are not in the polypeptide chain
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 8.992229 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MINANPGFWN GPFRYLRWSA HNRPHLFFAF AIGIAGPVAA LTLTPLRRKY LYPDHSPLPQ SYPLPQRARE QLTGFDDE

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Macromolecule #29: Subunit NUZM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUZM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 19.772525 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MLPGGPVPVF KKYTVGSKGI WEKLRVLLAI APNRSTGNPI VPLYRVPTPG SRPEANVYQD PSSYPTNDIA ENPYWKRDHR RAYPQTAFF DQKTVTGLLE LGSEATPRIA DGEAGTKALA NIANGGVSFT QALGKSSKDV IYGEVLTVNG LPPVAPTLAP K QWKIIEGE AAIYPKGYPC RTFH

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Macromolecule #30: subunit NEBM of protein NADH:Ubiquinone Oxidoreductase (Complex I...

MacromoleculeName: subunit NEBM of protein NADH:Ubiquinone Oxidoreductase (Complex I) [Yarrowia lipolytica]
type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 7.928171 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
ALFTSLVGAS GLGFATKFLS NKIRLKPAGY YPLGYVFSGV AWAGLGLVLH NVHQHSLEVL EKKKTALSEQ RTE

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Macromolecule #31: Subunit NIPM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NIPM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 10.035651 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MTAAGISLTG GRNRCFSEWQ SFMHCTAKTD AKSRAQCLPN FEDYMECLHH TKEKARLREI ESVLKQKKEG LEAPPVKVIP VKAIGLVEE

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Macromolecule #32: Subunit N7BM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit N7BM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 16.175141 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MSSSLYRVLR NAWEVGPRSY WKQLNSIGDT KSGRLVGTDI YGNKFYETDH QDEIHLRTRY VEYKEKDYDM SQVEPGWHFW LGYGVDTAP CNTPKEKLPI RAYPYKFQPN YTGTPGAFVT YNTLKPKISA WEPVTKQRS

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Macromolecule #33: Subunit NESM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NESM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 28.479941 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString: MLKLHYRNFI TAQHSTTNTT PTMIASVCKR AGLRAGPRAY PGVRQFALRA YNEEKELALK QRLSQLPPPG KAFVTAEGEP RPAKEAELA ELAEIAALYK TDRVGILDIL LLGNKHARLY RDNTALLKDY YYNGRRILDK IPVKDKQTGK VTWEIKREGA E KEDWVNQM ...String:
MLKLHYRNFI TAQHSTTNTT PTMIASVCKR AGLRAGPRAY PGVRQFALRA YNEEKELALK QRLSQLPPPG KAFVTAEGEP RPAKEAELA ELAEIAALYK TDRVGILDIL LLGNKHARLY RDNTALLKDY YYNGRRILDK IPVKDKQTGK VTWEIKREGA E KEDWVNQM YFLYAPSLIL LLIVMVYKSR EDITFWAKKE LDQRVLDKHP EINDAPENER DALIVERIIA GDYDKLASLQ KK ATPTPAT LI

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Macromolecule #34: subunit NUNM of protein NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: subunit NUNM of protein NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 15.818789 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MLRHTVRATQ TLRQARNVRF GSHGHGPELT PAVPFFQPYV LKWAGVSLGL VAFYQFNSSY EAKNGHTWVE TFFHPKSRED ILNEEAKIV QALNNQRELT IKMHELKREE KDYAHSYSPL FSDPVPQGGS IGKAPGSSRE

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Macromolecule #35: Subunit NUUM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUUM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 9.793966 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MGGGRYPFPK DVISMTGGWW ANPSNWKLNG LFATGIAVGL ALWVSTATLP YTRRREGITS ESDISKWNAA AGVWRERHGK ISTGEAAES E

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Macromolecule #36: Subunit NUVM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NUVM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 7.807067 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MAGHHTNYKW NGPLPRPHVS AGHRIATKFL GATMFFWMFL RIKEEYPAML GLHNFYPPKE GEKAVEH

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Macromolecule #37: Subunit NB2M of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NB2M of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 6.948902 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MAPQLKDPWA RREAWRYQTN FTRANRFKGA APGFGIAVVA FGAYLAAEKF LFEKKDDHHH

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Macromolecule #38: Subunit NIAM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NIAM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 17.328523 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MLSRRAVTML RSPVARVAQV QVRGIRASFD KAEEPMLGDY PDIDPFPAQL KNPYKKYDDQ QDRRNLEEPL SVNDDLYDMW SPDRFTHFK NQDALKYFIG FLTIFFGASY VATYFVPEKA AIPREFPYEG LWKESGGTEK SKAFFGQRSE

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Macromolecule #39: Subunit NB5M of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NB5M of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH dehydrogenase
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 10.494885 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MVELKPSSAI QRGPLNKGGW DAPHALHNDG AIDRYAHWRT FYQERFKYTR ATGKSTLIFL VAFPALIGYV AYQSEGLFEF AGKRRGESV TTRG

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Macromolecule #40: Subunit NI2M of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NI2M of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 12.90287 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MSHPVPFSAA NKKLVTSMYR QSLKLARNWI SNRQLFRQKA VEIRHKFDQN AQISNPRLLA RTLDETRAHL YEFRHPDPIV PPSFPGGTK YERNVPPRME KIMQHNLYEP

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Macromolecule #41: Subunit NB8M of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NB8M of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 11.219027 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MAEFPPLLSQ EDMKKHKILL AYRDRCAALL VPLNECRKKN YYMPWACGHE RHEYEMCEVA DFQRRVKAMD KLKAEKIEQA KAAAAAAAA AAAADAEESK

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Macromolecule #42: Subunit NIDM of NADH:Ubiquinone Oxidoreductase (Complex I)

MacromoleculeName: Subunit NIDM of NADH:Ubiquinone Oxidoreductase (Complex I)
type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Yarrowia lipolytica (yeast)
Molecular weightTheoretical: 11.039276 KDa
Recombinant expressionOrganism: Yarrowia lipolytica (yeast)
SequenceString:
MSEHQRPELV SFDDINYNDH KKVREAQESY TREQFIRLEA LKTVRKALEK CYEESGPNHF EDCKNLAEQY LDMLPTHRLQ GYLGYQRND PSK

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Macromolecule #43: DIUNDECYL PHOSPHATIDYL CHOLINE

MacromoleculeName: DIUNDECYL PHOSPHATIDYL CHOLINE / type: ligand / ID: 43 / Number of copies: 6 / Formula: PLC
Molecular weightTheoretical: 622.834 Da
Chemical component information

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

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Macromolecule #44: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 44 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

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Macromolecule #45: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 45 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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Macromolecule #46: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 46 / Number of copies: 5 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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Macromolecule #47: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 47 / Number of copies: 13 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

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Macromolecule #48: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 48 / Number of copies: 5 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #49: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 49 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

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Macromolecule #50: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 50 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #51: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...

MacromoleculeName: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
type: ligand / ID: 51 / Number of copies: 2 / Formula: EHZ
Molecular weightTheoretical: 584.703 Da
Chemical component information

ChemComp-EHZ:
~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate

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Macromolecule #52: DODECYL-BETA-D-MALTOSIDE

MacromoleculeName: DODECYL-BETA-D-MALTOSIDE / type: ligand / ID: 52 / Number of copies: 2 / Formula: LMT
Molecular weightTheoretical: 510.615 Da
Chemical component information

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.45
GridModel: UltrAuFoil / Material: GOLD / Support film - Material: GOLD / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 90 sec. / Details: PEG-thiol treated
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated defocus max: -2.7 µm / Calibrated defocus min: -1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal magnification: 130000
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 2241 / Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 110787 / Details: Post manual curation of Relion auto-pick
Startup modelType of model: EMDB MAP
Details: Low-pass filtered (60 angstroms) in-house map from previous work
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 3.1)
Details: Initial 2D classification to remove junk before the same in 3D classification.
Final 3D classificationNumber classes: 5 / Avg.num./class: 6 / Software - Name: RELION (ver. 3.1) / Details: Grouped good classes
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1) / Details: Using Relion solvent-flattened 3D refinement
Final reconstructionNumber classes used: 1 / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 21013
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6yj4

Output model

PDB-7b0n:
A 3.7-angstrom structure of Yarrowia lipolytica complex I with an R121M mutation in NUCM.

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