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- EMDB-18140: Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially... -

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Basic information

Entry
Database: EMDB / ID: EMD-18140
TitleInward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.
Map dataLocally sharpened consensus map
Sample
  • Complex: Complex I from Bos taurus reconstituted into proteoliposome.
    • Protein or peptide: x 44 types
  • Ligand: x 16 types
KeywordsComplex I / Oxidoreductase / Proteoliposomes / Membrane-bound / metabolism / MEMBRANE PROTEIN
Function / homology
Function and homology information


Complex I biogenesis / Mitochondrial protein import / RHOG GTPase cycle / ubiquinone-6 biosynthetic process / Respiratory electron transport / cellular response to oxygen levels / mitochondrial large ribosomal subunit binding / gliogenesis / neural precursor cell proliferation / [2Fe-2S] cluster assembly ...Complex I biogenesis / Mitochondrial protein import / RHOG GTPase cycle / ubiquinone-6 biosynthetic process / Respiratory electron transport / cellular response to oxygen levels / mitochondrial large ribosomal subunit binding / gliogenesis / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / cellular respiration / Neutrophil degranulation / ubiquinone binding / Mitochondrial protein degradation / NADH:ubiquinone reductase (H+-translocating) / apoptotic mitochondrial changes / NADH dehydrogenase activity / mitochondrial ATP synthesis coupled electron transport / respiratory chain complex I / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / ATP metabolic process / response to cAMP / aerobic respiration / neurogenesis / respiratory electron transport chain / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / fatty acid binding / mitochondrial membrane / electron transport chain / brain development / regulation of protein phosphorylation / mitochondrial intermembrane space / fatty acid biosynthetic process / 2 iron, 2 sulfur cluster binding / positive regulation of fibroblast proliferation / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / oxidoreductase activity / mitochondrial matrix / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / protein-containing complex binding / apoptotic process / mitochondrion / nucleoplasm / metal ion binding / cytoplasm
Similarity search - Function
Complex1_LYR-like / NADH:ubiquinone oxidoreductase, subunit NDUFB4 / : / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 / MNLL subunit / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) ...Complex1_LYR-like / NADH:ubiquinone oxidoreductase, subunit NDUFB4 / : / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 / MNLL subunit / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / Tim17/Tim22/Tim23/Pmp24 family / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, metazoa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, animal type / NADH dehydrogenase 1 beta subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 subunit C2, NDUC2 / NADH-ubiquinone oxidoreductase subunit b14.5b (NDUFC2) / NADH dehydrogenase 1, beta subcomplex, subunit 6 / NADH:ubiquinone oxidoreductase, NDUFB6/B17 subunit / : / NADH:ubiquinone oxidoreductase chain 4, N-terminal / NADH:ubiquinone oxidoreductase, chain 2 / NADH dehydrogenase subunit 2, C-terminal / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / : / NADH-ubiquinone oxidoreductase chain 4, amino terminus / NADH dehydrogenase subunit 2 C-terminus / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / : / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase 1 alpha subcomplex subunit 3 / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase subunit 5, C-terminal / NADH dehydrogenase subunit 5 C-terminus / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / GRIM-19 / GRIM-19 protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NDUFB9, LYR domain / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / Deoxynucleoside kinase domain / Deoxynucleoside kinase / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / : / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH-quinone oxidoreductase subunit 3, ferredoxin-like domain / SLBB domain / : / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-quinone oxidoreductase, chain M/4 / NADH-ubiquinone oxidoreductase chain 4L/K / Complex 1 LYR protein domain / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / Complex 1 protein (LYR family) / NAD(P)H-quinone oxidoreductase subunit D/H / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / : / NADH-quinone oxidoreductase, subunit D / NADH:ubiquinone oxidoreductase, subunit G
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial ...NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 / Acyl carrier protein, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH-ubiquinone oxidoreductase chain 3 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
Similarity search - Component
Biological speciesBos taurus (cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsGrba DN / Hirst J
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_UU_00015/2 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UU_00028/1 United Kingdom
CitationJournal: Science / Year: 2024
Title: Molecular mechanism of the ischemia-induced regulatory switch in mammalian complex I.
Authors: Daniel N Grba / John J Wright / Zhan Yin / William Fisher / Judy Hirst /
Abstract: Respiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and ...Respiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and cellular damage. Ischemic conditions switch complex I from rapid, reversible catalysis into a dormant state that protects upon reoxygenation, but the molecular basis for the switch is unknown. We combined precise biochemical definition of complex I catalysis with high-resolution cryo-electron microscopy structures in the phospholipid bilayer of coupled vesicles to reveal the mechanism of the transition into the dormant state, modulated by membrane interactions. By implementing a versatile membrane system to unite structure and function, attributing catalytic and regulatory properties to specific structural states, we define how a conformational switch in complex I controls its physiological roles.
History
DepositionAug 5, 2023-
Header (metadata) releaseJun 5, 2024-
Map releaseJun 5, 2024-
UpdateJun 26, 2024-
Current statusJun 26, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18140.png

Downloads & links

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Map

FileDownload / File: emd_18140.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLocally sharpened consensus map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 450 pix.
= 479.7 Å		1.07 Å/pix.
x 450 pix.
= 479.7 Å		1.07 Å/pix.
x 450 pix.
= 479.7 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.066 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.025
Minimum - Maximum-0.006772912 - 0.36352578
Average (Standard dev.)-0.000099455756 (±0.005011099)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 479.69998 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18140_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Additional map: Unfiltered consensus map

Fileemd_18140_additional_1.map
AnnotationUnfiltered consensus map
Projections & Slices
AxesZYX

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Additional map: Globally sharpened/postprocessed consensus map

Fileemd_18140_additional_2.map
AnnotationGlobally sharpened/postprocessed consensus map
Projections & Slices
AxesZYX

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Half map: half map 1

Fileemd_18140_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Half map: half map 2

Fileemd_18140_half_map_2.map
Annotationhalf map 2
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Sample components

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Entire : Complex I from Bos taurus reconstituted into proteoliposome.

EntireName: Complex I from Bos taurus reconstituted into proteoliposome.
Components
  • Complex: Complex I from Bos taurus reconstituted into proteoliposome.
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4L
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 5
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: Acyl carrier protein, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: DIUNDECYL PHOSPHATIDYL CHOLINE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: POTASSIUM ION
  • Ligand: UBIQUINONE-10
  • Ligand: CARDIOLIPIN
  • Ligand: ZINC ION
  • Ligand: 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
  • Ligand: CHOLIC ACID
  • Ligand: MYRISTIC ACID

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Supramolecule #1: Complex I from Bos taurus reconstituted into proteoliposome.

SupramoleculeName: Complex I from Bos taurus reconstituted into proteoliposome.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#44
Details: Complex I from Bos taurus, purified as prepared in LMNG, and reconstituted into proteoliposomes.
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 1.09 MDa

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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: Bos taurus (cattle)
Molecular weightTheoretical: 13.086531 KDa
SequenceString:
(FME)NLMLALLTN FTLATLLVII AFWLPQLNVY SEKTSPYECG FDPMGSARLP FSMKFFLVAI TFLLFDLEIA LLLPLP WAS QTANLNTMLT MALFLIILLA VSLAYEWTQK GLEWTE

UniProtKB: NADH-ubiquinone oxidoreductase chain 3

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Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 23.802926 KDa
SequenceString: MAALAALRLL HPILAVRSGV GAALQVRGVH SSMAADSPSS TQPAVSQARA VVPKPAALPS SRGEYVVAKL DDLINWARRS SLWPMTFGL ACCAVEMMHM AAPRYDMDRF GVVFRASPRQ SDVMIVAGTL TNKMAPALRK VYDQMPEPRY VVSMGSCANG G GYYHYSYS ...String:
MAALAALRLL HPILAVRSGV GAALQVRGVH SSMAADSPSS TQPAVSQARA VVPKPAALPS SRGEYVVAKL DDLINWARRS SLWPMTFGL ACCAVEMMHM AAPRYDMDRF GVVFRASPRQ SDVMIVAGTL TNKMAPALRK VYDQMPEPRY VVSMGSCANG G GYYHYSYS VVRGCDRIVP VDIYVPGCPP TAEALLYGIL QLQKKIKREK RLRIWYRR

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

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Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 30.323445 KDa
SequenceString: MAAAVAAAAR GCWQRLVGSA APARVAGRPS VLLLPVRRES SAADTRPTVR PRNDVAHKQL SAFGEYVAEI LPKYVQQVQV SCFNELEIC IHPDGVIPVL TFLRDHSNAQ FKSLADLTAV DIPTRQNRFE IVYNLLSLRF NSRIRVKTYT DELTPIESSV P VYKAANWY ...String:
MAAAVAAAAR GCWQRLVGSA APARVAGRPS VLLLPVRRES SAADTRPTVR PRNDVAHKQL SAFGEYVAEI LPKYVQQVQV SCFNELEIC IHPDGVIPVL TFLRDHSNAQ FKSLADLTAV DIPTRQNRFE IVYNLLSLRF NSRIRVKTYT DELTPIESSV P VYKAANWY EREIWDMFGV FFANHPDLRR ILTDYGFEGH PFRKDFPLSG YVELRYDDEV KRVVAEPVEL AQEFRKFDLN SP WEAFPAY RQPPESLKLE AGDTKPEAK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

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Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 52.678547 KDa
SequenceString: MAALRALCRL RGAAAQVLRP GAGVRLPIQP SRGARQWQPD VEWAEQYGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSNL TLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSLAVE KL LNIRPPPRAQ ...String:
MAALRALCRL RGAAAQVLRP GAGVRLPIQP SRGARQWQPD VEWAEQYGGA VMYPTKETAH WKPPPWNDVD PPKDTLVSNL TLNFGPQHP AAHGVLRLVM ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSLAVE KL LNIRPPPRAQ WIRVLFGEIT RLLNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAYVR PGGVHQDL P LGLMDDIYEF SKNFSLRIDE LEEMLTNNRI WRNRTVDIGI VTAEDALNYG FSGVMLRGSG IQWDLRKTQP YDVYDQVEF DVPIGSRGDC YDRYLCRVEE MRQSIRIISQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGAT YTAIEAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEVDR

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

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Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 27.341496 KDa
SequenceString: MFLSAALRAR AAGLAAHWGK HIRNLHKTAV QNGAGGALFV HRDTPENNPE TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL ...String:
MFLSAALRAR AAGLAAHWGK HIRNLHKTAV QNGAGGALFV HRDTPENNPE TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL FTLIEVECLG ACVNAPMVQI NDNYYEDLTP KDIEEIIDEL KAGKIPKPGP RSGRFSCEPA GGLTSLTEPP KG PGFGVQA GL

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

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Macromolecule #6: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 50.718777 KDa
SequenceString: MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SGYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGAWFASFGR ERNSGTKLFN ISGHVNNPCT VEEEMSVPLK ELIEKHAGGV TGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALIQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV RGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEERMQQFAQ QHQARQAAF

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

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Macromolecule #7: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 79.532219 KDa
SequenceString: MLRIPVRKAL VGLSKSSKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKT KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPVRKAL VGLSKSSKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKT KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNIIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTEPMV RNEKGLLTHT TWE DALSRV AGMLQSFQGN DVAAIAGGLV DAEALIALKD LLNRVDSDTL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVV LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGSHPFSQV LQEAKKPMVI LGSSA LQRN DGAAILAAVS NIAQKIRTSS GVTGDWKVMN ILHRIASQVA ALDLGYKPGV EAIQKNPPKM LFLLGADGGC ITRQDL PKD CFIVYQGHHG DVGAPIADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGMT LPYDTLD QV RNRLEEVSPN LVRYDDVEGA NYFQQASELS KLVNQQLLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGAHA V EEPSIC

UniProtKB: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

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Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 35.716785 KDa
SequenceString: (FME)FMINILMLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DAIKLFIKEP LRPATSSASM FILAPI MAL GLALTMWIPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLM SG SFTLSTLITT ...String:
(FME)FMINILMLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DAIKLFIKEP LRPATSSASM FILAPI MAL GLALTMWIPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLM SG SFTLSTLITT QEQMWLILPA WPLAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFALFFMAEY ANIIMMNI F TAILFLGTSH NPHMPELYTI NFTIKSLLLT MSFLWIRASY PRFRYDQLMH LLWKNFLPLT LALCMWHVSL PILTSGIPP QT

UniProtKB: NADH-ubiquinone oxidoreductase chain 1

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Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 23.9264 KDa
SequenceString: MRCLTMPMLL RALAQAQAAR AGHASVRGLH SSAVAATYKY VNLREPSMDM KSVTDRAAQT LLWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAVCPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV ...String:
MRCLTMPMLL RALAQAQAAR AGHASVRGLH SSAVAATYKY VNLREPSMDM KSVTDRAAQT LLWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAVCPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV EGPNFEFSTE THEELLYNKE KLLNNGDKWE AEIAANIQAD YLYR

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

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Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 19.110488 KDa
SequenceString:
(FME)MLYIVFILS VIFVMGFVGF SSKPSPIYGG LGLIVSGGVG CGIVLNFGGS FLGLMVFLIY LGGMMVVFGY TTAMAT EQY PEIWLSNKAV LGAFVTGLLM EFFMVYYVLK DKEVEVVFEF NGLGDWVIYD TGDSGFFSEE AMGIAALYSY GTWLVIV TG WSLLIGVVVI MEITRGN

UniProtKB: NADH-ubiquinone oxidoreductase chain 6

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Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 10.828195 KDa
SequenceString:
(FME)SMVYMNIMM AFTVSLVGLL MYRSHLMSSL LCLEGMMLSL FVMAALTILN SHFTLASMMP IILLVFAACE AALGLS LLV MVSNTYGTDY VQNLNLLQC

UniProtKB: NADH-ubiquinone oxidoreductase chain 4L

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Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 68.35593 KDa
SequenceString: (FME)NMFSSLSLV TLLLLTMPIM MMSFNTYKPS NYPLYVKTAI SYAFITSMIP TMMFIHSGQE LIISNWHWLT IQTLKL SLS FKMDYFSMMF IPVALFVTWS IMEFSMWYMY SDPNINKFFK YLLLFLITML ILVTANNLFQ LFIGWEGVGI MSFLLIG WW YGRADANTAA ...String:
(FME)NMFSSLSLV TLLLLTMPIM MMSFNTYKPS NYPLYVKTAI SYAFITSMIP TMMFIHSGQE LIISNWHWLT IQTLKL SLS FKMDYFSMMF IPVALFVTWS IMEFSMWYMY SDPNINKFFK YLLLFLITML ILVTANNLFQ LFIGWEGVGI MSFLLIG WW YGRADANTAA LQAILYNRIG DIGFILAMAW FLTNLNTWDL QQIFMLNPSD SNMPLIGLAL AATGKSAQFG LHPWLPSA M EGPTPVSALL HSSTMVVAGI FLLIRFYPLT ENNKYIQSIT LCLGAITTLF TAMCALTQND IKKIIAFSTS SQLGLMMVT IGINQPYLAF LHICTHAFFK AMLFMCSGSI IHSLNDEQDI RKMGGLFKAM PFTTTALIVG SLALTGMPFL TGFYSKDLII EAANTSYTN AWALLMTLIA TSFTAIYSTR IIFFALLGQP RFPTLVNINE NNPLLINSIK RLLIGSLFAG YIISNNIPPT T IPQMTMPY YLKTTALIVT ILGFILALEI SNMTKNLKYH YPSNAFKFST LLGYFPTIMH RLAPYMNLSM SQKSASSLLD LI WLEAILP KTISLAQMKA STLVTNQKGL IKLYFLSFLI TILISMILFN FHE

UniProtKB: NADH-ubiquinone oxidoreductase chain 5

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 52.158758 KDa
SequenceString: (FME)LKYIIPTIM LMPLTWLSKN NMIWVNSTAH SLLISFTSLL LMNQFGDNSL NFSLLFFSDS LSTPLLILTM WLLPLM LMA SQHHLSKENL TRKKLFITML ISLQLFLIMT FTAMELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAG SL PLLVALIYIQ ...String:
(FME)LKYIIPTIM LMPLTWLSKN NMIWVNSTAH SLLISFTSLL LMNQFGDNSL NFSLLFFSDS LSTPLLILTM WLLPLM LMA SQHHLSKENL TRKKLFITML ISLQLFLIMT FTAMELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAG SL PLLVALIYIQ NTVGSLNFLM LQYWVQPVHN SWSNVFMWLA CMMAFMVKMP LYGLHLWLPK AHVEAPIAGS MVLAAVLL K LGGYGMLRIT LILNPMTDFM AYPFIMLSLW GMIMTSSICL RQTDLKSLIA YSSVSHMALV IVAILIQTPW SYMGATALM IAHGLTSSML FCLANSNYER IHSRTMILAR GLQTLLPLMA TWWLLASLTN LALPPTINLI GELFVVMSTF SWSNITIILM GVNMVITAL YSLYMLIMTQ RGKYTYHINN ISPSFTRENA LMSLHILPLL LLTLNPKIIL GPLY

UniProtKB: NADH-ubiquinone oxidoreductase chain 4

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Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 39.302941 KDa
SequenceString: (FME)NPIIFIIIL LTIMLGTIIV MISSHWLLVW IGFEMNMLAI IPIMMKNHNP RATEASTKYF LTQSTASMLL MMAVII NLM FSGQWTVMKL FNPMASMLMT MALAMKLGMA PFHFWVPEVT QGIPLSSGLI LLTWQKLAPM SVLYQIFPSI NLNLILT LS VLSILIGGWG ...String:
(FME)NPIIFIIIL LTIMLGTIIV MISSHWLLVW IGFEMNMLAI IPIMMKNHNP RATEASTKYF LTQSTASMLL MMAVII NLM FSGQWTVMKL FNPMASMLMT MALAMKLGMA PFHFWVPEVT QGIPLSSGLI LLTWQKLAPM SVLYQIFPSI NLNLILT LS VLSILIGGWG GLNQTQLRKI MAYSSIAHMG WMTAVLPYNP TMTLLNLIIY IIMTSTMFTM FMANSTTTTL SLSHTWNK T PIMTVLILAT LLSMGGLPPL SGFMPKWMII QEMTKNNSII LPTFMAITAL LNLYFYMRLT YSTTLTMFPS TNNMKMKWQ FPLMKKMTFL PTMVVLSTMM LPLTPMLSVL E

UniProtKB: NADH-ubiquinone oxidoreductase chain 2

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Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 39.330984 KDa
SequenceString: MALRLLRLVP PRVGGIHTSV QFKLQYGPLA YILGEKATKK MTEKSKLITV DGNICSGKSK LAKEIAEKLG LKHFPEAGIH YVDSTTGDG KPLPVQFSGN CSLEKFYDDP KSNDGNSYRL QAWLYASRLL QYADALEHLL STGQGVVLER SIYSDFVFLE A MYRQGFIR ...String:
MALRLLRLVP PRVGGIHTSV QFKLQYGPLA YILGEKATKK MTEKSKLITV DGNICSGKSK LAKEIAEKLG LKHFPEAGIH YVDSTTGDG KPLPVQFSGN CSLEKFYDDP KSNDGNSYRL QAWLYASRLL QYADALEHLL STGQGVVLER SIYSDFVFLE A MYRQGFIR KQCVDHYNQV KKVTICEYLP PHVVVYVDVP VPEVQSRIQK KGNPHEMKIT SAYLQDIENA YKGTFLPEMS EK CEVLQYS AWEAQDAEKV VEDIEYLKYD KGPWLDQNDR KLHKLRMLVQ DKLEVLNYTS IPVFLPEVTV GAHQSDQVFQ EFT ELPGRK YRAGYNEDVG DKWIWLK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial

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Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 42.91343 KDa
SequenceString: MAAAVHPRVV RVLPMSRSSV PALAASVFHS PPQRQLHHAV IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPHRCEPY DTMHLRPMGD LGQIIFMDWN GRDKDSIRRA VEHSSVVINL VGREWETQNF DFEDVFVKIP QAIAQVSKEA G VEKFIHIS ...String:
MAAAVHPRVV RVLPMSRSSV PALAASVFHS PPQRQLHHAV IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPHRCEPY DTMHLRPMGD LGQIIFMDWN GRDKDSIRRA VEHSSVVINL VGREWETQNF DFEDVFVKIP QAIAQVSKEA G VEKFIHIS HLNADIKSSS KYLRSKAVGE KEVRETFPEA TIIKPAEIFG REDRFLNYFA NIRWFGGVPL ISLGKKTVKQ PV YIVDVTK GIINAIKDPD ARGKTFAFVG PSRYLLFDLV QYVFAVAHRP FLPYPLPHFA YRWIGRLFEI SPFEPWTTRD KVE RIHTTD KILPHLPGLE DLGVEATPLE LKAIEVLRRH RTYRWLSSEI EDVQPAKTIP TSGP

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

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Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 19.841555 KDa
SequenceString:
MAAVSMSVAL RQALWGRRVA TVAAVSVSKV STRSLSTSTW RLAQDQTRDT QLITVDEKLD ITTITGVPEE HIKTRKARIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWASTAD PLSNLVLTFS TKEDAVAFAE KNGWSYDVEE RKVPKPKSKS Y GANFSWNK RTRVSTK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

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Macromolecule #18: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 13.433194 KDa
SequenceString:
MAAVLTFLRF LGRGGAVTRG LPGGARCFGV RTSPTGEKVT HTGQVYDDGD YRKVRFVGRQ KEVNENFAID LIAEQPVSQV GSRVISCDG GGGALGHPRV YINLDKETKT GTCGYCGLQF RQQHH

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

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Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 11.097824 KDa
SequenceString:
MAAAAAIRGV RGKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD VQPKLWARYA FGQEKNVSLN NFSADQVTR ALENVLSSKA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

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Macromolecule #20: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 20 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 17.42134 KDa
SequenceString:
MAVRVLCACV RRLPTAFAPL PRLPTLAAAR PLSTTLFAAE TRTRPGAPLP ALVLAQVPGR VTQLCRQYSD APPLTLEGIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

UniProtKB: Acyl carrier protein, mitochondrial

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Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 13.334608 KDa
SequenceString:
MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGHIPK NAAYRKYTEQ ITNEKLSMVK AEPDVKKLEE RLQGGQIEEV ILQAENELS LARKMIQWKP WEPLVEEPPA SQWKWPI

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

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Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 15.083544 KDa
SequenceString:
MAASGLRQAA VAASTSVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHLF QLDISVKQGR DKVREMFKKN AHITDPRVVD LLVIKGKME LEETIKVWKQ RTHVMRFFHE TEAPRPKDFL SKFYVGHDP

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

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Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 20.124133 KDa
SequenceString:
MPGIVELPSL EDLKVQEVKV SSSVLKAAAH HYGAQCDKPN KEFMLCRWEE KDPRRCLEEG KLVNQCALEF FRQIKRHCAE PFTEYWTCI DYSGLQLFRR CRKQQAQFDE CVLDKLGWVR PDLGDLSKVT KVKTDRPLPE NPYHSRARPE PNPEVEGDLK P ARHGSRLF FWTM

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

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Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 14.814058 KDa
SequenceString:
M(AYA)KTVLRQYW DIPEGTECHR KTYATTSIGG AAGLVVSAYS VALKTPTSFL EGVARTGRYT FTAAAIGAIF GLTSCI SAQ VREKPDDPLN YLIGGCAGGL ILGARTRSYG IGAAACAYMG LTAALVKMGQ LEGWQVFAEP KV

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

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Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 16.694395 KDa
SequenceString:
MAASKVKQDM PPVGGYGPID YKRNLPRRGL SGYSMFAVGI GALLFGYWSM MKWNRERRRL QIEDFEARIA LMPLLQAEKD RRVLQMLRE NLEEEATVMK DVPGWKVGES VFHTTRWVTP MMGELYGLRA SEEVLSATYG FIWYT

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

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Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 8.117445 KDa
SequenceString:
MWFEVLPGIA VMGVCLFIPG MATARIHRFS NGGKEKRVAH YPYQWYLMER DRRVSGVNRS YVSKGLENID

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

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Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 9.399887 KDa
SequenceString:
M(AYA)ERVAAFLK NVWAKEPVLV ASFAIAGLAV ILPTLSPYTK YSLMINRATP YNYPVPLRDD GNMPDVPSHP QDPQGP SLE WLKRL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

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Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 8.796211 KDa
SequenceString:
MAPSALLRPF WKLLAPARFP SVSSSRSKFY IQEPPHGSPN WLKVGLTLGT SVFLWIYLIK QHNEDVLEYK RRNGLE

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

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Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 subunit C2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C2 / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 14.159332 KDa
SequenceString:
(AME)MTGRQGRAT FQFLPDEARS LPPPKLTDPR LAFVGFLGYC SGLIDNAIRR RPVLLAGLHR QLLYITSFVF VGYYLL KRQ DYMYAVRDHD MFSYIKSHPE DFPEKDKKTY GEVFEEFHPV R

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C2

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Macromolecule #30: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 12.694671 KDa
SequenceString:
MPFFDVQKRL GVDLDRWMTI QSAEQPHKIP SRCHAFEKEW IECAHGIGSI RAEKECKIEF EDFRECLLRQ KTMKRLHAIR RQREKLIKE GKYTPPPHHS GQEEPRS

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

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Macromolecule #31: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 6.978148 KDa
SequenceString:
MNLLQVVRDH WVHVLVPMGF VFGYYLDRKN DEKLTAFRNK SLLYKRELKP NEEVTWK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1

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Macromolecule #32: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 17.594945 KDa
SequenceString:
MAARMLGLCG RRLLAVAATR GLPAARVRWE SSSSRAVIAP STLAGKRPSE PTLRWQEDPE PEDENLYEKN PDSHGYDKDP AVDIWNMRV VFFFGFSIVL VLGSTFVAYL PDYRMQEWAR REAERLVKYR EAHGLPIMES NCFDPSKIQL PEDED

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial

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Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 21.624135 KDa
SequenceString:
MAAMSLLHRA SVSAVAALSG RRLGTRLGFG GFLTRDFPKT VAPVRHSGDH GKRLFIIKPS GFYDKRFLKL LRFYILLTGI PVAIGITLI NVFIGEAELA EIPEGYVPEH WEYFKHPISR WIARTFFDGP EKNYERTMAI LQIEAEKAEL RLKELEVRRL M RARGDGPW FHYPTIDKEL IDHSPKATPD N

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial

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Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 15.592122 KDa
SequenceString:
M(SAC)GYTPEEKL RLQQLRELRR RWLKDQELSP REPVLPPQRV SPVERFWNKF LQDGALWKNV IYKTYRHSIF AFTHVL IPV WIIHYYLKYH VTTKPYTIVE KKPRIFPGDT ILETGEVIPP MKEFPDQHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

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Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 12.298858 KDa
SequenceString:
MAGMSALKRL APFAHVGGHL FRGRCARAAG ARGVRRAGGG AHIEPRYRQF PQLTRSQVIQ AEFFSATMWF WILWRFWHDS DAVLGHFPY PDPSQWTDEE LGIPPDDED

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial

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Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 11.160705 KDa
SequenceString:
MAHGHGHEHG PSKMELPDYK QWKIEGTPLE TVQEKLAARG LRDPWGRNEA WRYMGGFANN VSFVGALLKG FKWGFAAFVV AIGAEYYLE SQKKDKKHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

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Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 21.678459 KDa
SequenceString:
MAAARAGVLG VRWLQKAARN VVPLGARTAS HITKDMLPGP YPKTPEERAA AAKKYNMRVE DYEPYPDDGT GYGDYPKLPD RSQQERDPW YDWDHPDLRL NWGEPMHWDL DMYIRNRVDT SPTPVNWNLM CKHLFGFVAF MLFMFWVGET YPAYQPVGPK Q YPYNNLYL ERGGDPNKEP EPVVHYEI

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial

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Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 15.248297 KDa
SequenceString:
M(SAC)FPKYEASR LSSLPTTLDP AEYDISSETR KAQAERLAIR SRLKREYQLQ YYDPSRRGVI EDPALVRWTY ARSANI YPN FRPNTKTSLL GALFGIGPLV FWYYVFKTDR DRKEKLIQEG KLDRTFNISY

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

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Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 21.827889 KDa
SequenceString:
MAFLSSGAYL THQQKVLRLY KRALRHLESW CIHRDKYRYF ACLLRARFDE HKNEKDMVKA TQLLREAEEE FWHGQHPQPY IFPESPGGT SYERYECYKV PEWCLDDWHP SEKAMYPDYF AKREQWKKLR RESWEREVKQ LQEETPVGGP RTEALPPARK Q GDLPPLWW HIVTRPRERP M

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

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Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 16.428846 KDa
SequenceString:
MGAHLARRYL GDASVEPDPL RMPTFPPDYG FPERKEREMV ATQQEMNDAQ LVLQQRDYCA HYLIRFLKCK RDSFPNFLAC KHERHDWDY CEHLDYVKRM KEFERERRLL QRKKRREQRE ADMAKGLGPG EVAPEVAL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

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Macromolecule #41: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 21.0009 KDa
SequenceString:
MPDSWDKDVY PEPPRRTPAP SPQTSLPNPI TYLTKAFDLL VDRPVTLVRE FIERQHAKNK YYYYHREFRR VPDITECQEK DVLCMFEAE MQWRRDYKVD QEIVNIIQER LKACQQREGE SHRQNCAKEL EQFTQVVKAY QDRYHDLGAH YSARKCLAKQ K QRMLAERK AAKEAAAA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

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Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 17.157547 KDa
SequenceString:
(AME)ELLQVLKRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG KNTFWD VDG SMVPPEWHRW LHCMTDDPPT VKPPTARKFI WTNHKFNLSG TPQQYVPYST TRKKIQEWVP PSTPYK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

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Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 12.73762 KDa
SequenceString:
M(AYA)SATRFIQW LRNWASGRDL QAKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR REAMPPSIVM SSQKVL VAG KPAESSAVAA SEKKAVSPAP PIKRWELSQD EPYL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

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Macromolecule #44: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 44 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Molecular weightTheoretical: 11.874492 KDa
SequenceString:
MAASLLLRQG RAGALKTVLL EAGVFRGVAP AVSLSAESGK NEKGLPPNPK KQSPPKKPVS AAPTEPFDNT TYKNLQHHDY STYTFLDLN LDLSKFRMPQ PSSGRESPRH

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

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Macromolecule #45: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 45 / Number of copies: 15 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

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Macromolecule #46: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 46 / Number of copies: 26 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

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Macromolecule #47: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 47 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

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Macromolecule #48: DIUNDECYL PHOSPHATIDYL CHOLINE

MacromoleculeName: DIUNDECYL PHOSPHATIDYL CHOLINE / type: ligand / ID: 48 / Number of copies: 5 / Formula: PLC
Molecular weightTheoretical: 622.834 Da
Chemical component information

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

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Macromolecule #49: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 49 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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Macromolecule #50: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 50 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

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Macromolecule #51: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 51 / Number of copies: 1 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #52: UBIQUINONE-10

MacromoleculeName: UBIQUINONE-10 / type: ligand / ID: 52 / Number of copies: 1 / Formula: U10
Molecular weightTheoretical: 863.343 Da
Chemical component information

ChemComp-U10:
UBIQUINONE-10

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Macromolecule #53: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 53 / Number of copies: 8 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #54: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 54 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #55: 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 55 / Number of copies: 1 / Formula: DGT
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-DGT:
2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

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Macromolecule #56: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 56 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #57: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 57 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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Macromolecule #58: ~{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: 58 / 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 #59: CHOLIC ACID

MacromoleculeName: CHOLIC ACID / type: ligand / ID: 59 / Number of copies: 1 / Formula: CHD
Molecular weightTheoretical: 408.571 Da
Chemical component information

ChemComp-CHD:
CHOLIC ACID

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Macromolecule #60: MYRISTIC ACID

MacromoleculeName: MYRISTIC ACID / type: ligand / ID: 60 / Number of copies: 1 / Formula: MYR
Molecular weightTheoretical: 228.371 Da
Chemical component information

ChemComp-MYR:
MYRISTIC ACID

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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

Concentration0.2 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
10.0 mMC7H15NO4S3-(N-morpholino)propanesulfonic acid
50.0 mMKClpotassium chloride
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III
Details: Sample was incubated on grid for 30 s before plunge freezing.
DetailsComplex I proteoliposomes on a graphene-oxide coated gold grid with even liposome distribution.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 27014 / Average exposure time: 2.67 sec. / Average electron dose: 45.4 e/Å2
Details: The data were collected with aberration-free image shift (AFIS).
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 0.9 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0-beta) / Number images used: 30701
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 4.0-beta)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0-beta)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

7qsn


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-8q47:
Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.

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