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Entry
Database: EMDB / ID: EMD-35337
TitleRespiratory complex Peripheral Arm of CI, focus-refined map of type IB, Wild type mouse under cold temperature
Map dataFocus-refined map, Peripheral Arm, Cold Acclimated, Type IB of Respiratory Supercomplex
Sample
  • Complex: Respiratory Supercomplex CI:CIII2
    • Protein or peptide: x 23 types
  • Ligand: x 11 types
KeywordsRespiratory complex / Respiratory supercomplex / ELECTRON TRANSPORT
Function / homology
Function and homology information


response to injury involved in regulation of muscle adaptation / reproductive system development / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / Respiratory electron transport / protein insertion into mitochondrial inner membrane / blastocyst hatching / circulatory system development ...response to injury involved in regulation of muscle adaptation / reproductive system development / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / Respiratory electron transport / protein insertion into mitochondrial inner membrane / blastocyst hatching / circulatory system development / respiratory system process / psychomotor behavior / ubiquinone-6 biosynthetic process / Mitochondrial protein degradation / response to light intensity / cellular response to oxygen levels / iron-sulfur cluster assembly complex / : / mitochondrial large ribosomal subunit binding / gliogenesis / cellular response to glucocorticoid stimulus / neural precursor cell proliferation / cardiac muscle tissue development / [2Fe-2S] cluster assembly / oxygen sensor activity / adult walking behavior / response to hydroperoxide / iron-sulfur cluster assembly / adult behavior / dopamine metabolic process / NADH:ubiquinone reductase (H+-translocating) / positive regulation of execution phase of apoptosis / proton motive force-driven mitochondrial ATP synthesis / 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 / neuron development / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / cellular response to interferon-beta / negative regulation of intrinsic apoptotic signaling pathway / quinone binding / cellular response to retinoic acid / muscle contraction / extrinsic apoptotic signaling pathway / tricarboxylic acid cycle / aerobic respiration / visual perception / response to hormone / neurogenesis / respiratory electron transport chain / reactive oxygen species metabolic process / kidney development / regulation of mitochondrial membrane potential / synaptic membrane / mitochondrion organization / fatty acid metabolic process / mitochondrial membrane / sensory perception of sound / brain development / regulation of protein phosphorylation / negative regulation of cell growth / multicellular organism growth / response to organic cyclic compound / mitochondrial intermembrane space / cognition / 2 iron, 2 sulfur cluster binding / circadian rhythm / positive regulation of protein catabolic process / NAD binding / FMN binding / myelin sheath / nervous system development / 4 iron, 4 sulfur cluster binding / protease binding / neuron apoptotic process / response to oxidative stress / mitochondrial inner membrane / electron transfer activity / nuclear body / response to hypoxia / mitochondrial matrix / inflammatory response / response to xenobiotic stimulus / innate immune response / negative regulation of DNA-templated transcription / neuronal cell body / ubiquitin protein ligase binding / dendrite / synapse / protein-containing complex binding / protein-containing complex / mitochondrion / nucleoplasm
Similarity search - Function
NmrA-like domain / NmrA-like family / Complex1_LYR-like / NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / : / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain ...NmrA-like domain / NmrA-like family / Complex1_LYR-like / NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / : / 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 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 / GRIM-19 / GRIM-19 protein / 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 / 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 / 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 / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / NADH dehydrogenase, subunit C / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / 2Fe-2S iron-sulfur cluster binding domain / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / CHCH / CHCH domain / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NuoE domain / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / NADH-quinone oxidoreductase subunit E-like / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / Thioredoxin-like [2Fe-2S] ferredoxin / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / [NiFe]-hydrogenase, large subunit / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Acyl carrier protein (ACP) / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial ...NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / Acyl carrier protein, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsShin Y-C / Liao M
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)RO1 DK081418 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)RO1 DK089883 United States
CitationJournal: Cell / Year: 2024
Title: Structural basis of respiratory complex adaptation to cold temperatures.
Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / ...Authors: Young-Cheul Shin / Pedro Latorre-Muro / Amina Djurabekova / Oleksii Zdorevskyi / Christopher F Bennett / Nils Burger / Kangkang Song / Chen Xu / Joao A Paulo / Steven P Gygi / Vivek Sharma / Maofu Liao / Pere Puigserver /
Abstract: In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold ...In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold exposure remains elusive. Herein, we combined thermoregulatory physiology and cryoelectron microscopy (cryo-EM) to study endogenous respiratory supercomplexes from mice exposed to different temperatures. A cold-induced conformation of CI:III (termed type 2) supercomplex was identified with a ∼25° rotation of CIII around its inter-dimer axis, shortening inter-complex Q exchange space, and exhibiting catalytic states that favor electron transfer. Large-scale supercomplex simulations in mitochondrial membranes reveal how lipid-protein arrangements stabilize type 2 complexes to enhance catalytic activity. Together, our cryo-EM studies, multiscale simulations, and biochemical analyses unveil the thermoregulatory mechanisms and dynamics of increased respiratory capacity in brown fat at the structural and energetic level.
History
DepositionFeb 10, 2023-
Header (metadata) releaseSep 18, 2024-
Map releaseSep 18, 2024-
UpdateNov 6, 2024-
Current statusNov 6, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35337.png

Downloads & links

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Map

FileDownload / File: emd_35337.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocus-refined map, Peripheral Arm, Cold Acclimated, Type IB of Respiratory Supercomplex
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 384 pix.
= 422.4 Å		1.1 Å/pix.
x 384 pix.
= 422.4 Å		1.1 Å/pix.
x 384 pix.
= 422.4 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.55
Minimum - Maximum-2.0358446 - 6.196432
Average (Standard dev.)0.001145139 (±0.088341594)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 422.40002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_35337_msk_1.map
Projections & Slices
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Histogram (log scale)

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Half map: Focus-refined map, Peripheral Arm, Cold Acclimated, Type IB...

Fileemd_35337_half_map_1.map
AnnotationFocus-refined map, Peripheral Arm, Cold Acclimated, Type IB of Respiratory Supercomplex
Projections & Slices
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Histogram

Histogram (log scale)

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Half map: Focus-refined map, Peripheral Arm, Cold Acclimated, Type IB...

Fileemd_35337_half_map_2.map
AnnotationFocus-refined map, Peripheral Arm, Cold Acclimated, Type IB of Respiratory Supercomplex
Projections & Slices
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Slices (1/2)
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Histogram (log scale)

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Sample components

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Entire : Respiratory Supercomplex CI:CIII2

EntireName: Respiratory Supercomplex CI:CIII2
Components
  • Complex: Respiratory Supercomplex CI:CIII2
    • 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 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 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 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-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: UBIQUINONE-1
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: Ubiquinone-9
  • 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: CARDIOLIPIN

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Supramolecule #1: Respiratory Supercomplex CI:CIII2

SupramoleculeName: Respiratory Supercomplex CI:CIII2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#23
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 1.32 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: Mus musculus (house mouse)
Molecular weightTheoretical: 13.223775 KDa
SequenceString:
MNLYTVIFIN ILLSLTLILV AFWLPQMNLY SEKANPYECG FDPTSSARLP FSMKFFLVAI TFLLFDLEIA LLLPLPWAIQ TIKTSTMMI MAFILVTILS LGLAYEWTQK 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: Mus musculus (house mouse)
Molecular weightTheoretical: 24.715912 KDa
SequenceString: MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV PKLSHLPRSR AEYVVTKLDD LINWARRSS LWPMTFGLAC CAVEMMHMAA PRYDMDRFGV VFRASPRQAD VMIVAGTLTN KMAPALRKVY DQMPEPRYVV S MGSCANGG ...String:
MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV PKLSHLPRSR AEYVVTKLDD LINWARRSS LWPMTFGLAC CAVEMMHMAA PRYDMDRFGV VFRASPRQAD VMIVAGTLTN KMAPALRKVY DQMPEPRYVV S MGSCANGG GYYHYSYSVV RGCDRIVPVD IYVPGCPPTA EALLYGILQL QRKIKREQKL KIWYRR

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: Mus musculus (house mouse)
Molecular weightTheoretical: 30.191307 KDa
SequenceString: MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHP DGVIPTLTFL RDHTNAQFKS LADLTAVDVP TRQNRFEIVY NLLSLRFNSR IRVKTYADEL TPIDSIVSVH I AANWYERE ...String:
MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHP DGVIPTLTFL RDHTNAQFKS LADLTAVDVP TRQNRFEIVY NLLSLRFNSR IRVKTYADEL TPIDSIVSVH I AANWYERE VWDMFGVFFF NHPDLRRILT DYGFEGHPFR KDFPLTGYVE LRYDDEVKRV VAEPVELAQE FRKFDLNSPW EA FPAYRQP PESLKLEAGD KKPETK

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: Mus musculus (house mouse)
Molecular weightTheoretical: 52.693559 KDa
SequenceString: MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVEKLL N IQPPPRAQ ...String:
MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVEKLL N IQPPPRAQ WIRVLFGEIT RILNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAYIR PGGVHQDLPL GL LDDIYEF SKNFSLRIDE VEEMLTNNRI WRNRTVDIGV VTAEDALNYG FSGVMLRGSG IQWDLRKTQP YDVYDQVEFD VPI GSRGDC YDRYLCRVEE MRQSLRIIEQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGAT YTAI EAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEIDR

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: Mus musculus (house mouse)
Molecular weightTheoretical: 27.318336 KDa
SequenceString: MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF ...String:
MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTPK DIEEIIDELK AGKVPKPGPR SGRFCCEPAG GLTSLTEPPK GP GFGVQAG L

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: Mus musculus (house mouse)
Molecular weightTheoretical: 50.904152 KDa
SequenceString: MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SDYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGTWFAGFGR ERNSGTKLFN ISGHVNHPCT VEEEMSVPLK ELIEKHAGGV TGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALVQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV KGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEDRMQRFAQ QHRAWQAAS

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: Mus musculus (house mouse)
Molecular weightTheoretical: 79.866688 KDa
SequenceString: MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNVIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTEPMV RNEKGLLTYT SWE DALSRV AGMLQNFEGN AVAAIAGGLV DAEALVALKD LLNKVDSDNL CTEEIFPTEG AGTDLRSNYL LNTTIAGVEE ADVV LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGRHSFCEV LKDAKKPMVV LGSSA LQRD DGAAILVAVS NMVQKIRVTT GVAAEWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKM LFLLGADGGC ITRQDL PKD CFIVYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGIT LPYDTLD QV RNRLEEVSPN LVRYDDIEET NYFQQASELA KLVNQEVLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGAQA 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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 36.077016 KDa
SequenceString: MFFINILTLL VPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP MRPLTTSMSL FIIAPTLSLT LALSLWVPL PMPHPLINLN LGILFILATS SLSVYSILWS GWASNSKYSL FGALRAVAQT ISYEVTMAII LLSVLLMNGS Y SLQTLITT ...String:
MFFINILTLL VPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP MRPLTTSMSL FIIAPTLSLT LALSLWVPL PMPHPLINLN LGILFILATS SLSVYSILWS GWASNSKYSL FGALRAVAQT ISYEVTMAII LLSVLLMNGS Y SLQTLITT QEHMWLLLPA WPMAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFALFFMAEY TNIILMNALT TI IFLGPLY YINLPELYST NFMMEALLLS STFLWIRASY PRFRYDQLMH LLWKNFLPLT LALCMWHISL PIFTAGVPPY M

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: Mus musculus (house mouse)
Molecular weightTheoretical: 24.068355 KDa
SequenceString: MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI LMWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAICPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV ...String:
MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI LMWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAICPAQAIT 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 dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 42.588129 KDa
SequenceString: MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG ATGFLGRYVV NHLGRMGSQV IIPYRCDVY DIMHLRLMGD LGQLTFLEWD ARDKDSIRKA VQHSNVVINL IGREWETRNF DFEDVFVNIP RAIAQASKEA G VERFIHVS ...String:
MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG ATGFLGRYVV NHLGRMGSQV IIPYRCDVY DIMHLRLMGD LGQLTFLEWD ARDKDSIRKA VQHSNVVINL IGREWETRNF DFEDVFVNIP RAIAQASKEA G VERFIHVS HLNASMKSSS KSLRSKAVGE KEVRSVFPEA IIIRPSDIFG REDRFLNHFA NYRWFLAVPL VSLGFKTVKQ PV YVADVSK GIVNATKDPD AVGKTFAFTG PNRYLLFHLV KYIFGMTHRT FIPYPLPLFV YSWIGKLFGL SPFEPWTTKD KVE RIHISD VMPTDLPGLE DLGVQPTPLE LKSIEVLRRH RTYRWLSSEI EETKPAKTVN Y

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

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Macromolecule #11: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 19.814725 KDa
SequenceString:
MAAVSISVSL RQAMLGRRAM ATAAVSVCRV PSRLLSTSTW KLADNQTRDT QLITVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWASTAD PLSNMVLTFS AKEDAIAFAE KNGWSYDVEE KKVPKPKSKS Y GANFSWNK RTRVSTK

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

+
Macromolecule #12: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 13.041828 KDa
SequenceString:
MAAVLTFRRL LTLPRAARGF GVQVSPSGEK ITHTGQVYDE KDYRRVRFVD RQKEVNENFA IDLIAQQPVN EVEHRIIACD GGGGALGHP KVYINLDKET KTGTCGYCGL QFKQHHH

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

+
Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.932675 KDa
SequenceString:
MAAAAASRAV GAKLGLREIR VHLCQRSPGS QGVRDFIVQR YVELKKAHPN LPILIRECSE VQPKLWARYA FGQEKTVSLN NLSADEVTR AMQNVLSGKA

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

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Macromolecule #14: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 17.390289 KDa
SequenceString:
MASRVLCACV RRLPAAFAPL PRLPTLALAR PLSTTLCPEG IRRRPGALQS ALALAQVPGT VTHLCRQYSD APPLTLDGIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

UniProtKB: Acyl carrier protein, mitochondrial

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Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 13.380719 KDa
SequenceString:
MAGLLKKTTG LVGLAVCDTP HERLTILYTK TLDILKHFPK HAAYRKYTEQ ITNEKLDMVK AEPDVKKLEA LLQGGEVEEV ILQAEKELS LARKMLKWKP WEPLVEEPPA NQWKWPI

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

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Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 15.311858 KDa
SequenceString:
MAAAATGLRQ AAAAAASTSV KPIFSRDLNE AKRRVRELYR AWYREVPNTV HLMQLDITVK QGRDKVREMF MKNAHVTDPR VVDLLVIKG KMELQETIKV WKQRTHVMRF FHETETPRPK DFLSKFYMGH DP

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

+
Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 20.025127 KDa
SequenceString:
MPGIVELPTL EELKVEEVKV SSAVLKAAAH HYGAQCDKTN KEFMLCRWEE KDPRRCLKEG KLVNGCALNF FRQIKSHCAE PFTEYWTCL DYSNMQLFRH CRQQQAKFDQ CVLDKLGWVR PDLGQLSKVT KVKTDRPLPE NPYHSRARPE PNPVIEGDLK P AKHGTRFF FWTV

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

+
Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 16.881588 KDa
SequenceString:
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMFAVGI GALIFGYWRM MRWNQERRRL LIEDLEARIA LMPLFQAEKD RRTLQILRE NLEEEAIIMK DVPNWKVGES VFHTTRWVPP LIGEMYGLRT KEEMSNANFG FTWYT

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

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 8.149524 KDa
SequenceString:
MWFEILPGLA IMGVCLVIPG VSTAYIHKFT NGGKEKRVAR VQYQWYLMER DRRISGVNRY YVSKGLENID

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

+
Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 9.338867 KDa
SequenceString:
MAGRISAFLK NAWAKEPVLV VSFSVWGLAI IMPMISPYTK YASMINKATP YNYPVPVRDD GNMPDVPSHP QDPLGPSLDW LKNL

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

+
Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 17.112416 KDa
SequenceString:
MELVEVLKRG VQQVTGHGGL RGLLRVFFRA NDIRIGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG KNTFWDVDGS MVPPEWHRW LHCMTDDPPT TNPPTARKFI WTNHKFNVSA TPEQYVPYST TRKKIHEWVP PSTPYK

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

+
Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 12.595592 KDa
SequenceString:
MASATRVIQK LRNWASGQDL QAKLQLRYQE IAKRTQPPPK LPVGPSHKLS NNYYCTRDGR REVVPPSIIM SSQKALVSGK AAESSAMAA TEKKAVTPAP PMKRWELSKD QPYL

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

+
Macromolecule #23: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.833504 KDa
SequenceString:
MAVSLLLRGG RIRALKAVLL EARVFPGELV SVVRLSTESE KSAKEKELHP KTQSVLKEPE PTDTTTYKNL QHHDYNTYTF LDLNLDLSK FRLPQPSSGR ESPRH

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

+
Macromolecule #24: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 24 / Number of copies: 3 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

+
Macromolecule #25: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 25 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

+
Macromolecule #26: UBIQUINONE-1

MacromoleculeName: UBIQUINONE-1 / type: ligand / ID: 26 / Number of copies: 1 / Formula: UQ1
Molecular weightTheoretical: 250.29 Da
Chemical component information

ChemComp-UQ1:
UBIQUINONE-1

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Macromolecule #27: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 27 / Number of copies: 2 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

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

+
Macromolecule #28: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 28 / 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 #29: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 29 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

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Macromolecule #30: Ubiquinone-9

MacromoleculeName: Ubiquinone-9 / type: ligand / ID: 30 / Number of copies: 1 / Formula: UQ9
Molecular weightTheoretical: 795.226 Da
Chemical component information

ChemComp-UQ9:
Ubiquinone-9

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Macromolecule #31: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 31 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

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

+
Macromolecule #32: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 32 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #33: ~{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: 33 / Number of copies: 1 / 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

+
Macromolecule #34: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 34 / Number of copies: 1 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.33 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recording#0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 (6k x 4k) / #0 - Average electron dose: 46.1 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Average electron dose: 45.9 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

+
Image processing

Image recording ID1
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7ak5

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 147426
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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