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- EMDB-14134: Bovine complex I in lipid nanodisc, Deactive-ligand (composite) -

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Basic information

Entry
Database: EMDB / ID: EMD-14134
TitleBovine complex I in lipid nanodisc, Deactive-ligand (composite)
Map dataComposite of 3 globally sharpened focus-refined maps generated using Phenix Combine Focused Maps
Sample
  • Complex: Mitochondrial complex I in the deactive state with a ligand bound
    • Protein or peptide: x 44 types
  • Ligand: x 17 types
Function / homology
Function and homology information


Complex I biogenesis / Mitochondrial protein import / RHOG GTPase cycle / ubiquinone biosynthetic process / Respiratory electron transport / cellular response to oxygen levels / mitochondrial large ribosomal subunit binding / gliogenesis / Neutrophil degranulation / neural precursor cell proliferation ...Complex I biogenesis / Mitochondrial protein import / RHOG GTPase cycle / ubiquinone biosynthetic process / Respiratory electron transport / cellular response to oxygen levels / mitochondrial large ribosomal subunit binding / gliogenesis / Neutrophil degranulation / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / NADH dehydrogenase activity / Mitochondrial protein degradation / ubiquinone binding / acyl binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial ATP synthesis coupled electron transport / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / response to cAMP / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / neurogenesis / reactive oxygen species metabolic process / aerobic respiration / fatty acid binding / respiratory electron transport chain / electron transport chain / circadian rhythm / brain development / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / fatty acid biosynthetic process / FMN binding / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / mitochondrial inner membrane / mitochondrial matrix / negative regulation of DNA-templated transcription / apoptotic process / protein-containing complex binding / mitochondrion / nucleoplasm / metal ion binding / cytoplasm
Similarity search - Function
Complex1_LYR-like / 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 flavoprotein 3 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / Tim17/Tim22/Tim23/Pmp24 family ...Complex1_LYR-like / 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 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] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / 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 NDUFB4 / NADH-ubiquinone oxidoreductase subunit b14.5b (NDUFC2) / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / : / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / 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: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-ubiquinone oxidoreductase MWFE subunit / : / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / 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 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase subunit 5, C-terminal / NADH dehydrogenase subunit 5 C-terminus / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / GRIM-19 / GRIM-19 protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NDUFB9, LYR domain / Deoxynucleoside kinase domain / Deoxynucleoside kinase / 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 / : / SLBB domain / : / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / : / NADH-quinone oxidoreductase subunit 3, ferredoxin-like domain / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-ubiquinone oxidoreductase chain 4L/K / NADH-quinone oxidoreductase, chain M/4 / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NAD(P)H-quinone oxidoreductase subunit D/H / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / NADH ubiquinone oxidoreductase, F subunit / NADH-quinone oxidoreductase, subunit D
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 (domestic cattle) / cattle (cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.3 Å
AuthorsChung I / Bridges HR / Hirst J
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_UU_00015/2 United Kingdom
CitationJournal: Nat Commun / Year: 2022
Title: Cryo-EM structures define ubiquinone-10 binding to mitochondrial complex I and conformational transitions accompanying Q-site occupancy.
Authors: Injae Chung / John J Wright / Hannah R Bridges / Bozhidar S Ivanov / Olivier Biner / Caroline S Pereira / Guilherme M Arantes / Judy Hirst /
Abstract: Mitochondrial complex I is a central metabolic enzyme that uses the reducing potential of NADH to reduce ubiquinone-10 (Q) and drive four protons across the inner mitochondrial membrane, powering ...Mitochondrial complex I is a central metabolic enzyme that uses the reducing potential of NADH to reduce ubiquinone-10 (Q) and drive four protons across the inner mitochondrial membrane, powering oxidative phosphorylation. Although many complex I structures are now available, the mechanisms of Q reduction and energy transduction remain controversial. Here, we reconstitute mammalian complex I into phospholipid nanodiscs with exogenous Q. Using cryo-EM, we reveal a Q molecule occupying the full length of the Q-binding site in the 'active' (ready-to-go) resting state together with a matching substrate-free structure, and apply molecular dynamics simulations to propose how the charge states of key residues influence the Q binding pose. By comparing ligand-bound and ligand-free forms of the 'deactive' resting state (that require reactivating to catalyse), we begin to define how substrate binding restructures the deactive Q-binding site, providing insights into its physiological and mechanistic relevance.
History
DepositionJan 13, 2022-
Header (metadata) releaseMay 25, 2022-
Map releaseMay 25, 2022-
UpdateSep 28, 2022-
Current statusSep 28, 2022Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_14134.png

Downloads & links

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Map

FileDownload / File: emd_14134.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite of 3 globally sharpened focus-refined maps generated using Phenix Combine Focused Maps
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.75 Å/pix.
x 640 pix.
= 479.744 Å		0.75 Å/pix.
x 640 pix.
= 479.744 Å		0.75 Å/pix.
x 640 pix.
= 479.744 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.7496 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 5.5
Minimum - Maximum-19.322933 - 47.074524
Average (Standard dev.)0.008298433 (±1.0859311)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions640640640
Spacing640640640
CellA=B=C: 479.744 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Mitochondrial complex I in the deactive state with a ligand bound

EntireName: Mitochondrial complex I in the deactive state with a ligand bound
Components
  • Complex: Mitochondrial complex I in the deactive state with a ligand bound
    • 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-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: POTASSIUM ION
  • Ligand: GLYCEROL
  • Ligand: DODECYL-BETA-D-MALTOSIDE
  • Ligand: CARDIOLIPIN
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • 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: CHOLIC ACID
  • Ligand: MYRISTIC ACID
  • Ligand: water

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Supramolecule #1: Mitochondrial complex I in the deactive state with a ligand bound

SupramoleculeName: Mitochondrial complex I in the deactive state with a ligand bound
type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#44
Source (natural)Organism: Bos taurus (domestic cattle) / Tissue: Heart / Organelle: Mitochondria
Molecular weightExperimental: 1 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: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 13.086531 KDa
SequenceString:
(FME)NLMLALLTN FTLATLLVII AFWLPQLNVY SEKTSPYECG FDPMGSARLP FSMKFFLVAI TFLLFDLEIA LLLPLP WAS QTANLNTMLT MALFLIILLA VSLAYEWTQK GLEWTE

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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: cattle (cattle) / Tissue: HEART
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

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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: cattle (cattle) / Tissue: HEART
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

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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: cattle (cattle) / Tissue: HEART
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

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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: cattle (cattle) / Tissue: HEART
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

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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: cattle (cattle) / Tissue: HEART
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

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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: cattle (cattle) / Tissue: HEART
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

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Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 8 / Details: Uniprot accession code: P03887 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: P42028 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 10 / Details: Uniprot accession code: P03924 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / type: protein_or_peptide / ID: 11 / Details: Uniprot accession code: P03902 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 10.828195 KDa
SequenceString:
(FME)SMVYMNIMM AFTVSLVGLL MYRSHLMSSL LCLEGMMLSL FVMAALTILN SHFTLASMMP IILLVFAACE AALGLS LLV MVSNTYGTDY VQNLNLLQC

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Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 12 / Details: Uniprot accession code: P03920 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13 / Details: Uniprot accession code: P03910 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 14 / Details: Uniprot accession code: P03892 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: P34942 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: P34943 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: Q02375 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: P23934 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 13.433194 KDa
SequenceString:
MAAVLTFLRF LGRGGAVTRG LPGGARCFGV RTSPTGEKVT HTGQVYDDGD YRKVRFVGRQ KEVNENFAID LIAEQPVSQV GSRVISCDG GGGALGHPRV YINLDKETKT GTCGYCGLQF RQQHH

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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 / Details: Uniprot accession code: Q02370 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 11.097824 KDa
SequenceString:
MAAAAAIRGV RGKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD VQPKLWARYA FGQEKNVSLN NFSADQVTR ALENVLSSKA

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Macromolecule #20: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 20 / Details: Uniprot accession code: P52505 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 17.42134 KDa
SequenceString:
MAVRVLCACV RRLPTAFAPL PRLPTLAAAR PLSTTLFAAE TRTRPGAPLP ALVLAQVPGR VTQLCRQYSD APPLTLEGIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

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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 / Details: Uniprot accession code: P23935 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 13.334608 KDa
SequenceString:
MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGHIPK NAAYRKYTEQ ITNEKLSMVK AEPDVKKLEE RLQGGQIEEV ILQAENELS LARKMIQWKP WEPLVEEPPA SQWKWPI

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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 / Details: Uniprot accession code: Q02366 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 15.083544 KDa
SequenceString:
MAASGLRQAA VAASTSVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHLF QLDISVKQGR DKVREMFKKN AHITDPRVVD LLVIKGKME LEETIKVWKQ RTHVMRFFHE TEAPRPKDFL SKFYVGHDP

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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 / Details: Uniprot accession code: P42029 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: Q8HXG6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 14.814058 KDa
SequenceString:
M(AYA)KTVLRQYW DIPEGTECHR KTYATTSIGG AAGLVVSAYS VALKTPTSFL EGVARTGRYT FTAAAIGAIF GLTSCI SAQ VREKPDDPLN YLIGGCAGGL ILGARTRSYG IGAAACAYMG LTAALVKMGQ LEGWQVFAEP KV

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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 / Details: Uniprot accession code: Q95KV7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 16.694395 KDa
SequenceString:
MAASKVKQDM PPVGGYGPID YKRNLPRRGL SGYSMFAVGI GALLFGYWSM MKWNRERRRL QIEDFEARIA LMPLLQAEKD RRVLQMLRE NLEEEATVMK DVPGWKVGES VFHTTRWVTP MMGELYGLRA SEEVLSATYG FIWYT

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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 / Details: Uniprot accession code: Q02377 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 8.117445 KDa
SequenceString:
MWFEVLPGIA VMGVCLFIPG MATARIHRFS NGGKEKRVAH YPYQWYLMER DRRVSGVNRS YVSKGLENID

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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 / Details: Uniprot accession code: Q02371 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 9.35785 KDa
SequenceString:
MAERVAAFLK NVWAKEPVLV ASFAIAGLAV ILPTLSPYTK YSLMINRATP YNYPVPLRDD GNMPDVPSHP QDPQGPSLEW LKRL

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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 / Details: Uniprot accession code: Q02376 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 8.796211 KDa
SequenceString:
MAPSALLRPF WKLLAPARFP SVSSSRSKFY IQEPPHGSPN WLKVGLTLGT SVFLWIYLIK QHNEDVLEYK RRNGLE

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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 / Details: Uniprot accession code: Q02827 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 14.159332 KDa
SequenceString:
(AME)MTGRQGRAT FQFLPDEARS LPPPKLTDPR LAFVGFLGYC SGLIDNAIRR RPVLLAGLHR QLLYITSFVF VGYYLL KRQ DYMYAVRDHD MFSYIKSHPE DFPEKDKKTY GEVFEEFHPV R

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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 / Details: Uniprot accession code: Q02379 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 12.694671 KDa
SequenceString:
MPFFDVQKRL GVDLDRWMTI QSAEQPHKIP SRCHAFEKEW IECAHGIGSI RAEKECKIEF EDFRECLLRQ KTMKRLHAIR RQREKLIKE GKYTPPPHHS GQEEPRS

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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 / Details: Uniprot accession code: Q02378 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 6.978148 KDa
SequenceString:
MNLLQVVRDH WVHVLVPMGF VFGYYLDRKN DEKLTAFRNK SLLYKRELKP NEEVTWK

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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 / Details: Uniprot accession code: Q8HXG5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 17.594945 KDa
SequenceString:
MAARMLGLCG RRLLAVAATR GLPAARVRWE SSSSRAVIAP STLAGKRPSE PTLRWQEDPE PEDENLYEKN PDSHGYDKDP AVDIWNMRV VFFFGFSIVL VLGSTFVAYL PDYRMQEWAR REAERLVKYR EAHGLPIMES NCFDPSKIQL PEDED

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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 / Details: Uniprot accession code: Q02380 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: Q02367 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 15.460927 KDa
SequenceString:
(SAC)GYTPEEKLR LQQLRELRRR WLKDQELSPR EPVLPPQRVS PVERFWNKFL QDGALWKNVI YKTYRHSIFA FTHVLI PVW IIHYYLKYHV TTKPYTIVEK KPRIFPGDTI LETGEVIPPM KEFPDQHH

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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 / Details: Uniprot accession code: Q02374 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 12.298858 KDa
SequenceString:
MAGMSALKRL APFAHVGGHL FRGRCARAAG ARGVRRAGGG AHIEPRYRQF PQLTRSQVIQ AEFFSATMWF WILWRFWHDS DAVLGHFPY PDPSQWTDEE LGIPPDDED

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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 / Details: Uniprot accession code: Q02365 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 11.160705 KDa
SequenceString:
MAHGHGHEHG PSKMELPDYK QWKIEGTPLE TVQEKLAARG LRDPWGRNEA WRYMGGFANN VSFVGALLKG FKWGFAAFVV AIGAEYYLE SQKKDKKHH

+
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 / Details: Uniprot accession code: Q02372 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: P48305 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 15.20626 KDa
SequenceString:
MSFPKYEASR LSSLPTTLDP AEYDISSETR KAQAERLAIR SRLKREYQLQ YYDPSRRGVI EDPALVRWTY ARSANIYPNF RPNTKTSLL GALFGIGPLV FWYYVFKTDR DRKEKLIQEG KLDRTFNISY

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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 / Details: Uniprot accession code: Q02369 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

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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 / Details: Uniprot accession code: Q02368 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 16.428846 KDa
SequenceString:
MGAHLARRYL GDASVEPDPL RMPTFPPDYG FPERKEREMV ATQQEMNDAQ LVLQQRDYCA HYLIRFLKCK RDSFPNFLAC KHERHDWDY CEHLDYVKRM KEFERERRLL QRKKRREQRE ADMAKGLGPG EVAPEVAL

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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 / Details: Uniprot accession code: Q02373 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
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

+
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 / Details: Uniprot accession code: O97725 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 17.115508 KDa
SequenceString:
MELLQVLKRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG KNTFWDVDGS MVPPEWHRW LHCMTDDPPT VKPPTARKFI WTNHKFNLSG TPQQYVPYST TRKKIQEWVP PSTPYK

+
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 / Details: Uniprot accession code: Q05752 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 12.73762 KDa
SequenceString:
M(AYA)SATRFIQW LRNWASGRDL QAKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR REAMPPSIVM SSQKVL VAG KPAESSAVAA SEKKAVSPAP PIKRWELSQD EPYL

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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 / Details: Uniprot accession code: P25712 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: cattle (cattle) / Tissue: HEART
Molecular weightTheoretical: 11.874492 KDa
SequenceString:
MAASLLLRQG RAGALKTVLL EAGVFRGVAP AVSLSAESGK NEKGLPPNPK KQSPPKKPVS AAPTEPFDNT TYKNLQHHDY STYTFLDLN LDLSKFRMPQ PSSGRESPRH

+
Macromolecule #45: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 45 / Number of copies: 29 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

+
Macromolecule #46: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 46 / Number of copies: 7 / 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 #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: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 48 / 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 #49: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 49 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

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Macromolecule #50: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 50 / Number of copies: 1 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #51: GLYCEROL

MacromoleculeName: GLYCEROL / type: ligand / ID: 51 / Number of copies: 1 / Formula: GOL
Molecular weightTheoretical: 92.094 Da
Chemical component information

ChemComp-GOL:
GLYCEROL

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Macromolecule #52: DODECYL-BETA-D-MALTOSIDE

MacromoleculeName: DODECYL-BETA-D-MALTOSIDE / type: ligand / ID: 52 / Number of copies: 1 / Formula: LMT
Molecular weightTheoretical: 510.615 Da
Chemical component information

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

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Macromolecule #53: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 53 / Number of copies: 6 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #54: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 54 / Number of copies: 1 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

+
Macromolecule #55: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 55 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #56: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 56 / 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 #57: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 57 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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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Macromolecule #61: water

MacromoleculeName: water / type: ligand / ID: 61 / Number of copies: 2774 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration4.78 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
10.0 mMMOPS3-(N-morpholino)propanesulfonic acid
50.0 mMKClpotassium chloride
GridModel: UltrAuFoil R0.6/1 / Material: GOLD / Pretreatment - Type: GLOW DISCHARGE
Details: Following glow discharge for 90 s at 20 mA, the grid was treated for 48 hours in an anaerobic glovebox in ethanol containing 5 mM 11-mercaptoundecyl hexaethyleneglycol, washed three times in ...Details: Following glow discharge for 90 s at 20 mA, the grid was treated for 48 hours in an anaerobic glovebox in ethanol containing 5 mM 11-mercaptoundecyl hexaethyleneglycol, washed three times in ethanol and dried prior to blotting
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 10 seconds before plunging.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 6780 / Average exposure time: 2.4 sec. / Average electron dose: 40.5 e/Å2
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: 2.4 µm / Nominal defocus min: 1.0 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

+
Image processing

Particle selectionNumber selected: 1078933
CTF correctionSoftware - Name: RELION (ver. 3.1.0)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1.0)
Details: Composite of 3 globally sharpened focus-refined maps generated using Phenix Combine Focused Maps. Resolution refers to the consensus map resolution.
Number images used: 235957
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 3.1.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.1.0)

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