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- EMDB-11876: Cryo-EM structure of Arabidopsis thaliana complex-I (closed confo... -

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Basic information

Entry
Database: EMDB / ID: EMD-11876
TitleCryo-EM structure of Arabidopsis thaliana complex-I (closed conformation)
Map data
Sample
  • Complex: Cryo-EM structure of Arabidopsis thaliana complex-I (closed conformation)
    • Protein or peptide: x 47 types
  • Ligand: x 14 types
Function / homology
Function and homology information


anther dehiscence / vegetative to reproductive phase transition of meristem / cold acclimation / NADH dehydrogenase complex / P450-containing electron transport chain / Lyases; Carbon-oxygen lyases; Hydro-lyases / photorespiration / embryo development ending in seed dormancy / response to abscisic acid / plant-type vacuole ...anther dehiscence / vegetative to reproductive phase transition of meristem / cold acclimation / NADH dehydrogenase complex / P450-containing electron transport chain / Lyases; Carbon-oxygen lyases; Hydro-lyases / photorespiration / embryo development ending in seed dormancy / response to abscisic acid / plant-type vacuole / respiratory chain complex I / regulation of reactive oxygen species metabolic process / cobalt ion binding / response to osmotic stress / acyl carrier activity / plastid / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / protein homotrimerization / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / respirasome / response to salt stress / respiratory electron transport chain / chloroplast / mitochondrial membrane / carbonate dehydratase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / peroxisome / fatty acid biosynthetic process / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / carbohydrate metabolic process / mitochondrial matrix / copper ion binding / nucleolus / mitochondrion / zinc ion binding / extracellular region / membrane / identical protein binding / metal ion binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Putative NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, plant/fungi / At2g27730-like / NADH-ubiquinone oxidoreductase 11kDa subunit / NADH-ubiquinone oxidoreductase 11 kDa subunit / : / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid ...Putative NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, plant/fungi / At2g27730-like / NADH-ubiquinone oxidoreductase 11kDa subunit / NADH-ubiquinone oxidoreductase 11 kDa subunit / : / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Soluble ligand binding domain / Zinc finger, CHCC-type / Zinc-finger domain / SLBB domain / Hexapeptide repeat / GRIM-19 / GRIM-19 protein / NADH dehydrogenase subunit 5, C-terminal / NADH dehydrogenase subunit 5 C-terminus / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NDUFA6, LYR domain / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NDUFB9, LYR domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Bacterial transferase hexapeptide (six repeats) / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH dehydrogenase, subunit C / NADH ubiquinone oxidoreductase, F subunit / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH-quinone oxidoreductase, chain M/4 / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / CHCH / NuoE domain / CHCH domain / NADH:ubiquinone oxidoreductase / NADH-quinone oxidoreductase subunit E-like / Trimeric LpxA-like superfamily / Thioredoxin-like [2Fe-2S] ferredoxin / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit
Similarity search - Domain/homology
(thale cress) hypothetical protein / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / NADH-ubiquinone oxidoreductase chain 4L / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 2 ...(thale cress) hypothetical protein / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / NADH-ubiquinone oxidoreductase chain 4L / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 2 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A / Acyl carrier protein 2, mitochondrial / Acyl carrier protein 1, mitochondrial / NADH-ubiquinone oxidoreductase chain 3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial / At4g16450 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A / Transmembrane protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Excitatory amino acid transporter / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / Gamma carbonic anhydrase 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / Gamma carbonic anhydrase 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / Furry / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein / Gamma carbonic anhydrase-like 2, mitochondrial / At2g46540/F11C10.23 / Uncharacterized protein At2g27730, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / Mouse-ear cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.53 Å
AuthorsKlusch N / Kuelbrandt W / Yildiz O
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Plant Cell / Year: 2021
Title: A ferredoxin bridge connects the two arms of plant mitochondrial complex I.
Authors: Niklas Klusch / Jennifer Senkler / Özkan Yildiz / Werner Kühlbrandt / Hans-Peter Braun /
Abstract: Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two ...Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric γ-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I.
History
DepositionOct 23, 2020-
Header (metadata) releaseDec 15, 2021-
Map releaseDec 15, 2021-
UpdateDec 15, 2021-
Current statusDec 15, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7ar8
  • Surface level: 0.011
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11876.png

Downloads & links

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Map

FileDownload / File: emd_11876.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 600 pix.
= 502.2 Å		0.84 Å/pix.
x 600 pix.
= 502.2 Å		0.84 Å/pix.
x 600 pix.
= 502.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.837 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.011 / Movie #1: 0.011
Minimum - Maximum-0.03772901 - 0.118650965
Average (Standard dev.)6.4309934e-05 (±0.0010541334)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 502.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.8370.8370.837
M x/y/z600600600
origin x/y/z0.0000.0000.000
length x/y/z502.200502.200502.200
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS600600600
D min/max/mean-0.0380.1190.000

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Supplemental data

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Half map: #2

Fileemd_11876_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_11876_half_map_2.map
Projections & Slices
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Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of Arabidopsis thaliana complex-I (closed confo...

EntireName: Cryo-EM structure of Arabidopsis thaliana complex-I (closed conformation)
Components
  • Complex: Cryo-EM structure of Arabidopsis thaliana complex-I (closed conformation)
    • 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
    • Protein or peptide: NADH dehydrogenase subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: NADH dehydrogenase subunit 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: AT3G07480.1
    • 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 1, mitochondrial
    • Protein or peptide: Acyl carrier protein 2, mitochondrial
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
    • Protein or peptide: At2g46540/F11C10.23
    • Protein or peptide: Transmembrane protein
    • Protein or peptide: Excitatory amino acid transporter
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B
    • Protein or peptide: At4g16450
    • Protein or peptide: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein
    • Protein or peptide: P1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
    • Protein or peptide: B15 -- 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-B
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: Furry
    • Protein or peptide: unknown
    • Protein or peptide: Uncharacterized protein At2g27730, mitochondrial
    • Protein or peptide: Gamma carbonic anhydrase-like 2, mitochondrial
    • Protein or peptide: Gamma carbonic anhydrase 2, mitochondrial
    • Protein or peptide: Gamma carbonic anhydrase 1, mitochondrial
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: Ubiquinone-9Coenzyme Q10
  • Ligand: PHOSPHATIDYLETHANOLAMINE
  • Ligand: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
  • Ligand: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
  • Ligand: FE (III) ION
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: ZINC ION
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • Ligand: Lauryl Maltose Neopentyl Glycol
  • Ligand: 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE
  • Ligand: Phosphatidylinositol

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Supramolecule #1: Cryo-EM structure of Arabidopsis thaliana complex-I (closed confo...

SupramoleculeName: Cryo-EM structure of Arabidopsis thaliana complex-I (closed conformation)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#47
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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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: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 13.941387 KDa
SequenceString:
MMLEFAPIFI YLVISLLVSL ILLGVPFLFA SNSSTYPEKL SAYECGFDPF GDARSRFDIR FYLVSILFLI FDLEVTFFFP WAVSLNKID LFGFWSMMAF LFILTIGFLY EWKRGALDWE

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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: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 24.071949 KDa
SequenceString: MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS ...String:
MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS YSVVRGCDRI VPVDIYVPGC PPTAEALLYG LLQLQKKINR RKDFLHWWNK

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 22.91091 KDa
SequenceString:
MDNQFIFKYS WETLPKKWVK KMERSEHGNR FDTNTDYLFQ LLCFLKLHTY TRVQVLIDIC GVDYPSRKRR FEVVYNLLST RYNSRIRVQ TSADEVTRIS SVVSLFPSAG WWEREVWDMF GVSFINHPDL RRILTDYGFE GHPLRKDFPL SGYVQVRYDD P EKRVVSEP IEMTQEFRYF DFASPWEQRS DG

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Macromolecule #4: NADH dehydrogenase subunit 7

MacromoleculeName: NADH dehydrogenase subunit 7 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 45.036844 KDa
SequenceString: MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP ...String:
MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP LGLCRDIDSF TQQFASRIDE LEEMLTGNRI WKQRLVDIGT VTAQQAKDWG FSGVMLRGSG VCWDLRRAAP YD VYDQLDF DVPVGTRGDC YDRYCIRIEE MRQSLRIIVQ CLNQMPSGMI KADDRKLCPP SRCRMKLSME SLIHHFELYT EGF SVPASS TYTAVEAPKG EFGVFLVSNG SNRPYRCKIR APGFAHSQGL DFMSKHHMLA DVVTIIGTQD 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: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 28.423607 KDa
SequenceString: MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE ...String:
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE MECMGCCVNA PMITVADYSN GSEGYTYNYF EDVTPEKVVE IVEKLRKGEK PPHGTQNPKR IKCGPEGGNK TL LGEPKPP QFRDLDAC

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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: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 53.522418 KDa
SequenceString: MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA ...String:
MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA GVGMRASAAY IYIRGEYVNE RLNLEKARRE AYAAGLLGKN ACGSGYDFEV YIHFGAGAYI CGEETALLES LE GKQGKPR LKPPFPANAG LYGCPTTVTN VETVAVSPTI LRRGPEWFSS FGRKNNAGTK LFCISGHVNK PCTVEEEMSI PLK ELIERH CGGVRGGWDN LLAIIPGGSS VPLIPKNICE DVLMDFDALK AVQSGLGTAA VIVMDKSTDV VDAIARLSYF YKHE SCGQC TPCREGTGWL WMIMERMKVG NAKLEEIDML QEVTKQIEGH TICALGDAAA WPVQGLIRHF RPELERRIRE RAERE LLQA AA

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Macromolecule #7: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 81.619367 KDa
SequenceString: MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL ...String:
MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL DCPICDQGGE CDLQDQSMAF GSDRGRFTEM KRSVVDKNLG PLVKTVMTRC IQCTRCVRFA SEVAGVQDLG IL GRGSGEE IGTYVEKLMT SELSGNVIDI CPVGALTSKP FAFKARNWEL KATETIDVSD AVGSNIRVDS RGPEVMRIIP RLN EDINEE WISDKTRFCY DGLKRQRLSD PMIRDSDGRF KAVSWRDALA VVGDIIHQVK PDEIVGVAGQ LSDAESMMVL KDFV NRMGS DNVWCEGTAA GVDADLRYSY LMNTSISGLE NADLFLLIGT QPRVEAAMVN ARICKTVRAS NAKVGYVGPP AEFNY DCKH LGTGPDTLKE IAEGRHPFCT ALKNAKNPAI IVGAGLFNRT DKNAILSSVE SIAQANNVVR PDWNGLNFLL QYAAQA AAL DLGLIQQSAK ALESAKFVYL MGADDVNVDK IPKDAFVVYQ GHHGDKAVYR ANVILPASAF TEKEGTYENT EGFTQQT VP AVPTVGDARD DWKIVRALSE VSGVKLPYNS IEGVRSRIKS VAPNLVHTDE REPAAFGPSL KPECKEAMST TPFQTVVE N FYMTNSITRA SKIMAQCSAV LLKKPFV

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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: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 36.02007 KDa
SequenceString: MYIAVPAEIL GIILPLLLGV AFLVLAERKV MAFVQRRKGP DVVGSFGLLQ PLADGLKLIL KEPISPSSAN FFLFRMAPVA TFMLSLVAW AVVPFDYGMV LSDLNIGLLY LFAISSLGVY GIIIAGRSSN SKYAFLGALR SAAQMVSYEV SIGLILITVL I CVGSCNLS ...String:
MYIAVPAEIL GIILPLLLGV AFLVLAERKV MAFVQRRKGP DVVGSFGLLQ PLADGLKLIL KEPISPSSAN FFLFRMAPVA TFMLSLVAW AVVPFDYGMV LSDLNIGLLY LFAISSLGVY GIIIAGRSSN SKYAFLGALR SAAQMVSYEV SIGLILITVL I CVGSCNLS EIVMAQKQIW FGIPLFPVLV MFFISCLAET NRAPFDLPEA EAELVAGYNV EYSSMGFALF FLGEYANMIL MS GLCTLFF LGGWLPILDL PIFKKIPGSI WFSIKVLFFL FLYIWVRAAF PRYRYDQLMG LGWKVFLPLS LAWVVSVSGL LVT FQWLP

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 25.536801 KDa
SequenceString: MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC ...String:
MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC QEACPVDAIV EGPNFEFATE THEELLYDKE KLLENGDRWE TEIAENLRSE SLYR

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Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 23.690385 KDa
SequenceString: MILSVLSSLA LVSGLMVVRA KNPVHSVLFF ILVFCDTSGL LLLLGLDFFA MIFLVVYIGA IAVLFLFVVM MFHIQIAEIH EEVLRYLPV SGIIGLIFWW EMFFILDNES IPLLPTQRNT TSLRYTVYAG KVRSWTNLET LGNLLYTYYF VWFLVSSLIL L VAMIGAIV ...String:
MILSVLSSLA LVSGLMVVRA KNPVHSVLFF ILVFCDTSGL LLLLGLDFFA MIFLVVYIGA IAVLFLFVVM MFHIQIAEIH EEVLRYLPV SGIIGLIFWW EMFFILDNES IPLLPTQRNT TSLRYTVYAG KVRSWTNLET LGNLLYTYYF VWFLVSSLIL L VAMIGAIV LTMHRTTKVK RQDVFRRNAI DFRRTIMRRT TDPLTIY

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Macromolecule #11: NADH dehydrogenase subunit 4L

MacromoleculeName: NADH dehydrogenase subunit 4L / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.165549 KDa
SequenceString:
MDLIKYFTFS MIIFILGIWG ILLNRRNILI MLMSIELMLL AVNLNFLVFS VSLDDMMGQV FALLVLTVAA AESAIGLAIF VITFRVRGT IAVEFINSIQ G

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Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 74.497977 KDa
SequenceString: MYLLIVFLPL LGSSVAGFFG RFLGSEGSAI MTTTCVSFSS ILSLIAFYEV ALGASACYLR IAPWISSEMF DASWGFLFDS LTVVMLIVV TFISSLVHLY SISYMSEDPH SPRFMCYLSI FTFFMLMLVT GDNFLQLFLG WEGVGLASYL LIHFWFTRLQ A DKAAIKAM ...String:
MYLLIVFLPL LGSSVAGFFG RFLGSEGSAI MTTTCVSFSS ILSLIAFYEV ALGASACYLR IAPWISSEMF DASWGFLFDS LTVVMLIVV TFISSLVHLY SISYMSEDPH SPRFMCYLSI FTFFMLMLVT GDNFLQLFLG WEGVGLASYL LIHFWFTRLQ A DKAAIKAM LVNRVGDFGL ALGILGCFTL FQTVDFSTIF ACASVPRNSW IFCNMRLNAI SLICILLFIG AVGKSAQIGL HT WLPDAME GPTPVSALIH AATMVTAGVF MIARCSPLFE YSPTALIVIT FAGAMTSFLA ATTGILQNDL KRVIAYSTCS QLG YMIFAC GISNYSVSVF HLMNHAFFKA LLFLSAGSVI HAMSDEQDMR KMGGLASSFP LTYAMMLIGS LSLIGFPFLT GFYS KDVIL ELAYTKYTIS GNFAFWLGSV SVLFTSYYSF RLLFLTFLVP TNSFGRDISR CHDAPIPMAI PLILLALGSL FVGYL AKDM MIGLGTNFWA NSLLVLPKNE ILAESEFAAP TIIKLIPILF STLGAFVAYN VNLVADQFQR AFQTSTFCNR LYSFFN KRW FFDQVLNDFL VRSFLRFGYE VSFEALDKGA IEILGPYGIS YTFRRLAERI SQLQSGFVYH YAFAMLLGLT LFVTFFC MW DSLSSWVDNR LSFILIVSSF YTKSSQE

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 55.995664 KDa
SequenceString: MLEHFCECYF NLSGLILCPV LGSIILLFIP NSRIRLIRLI GLCASLITFL YSLVLWIQFD SSTAKFQFVE SLRWLPYENI NFYLGIDGI SLFFVILTTF LIPICILVGW SGMRSYGKEY IIAFLICEFL MIAVFCMLDL LLFYVFFESV LIPMFIIIGV W GSRQRKIK ...String:
MLEHFCECYF NLSGLILCPV LGSIILLFIP NSRIRLIRLI GLCASLITFL YSLVLWIQFD SSTAKFQFVE SLRWLPYENI NFYLGIDGI SLFFVILTTF LIPICILVGW SGMRSYGKEY IIAFLICEFL MIAVFCMLDL LLFYVFFESV LIPMFIIIGV W GSRQRKIK AAYQFFLYTL LGSLFMLLAI LLILFQTGTT DLQILLTTEF SERRQIFLWI AFFASFAVKV PMVPVHIWLP EA HVEAPTA GSVILAGILL KFGTYGFLRF SIPMFPEATL CFTPFIYTLS AIAIIYTSLT TLRQIDLKKI IAYSSVAHMN LVT IGMFSL NIQGIGGSIL LMLSHGLVSS ALFLCVGVLY DRHKTRLVRY YGGLVSTMPN FSTIFFFFTL ANMSLPGTSS FIGE FLILV GAFQRNSLVA TLAALGMILG AAYSLWLYNR VVSGNLKPDF LHKFSDLNGR EVFIFIPFLV GLVWMGVYPK VFLDC MHTS VSNLVQHGKF H

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Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 55.486836 KDa
SequenceString: MKAEFVRILP HMFNLFLAVF PEIFIINATF ILLIHGVVFS TSKKYDYPPL ASNVGWLGLL SVLITLLLLA AGAPLLTIAH LFWNNLFRR DNFTYFCQIF LLLSTAGTIS MCFDFFDQER FDAFEFIVLI LLSTCGMLFM ISAYDLIAMY LAIELQSLCF Y VIAASKRK ...String:
MKAEFVRILP HMFNLFLAVF PEIFIINATF ILLIHGVVFS TSKKYDYPPL ASNVGWLGLL SVLITLLLLA AGAPLLTIAH LFWNNLFRR DNFTYFCQIF LLLSTAGTIS MCFDFFDQER FDAFEFIVLI LLSTCGMLFM ISAYDLIAMY LAIELQSLCF Y VIAASKRK SEFSTEAGLK YLILGAFSSG ILLFGCSMIY GSTGATHFDQ LAKILTGYEI TGARSSGIFM GILFIAVGFL FK ITAVPFH MWAPDIYEGS PTPVTAFLSI APKISIFANI LRVFIYGSYG ATLQQIFFFC SIASMILGAL AAMAQTKVKR LLA YSSIGH VGYICIGFSC GTIEGIQSLL IGIFIYALMT MDAFAIVLAL RQTRVKYIAD LGALAKTNPI LAITFSITMF SYAG IPPLA GFCSKFYLFF AALGCGAYFL ALVGVVTSVI GCFYYIRLVK RMFFDTPRTW ILYEPMDRNK SLLLAMTSFF ITLFL LYPS PLFSVTHQMA LSLYL

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Macromolecule #15: AT3G07480.1

MacromoleculeName: AT3G07480.1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 17.626197 KDa
SequenceString:
MATTLQKLSS QIHRLSPFTR SLIVRTSATS APSPSLGSKK VSDRIVKLSA IDPDGYKQDI IGLSGQTLLR ALTHTGLIDP ASHRLDDIE ACSAECEVQI AEEWLEKLPP RTYDEEYVLK RSSRSRILNK HSRLGCQVVL TQELQGMVVA VPEAKPWDIP

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 43.988652 KDa
SequenceString: MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA ...String:
MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA LVAKEHGGIM RYIQVSCLGA SVSSPSRMLR AKAAAEEAVL NALPEATIMR PATMIGTEDR ILNPWSMFVK KY GFLPLIG GGTTKFQPVY VVDVAAAIVA ALKDDGSSMG KTYELGGPDV FTTHELAEIM YDMIREWPRY VKLPFPIAKA MAA PRDFMV NKVPFPLPSP QIFNLDQINA LTTDTLVSDN ALKFQDLDLV PHKLKGYPVE FLIQYRKGGP NFGSTVSEKI PTDF YP

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 17.160445 KDa
SequenceString:
MALCATTQRT IRIAATLRRV ARPFATDAVV ESDYKRGEIG KVSGIPEEHL SRKVIIYSPA RTATQSGSGK LGKWKINFVS TLKWENPLM GWTSTGDPYA NVGDSALAFD SEEAAKSFAE RHGWDYKVKK PNTPLLKVKS YSDNFKWKGN PQPEN

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 12.251122 KDa
SequenceString:
MASNLLKALI RSQILPSSRR NFSVATTQLG IPTDDLVGNH TAKWMQDRSK KSPMELISEV PPIKVDGRIV ACEGDTNPAL GHPIEFICL DLNEPAICKY CGLRYVQDHH H

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 10.865765 KDa
SequenceString:
MAWRGSISKS MKELRILLCQ SSPASAPTRT FVEKNYKDLK SLNPKLPILI RECSGVQPQM WARYDMGVER CVNLDGLTEP QILKALENL VKSGATKA

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Macromolecule #20: Acyl carrier protein 1, mitochondrial

MacromoleculeName: Acyl carrier protein 1, mitochondrial / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 13.735628 KDa
SequenceString:
MALRNAILRH LRVPVQTLGL NQSKIGFLGT IRSFSSHDDH LSREAVVDRV LDVVKSFPKV DPSKVTPEVH FQNDLGLDSL DTVEIVMAI EEEFKLEIPD KEADKIDSCS LAIEYVYNHP MSS

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Macromolecule #21: Acyl carrier protein 2, mitochondrial

MacromoleculeName: Acyl carrier protein 2, mitochondrial / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 14.183111 KDa
SequenceString:
MAARGAMLRY LRVNVNPTIQ NPRECVLPFS ILLRRFSEEV RGSFLDKSEV TDRVLSVVKN FQKVDPSKVT PKANFQNDLG LDSLDSVEV VMALEEEFGF EIPDNEADKI QSIDLAVDFI ASHPQAK

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Macromolecule #22: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun...

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 19.201906 KDa
SequenceString:
MFLRAIGRPL LAKVKQTTGI VGLDVVPNAR AVLIDLYSKT LKEIQAVPED EGYRKAVESF TRQRLNVCKE EEDWEMIEKR LGCGQVEEL IEEARDELTL IGKMIEWDPW GVPDDYECEV IENDAPIPKH VPQHRPGPLP EQFYKTLEGL IAESKTEIPA A TPSDPQLK E

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Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 15.102261 KDa
SequenceString:
MAAPFALRKI GVPPNSANLT EARRRVFDFF RAACRSIPTI MDIYNLQDVV APSQLRYAIS AQIRNNAHIT DPKVIDLLIF KGMEELTDI VDHAKQRHHI IGQYVVGEGL VQNTGNKDQG KTDFLKNFYT SNYF

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Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.985954 KDa
SequenceString:
MSSAVDATGN PIPTSAVLTA SAKHIGMRCM PENVAFLKCK KNDPNPEKCL DKGRDVTRCV LGLLKDLHQK CQKEMDDYVG CMYYYTNEF DLCRKEQEAF EKVCPLK

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 16.145584 KDa
SequenceString:
MTEAMIRNKP GMASVKDMPL LQDGPPPGGF APVRYARRIS NTGPSAMAMF LAVSGAFAWG MYQVGQGNKI RRALKEEKYA ARRTILPIL QAEEDERFVS EWKKYLEYEA DVMKDVPGWK VGENVYNSGR WMPPATGELR PDVW

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 7.349628 KDa
SequenceString:
MSLVWLEAML PLGIIGGMLC IMGNSQYYIH KAYHGRPKHI GHDEWDVAME RRDKKVVEKA AAPSS

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Macromolecule #27: At2g46540/F11C10.23

MacromoleculeName: At2g46540/F11C10.23 / type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 6.810177 KDa
SequenceString:
MPVMEKLRMF VAQEPVVAAS CLIGGVGLFL PAVVRPILDS LEASKQVKAP PLTDVIAGVT GKKQS

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Macromolecule #28: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 9.876422 KDa
SequenceString:
MGGGDHGHGA EGGDFRAKVW SMTGGPNCRP KHWRRNTAIA MFGVFLVCIP IAKLSAKLEQ RPHMPVRPIP SQIWCKNFGT KDDYEKEH

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Macromolecule #29: Excitatory amino acid transporter

MacromoleculeName: Excitatory amino acid transporter / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 9.220749 KDa
SequenceString:
MPISATMVGA LLGLGTQMYS NALRKLPYMR HPWEHVVGMG LGAVFANQLV KWDVKLKEDL DVMLAKARAA NERRYFDEDR D

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B
type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 9.914133 KDa
SequenceString:
MASGWGITGN KGRCYDFWMD FSECMSHCRE PKDCTLLRED YLECLHHSKE FQRRNRIYKE EQRKLRAASR KGEETGDGTH THH

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Macromolecule #31: At4g16450

MacromoleculeName: At4g16450 / type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.355008 KDa
SequenceString:
MNTDITALEK AQYPVVDRNP AFTKVVGNFS TLDYLRFSTI TGISVTVGYL SGIKPGIKGP SMVTGGLIGL MGGFMYAYQN SAGRLMGFF PNDGEVASYQ KRGGFSK

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Macromolecule #32: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein

MacromoleculeName: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 12.648286 KDa
SequenceString:
MPSTQSLTVA AKTLRNRIFS RSGSTSAGPS RWATPGHEER PKGYFMNRTP PAPGQSRKWE DWELPCYITS FLTIVILGVG LNAKPDLSI ETWAHQKALE RLEMEKLATA GDSSD

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Macromolecule #33: P1

MacromoleculeName: P1 / type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.808244 KDa
SequenceString:
MGFIMEFAEN LVLRLMENPE ERDRKAREHI YEMHERCKKI KEMWALPIRP YGFWTFERHN AQLRWDPQIS QVAGRRDPYD DLLEDNYTP PSSSSSSSD

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Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 7.58259 KDa
SequenceString:
MGGGGHGGGI TYKGVTVHTP KTWHTVTGKG LCAVMWFWIL YRAKQDGPVV MGWRHPWDGH GDHGHGDHH

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Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A
type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 8.064313 KDa
SequenceString:
MAKPLGTTGE FFRRRDEWRK HPMLSNQMRH ALPGIGIGVG AFCVYLVGEQ IYSKLMAPSS QSSHQKQPAP SH

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Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 13.225222 KDa
SequenceString:
MAGRLSGVAS RIMGGNGVVA RSVGSSLRQR AGMGLPVGKH IVPDKPLSVN DELMWDNGTA FPEPCIDRIA DTVGKYEALA WLSGGLGFF VGLGLLAVLN DKASKVPFTP RVYPYDNLRV ELGGEP

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Macromolecule #37: B15 -- 1 beta subcomplex subunit 4

MacromoleculeName: B15 -- 1 beta subcomplex subunit 4 / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 8.305539 KDa
SequenceString:
MGGGMETNKN KFIEDWGSAR ENLEHNFRWT RRNFALIGIF GIALPIIVYK GIVKDFHMQD EDAGRPHRKF L

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Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 13.638335 KDa
SequenceString:
MSGVSTAAYF ARRAAQKERV RILYRRALKD TLNWAVHRHI FYRDASDLRE KFNVNQDVED VDRIDKLIAH GEAEYNKWRH PDPYIVPWA PGGSKFCRNP TPPAGIEIVY NYGLEDNP

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Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.757832 KDa
SequenceString:
MEVPGSSKKM IATQEEMSAA KIALGSRDMC AHLLIPLNKC RQAEFYLPWK CEDERHVYEK CEYELVMERM LAMKKIREEE ALAKQNKLQ GNAAVPLIPK TANA

+
Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B
type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 12.462276 KDa
SequenceString:
MGRKKGLPEF EESAPDGFDP ENPYKDPVAM VEMREHIVRE KWIQIEKAKI LREKVKWCYR VEGVNHYQKC RHLVQQYLDS TRGVGWGKD HRPISLHGPK PEAVEAE

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Macromolecule #41: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 18.346736 KDa
SequenceString:
MALTVAKSAL EAIREKGLGG FMRMIREEGF MRCLPDGNLL QTKIHNIGAT LVGVDKFGNK YYQKLGDTQY GRHRWVEYAS KDRYNASQV PAEWHGWLHF ITDHTGDELL SLKPKRYGLE HKENFSGEGD AYIYHSKGHT LNPGQKNWTR YQSWVPTKTQ

+
Macromolecule #42: Furry

MacromoleculeName: Furry / type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 15.060062 KDa
SequenceString:
MAKSVSTAAS SLVQNLRRYI KKPWQITGPC AHPEYLEAVP KATEYRLRCP ATIDEEAIVP SSDPETVYNI VYHGRDQRRN RPPIRRYVL TKDNVVQMMN EKKSFDVSDF PKVYLTTTVE EDLDTRGGGY EK

+
Macromolecule #43: unknown

MacromoleculeName: unknown / type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 2.571161 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)

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Macromolecule #44: Uncharacterized protein At2g27730, mitochondrial

MacromoleculeName: Uncharacterized protein At2g27730, mitochondrial / type: protein_or_peptide / ID: 44 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 11.96552 KDa
SequenceString:
MATRNALRIV SRRFSSGKVL SEEERAAENV FIKKMEQEKL QKLARQGPGE QAAGSASEAK VAGATASASA ESGPKVSEDK NRNYAVVAG VVAIVGSIGW YLKAGGKKQP EVQE

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Macromolecule #45: Gamma carbonic anhydrase-like 2, mitochondrial

MacromoleculeName: Gamma carbonic anhydrase-like 2, mitochondrial / type: protein_or_peptide / ID: 45 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 27.985113 KDa
SequenceString: MATSLARISK RSITSAVSSN LIRRYFAAEA VAVATTETPK PKSQVTPSPD RVKWDYRGQR QIIPLGQWLP KVAVDAYVAP NVVLAGQVT VWDGSSVWNG AVLRGDLNKI TVGFCSNVQE RCVVHAAWSS PTGLPAQTLI DRYVTVGAYS LLRSCTIEPE C IIGQHSIL ...String:
MATSLARISK RSITSAVSSN LIRRYFAAEA VAVATTETPK PKSQVTPSPD RVKWDYRGQR QIIPLGQWLP KVAVDAYVAP NVVLAGQVT VWDGSSVWNG AVLRGDLNKI TVGFCSNVQE RCVVHAAWSS PTGLPAQTLI DRYVTVGAYS LLRSCTIEPE C IIGQHSIL MEGSLVETRS ILEAGSVLPP GRRIPSGELW GGNPARFIRT LTNEETLEIP KLAVAINHLS GDYFSEFLPY ST IYLEVEK FKKSLGIAI

+
Macromolecule #46: Gamma carbonic anhydrase 2, mitochondrial

MacromoleculeName: Gamma carbonic anhydrase 2, mitochondrial / type: protein_or_peptide / ID: 46 / Number of copies: 1 / Enantiomer: LEVO / EC number: Lyases; Carbon-oxygen lyases; Hydro-lyases
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 30.102207 KDa
SequenceString: MGTLGRAIYT VGNWIRGTGQ ALDRVGSLLQ GSHRIEEHLS RHRTLMNVFD KSPLVDKDVF VAPSASVIGD VQIGKGSSIW YGCVLRGDV NNISVGSGTN IQDNTLVHVA KTNISGKVLP TLIGDNVTVG HSAVIHGCTV EDDAFVGMGA TLLDGVVVEK H AMVAAGSL ...String:
MGTLGRAIYT VGNWIRGTGQ ALDRVGSLLQ GSHRIEEHLS RHRTLMNVFD KSPLVDKDVF VAPSASVIGD VQIGKGSSIW YGCVLRGDV NNISVGSGTN IQDNTLVHVA KTNISGKVLP TLIGDNVTVG HSAVIHGCTV EDDAFVGMGA TLLDGVVVEK H AMVAAGSL VKQNTRIPSG EVWGGNPAKF MRKLTDEEIV YISQSAKNYI NLAQIHASEN SKSFEQIEVE RALRKKYARK DE DYDSMLG ITRETPPELI LPDNVLPGGK PVAKVPSTQY F

+
Macromolecule #47: Gamma carbonic anhydrase 1, mitochondrial

MacromoleculeName: Gamma carbonic anhydrase 1, mitochondrial / type: protein_or_peptide / ID: 47 / Number of copies: 1 / Enantiomer: LEVO / EC number: Lyases; Carbon-oxygen lyases; Hydro-lyases
Source (natural)Organism: Mouse-ear cress (thale cress)
Molecular weightTheoretical: 30.010039 KDa
SequenceString: MGTLGRAFYS VGFWIRETGQ ALDRLGCRLQ GKNYFREQLS RHRTLMNVFD KAPIVDKEAF VAPSASVIGD VHIGRGSSIW YGCVLRGDV NTVSVGSGTN IQDNSLVHVA KSNLSGKVHP TIIGDNVTIG HSAVLHGCTV EDETFIGMGA TLLDGVVVEK H GMVAAGAL ...String:
MGTLGRAFYS VGFWIRETGQ ALDRLGCRLQ GKNYFREQLS RHRTLMNVFD KAPIVDKEAF VAPSASVIGD VHIGRGSSIW YGCVLRGDV NTVSVGSGTN IQDNSLVHVA KSNLSGKVHP TIIGDNVTIG HSAVLHGCTV EDETFIGMGA TLLDGVVVEK H GMVAAGAL VRQNTRIPSG EVWGGNPARF LRKLTDEEIA FISQSATNYS NLAQAHAAEN AKPLNVIEFE KVLRKKHALK DE EYDSMLG IVRETPPELN LPNNILPDKE TKRPSNVN

+
Macromolecule #48: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 48 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

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

+
Macromolecule #49: FE2/S2 (INORGANIC) CLUSTER

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

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

+
Macromolecule #50: FLAVIN MONONUCLEOTIDE

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

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

+
Macromolecule #51: Ubiquinone-9

MacromoleculeName: Ubiquinone-9 / type: ligand / ID: 51 / Number of copies: 1 / Formula: UQ9
Molecular weightTheoretical: 795.226 Da
Chemical component information

ChemComp-UQ9:
Ubiquinone-9

+
Macromolecule #52: PHOSPHATIDYLETHANOLAMINE

MacromoleculeName: PHOSPHATIDYLETHANOLAMINE / type: ligand / ID: 52 / Number of copies: 3 / Formula: PTY
Molecular weightTheoretical: 734.039 Da
Chemical component information

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

+
Macromolecule #53: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5...

MacromoleculeName: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
type: ligand / ID: 53 / Number of copies: 2 / Formula: PC7
Molecular weightTheoretical: 763.1 Da
Chemical component information

ChemComp-PC7:
(7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE / phospholipid*YM / Phosphatidylcholine

+
Macromolecule #54: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
type: ligand / ID: 54 / Number of copies: 1 / Formula: PGT
Molecular weightTheoretical: 751.023 Da
Chemical component information

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

+
Macromolecule #55: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 55 / Number of copies: 1 / Formula: FE
Molecular weightTheoretical: 55.845 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 / Nicotinamide adenine dinucleotide phosphate

+
Macromolecule #57: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 57 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #58: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 58 / Number of copies: 2 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

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Macromolecule #59: Lauryl Maltose Neopentyl Glycol

MacromoleculeName: Lauryl Maltose Neopentyl Glycol / type: ligand / ID: 59 / Number of copies: 1 / Formula: LMN
Molecular weightTheoretical: 1.005188 KDa
Chemical component information

ChemComp-AV0:
Lauryl Maltose Neopentyl Glycol

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Macromolecule #60: 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE

MacromoleculeName: 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE / type: ligand / ID: 60 / Number of copies: 1 / Formula: PSF
Molecular weightTheoretical: 455.437 Da
Chemical component information

ChemComp-PSF:
1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE / Phosphatidylserine

+
Macromolecule #61: Phosphatidylinositol

MacromoleculeName: Phosphatidylinositol / type: ligand / ID: 61 / Number of copies: 1 / Formula: T7X
Molecular weightTheoretical: 887.128 Da
Chemical component information

ChemComp-T7X:
Phosphatidylinositol / Phosphatidylinositol

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Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.53 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 42096
FSC plot (resolution estimation)

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