[English] 日本語
Yorodumi
- EMDB-16172: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-16172
TitleCryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)
Map data
Sample
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)
    • Protein or peptide: x 57 types
  • Ligand: x 12 types
Function / homology
Function and homology information


plastid outer membrane / TIM22 mitochondrial import inner membrane insertion complex / anther dehiscence / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / mitochondrial processing peptidase / plant-type cell wall / cold acclimation / respiratory chain complex III / NADH dehydrogenase complex ...plastid outer membrane / TIM22 mitochondrial import inner membrane insertion complex / anther dehiscence / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / mitochondrial processing peptidase / plant-type cell wall / cold acclimation / respiratory chain complex III / NADH dehydrogenase complex / P450-containing electron transport chain / Lyases; Carbon-oxygen lyases; Hydro-lyases / protein insertion into mitochondrial inner membrane / photorespiration / embryo development ending in seed dormancy / response to abscisic acid / plant-type vacuole / mitochondrial respiratory chain complex III / vacuole / respiratory chain complex I / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / regulation of reactive oxygen species metabolic process / cobalt ion binding / response to osmotic stress / plastid / mitochondrial electron transport, ubiquinol to cytochrome c / acyl carrier activity / porin activity / NADH:ubiquinone reductase (H+-translocating) / pore complex / mitochondrial respiratory chain complex I / protein homotrimerization / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / respirasome / monoatomic ion transport / response to salt stress / respiratory electron transport chain / chloroplast / mitochondrial membrane / carbonate dehydratase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / peroxisome / fatty acid biosynthetic process / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / mitochondrial outer membrane / electron transfer activity / oxidoreductase activity / carbohydrate metabolic process / mitochondrial matrix / copper ion binding / heme binding / nucleolus / protein homodimerization activity / mitochondrion / proteolysis / zinc ion binding / extracellular region / ATP binding / membrane / identical protein binding / metal ion binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Mitochondrial import inner membrane translocase subunit TIM22 / Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / 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 ...Mitochondrial import inner membrane translocase subunit TIM22 / Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / 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 / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome b / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Tim17/Tim22/Tim23/Pmp24 family / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / Soluble ligand binding domain / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / SLBB domain / Rieske iron-sulphur protein, C-terminal / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Zinc finger, CHCC-type / Zinc-finger domain / Hexapeptide repeat / Rieske iron-sulphur protein / GRIM-19 / GRIM-19 protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / 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) / Metalloenzyme, LuxS/M16 peptidase-like / 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 / Bacterial transferase hexapeptide (six repeats) / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ
Similarity search - Domain/homology
(thale cress) hypothetical protein / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 6 / Cytochrome b / NADH-ubiquinone oxidoreductase chain 4L / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / Cytochrome b-c1 complex subunit 7-2, mitochondrial ...(thale cress) hypothetical protein / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 6 / Cytochrome b / NADH-ubiquinone oxidoreductase chain 4L / (thale cress) hypothetical protein / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / Cytochrome b-c1 complex subunit 7-2, mitochondrial / NADH-ubiquinone oxidoreductase chain 2 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / Outer envelope pore protein 16-3, chloroplastic/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 2 / Cytochrome b-c1 complex subunit 6-1, mitochondrial / Probable mitochondrial-processing peptidase subunit beta, mitochondrial / 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 / Uncharacterized protein At1g67785 / Transmembrane protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / Excitatory amino acid transporter / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B / Cytochrome b-c1 complex subunit Rieske-1, mitochondrial / Cytochrome b-c1 complex subunit 10, mitochondrial / 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 / Cytochrome c1 2, heme protein, 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 / Cytochrome b-c1 complex subunit 9, mitochondrial / 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 / Cytochrome b-c1 complex subunit 8-1, mitochondrial / 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 / Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial / Uncharacterized protein At2g27730, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / thale cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsKlusch N / Kuehlbrandt W
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Nat Plants / Year: 2023
Title: Cryo-EM structure of the respiratory I + III supercomplex from Arabidopsis thaliana at 2 Å resolution.
Authors: Niklas Klusch / Maximilian Dreimann / Jennifer Senkler / Nils Rugen / Werner Kühlbrandt / Hans-Peter Braun /
Abstract: Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis ...Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III with a co-purified ubiquinone in the Q site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.
History
DepositionNov 18, 2022-
Header (metadata) releaseMay 10, 2023-
Map releaseMay 10, 2023-
UpdateMay 10, 2023-
Current statusMay 10, 2023Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

emd_16172.png

Downloads & links

-
Map

FileDownload / File: emd_16172.map.gz / Format: CCP4 / Size: 1.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.57 Å/pix.
x 750 pix.
= 429.75 Å		0.57 Å/pix.
x 750 pix.
= 429.75 Å		0.57 Å/pix.
x 750 pix.
= 429.75 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.573 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.013
Minimum - Maximum-0.037389472 - 0.08770524
Average (Standard dev.)0.00016931392 (±0.0018781789)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions750750750
Spacing750750750
CellA=B=C: 429.75 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

+
Entire : Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete ...

EntireName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)
Components
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)
    • 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 [ubiquinone] iron-sulfur protein 2
    • 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: Outer envelope pore protein 16-3, chloroplastic/mitochondrial
    • 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: Uncharacterized protein At1g67785
    • 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
    • Protein or peptide: Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
    • Protein or peptide: Probable mitochondrial-processing peptidase subunit beta, mitochondrial
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
    • Protein or peptide: Cytochrome c1 2, heme protein, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7-2, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 8-1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 6-1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 9, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 10, mitochondrial
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: Ubiquinone-9Coenzyme Q10
  • 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: CROTONYL COENZYME A
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
  • Ligand: UBIQUINONE-7Coenzyme Q10

+
Supramolecule #1: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete ...

SupramoleculeName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)
type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#57
Source (natural)Organism: Arabidopsis thaliana (thale cress)

+
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: thale cress (thale cress)
Molecular weightTheoretical: 13.969396 KDa
SequenceString:
(FME)MLEFAPIFI YLVISLLVSL ILLGVPFLFA SNSSTYPEKL SAYECGFDPF GDARSRFDIR FYLVSILFLI FDLEVT FFF PWAVSLNKID LFGFWSMMAF LFILTIGFLY EWKRGALDWE

+
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: thale 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

+
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: thale 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

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 45.062922 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 APGFAHLQGL DFMSKHHMLA DVVTIIGTQD IVFGEVDR

+
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: thale 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

+
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: thale 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

+
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: thale 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

+
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: thale 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

+
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: thale 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

+
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: thale 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

+
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: thale cress (thale cress)
Molecular weightTheoretical: 11.193559 KDa
SequenceString:
(FME)DLIKYFTFS MIIFILGIWG ILLNRRNILI MLMSIELMLL AVNLNFLVFS VSLDDMMGQV FALLVLTVAA AESAIG LAI FVITFRVRGT IAVEFINSIQ G

+
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: thale 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

+
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: thale 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

+
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: thale 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

+
Macromolecule #15: AT3G07480.1

MacromoleculeName: AT3G07480.1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale 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

+
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: thale 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

+
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: thale 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

+
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: thale cress (thale cress)
Molecular weightTheoretical: 12.251122 KDa
SequenceString:
MASNLLKALI RSQILPSSRR NFSVATTQLG IPTDDLVGNH TAKWMQDRSK KSPMELISEV PPIKVDGRIV ACEGDTNPAL GHPIEFICL DLNEPAICKY CGLRYVQDHH H

+
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: thale cress (thale cress)
Molecular weightTheoretical: 10.865765 KDa
SequenceString:
MAWRGSISKS MKELRILLCQ SSPASAPTRT FVEKNYKDLK SLNPKLPILI RECSGVQPQM WARYDMGVER CVNLDGLTEP QILKALENL VKSGATKA

+
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: thale cress (thale cress)
Molecular weightTheoretical: 13.735628 KDa
SequenceString:
MALRNAILRH LRVPVQTLGL NQSKIGFLGT IRSFSSHDDH LSREAVVDRV LDVVKSFPKV DPSKVTPEVH FQNDLGLDSL DTVEIVMAI EEEFKLEIPD KEADKIDSCS LAIEYVYNHP MSS

+
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: thale cress (thale cress)
Molecular weightTheoretical: 14.183111 KDa
SequenceString:
MAARGAMLRY LRVNVNPTIQ NPRECVLPFS ILLRRFSEEV RGSFLDKSEV TDRVLSVVKN FQKVDPSKVT PKANFQNDLG LDSLDSVEV VMALEEEFGF EIPDNEADKI QSIDLAVDFI ASHPQAK

+
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: thale 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

+
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: thale cress (thale cress)
Molecular weightTheoretical: 15.102261 KDa
SequenceString:
MAAPFALRKI GVPPNSANLT EARRRVFDFF RAACRSIPTI MDIYNLQDVV APSQLRYAIS AQIRNNAHIT DPKVIDLLIF KGMEELTDI VDHAKQRHHI IGQYVVGEGL VQNTGNKDQG KTDFLKNFYT SNYF

+
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: thale cress (thale cress)
Molecular weightTheoretical: 11.985954 KDa
SequenceString:
MSSAVDATGN PIPTSAVLTA SAKHIGMRCM PENVAFLKCK KNDPNPEKCL DKGRDVTRCV LGLLKDLHQK CQKEMDDYVG CMYYYTNEF DLCRKEQEAF EKVCPLK

+
Macromolecule #25: Outer envelope pore protein 16-3, chloroplastic/mitochondrial

MacromoleculeName: Outer envelope pore protein 16-3, chloroplastic/mitochondrial
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 17.017348 KDa
SequenceString:
MDPAEMRYLE EEDGPLMKTI KGSITGFGAG TIYGTILATW KDVPRVERNV ALPGLIRTLK MMGTHGLTFA AIGGVYIGVE QLVQNFRSK RDFYNGAIGG FVAGASVLGY RARSIPTAIA AGATLAVTSA LIDSGGQTTR VDNGREYYPY TVEKRAEADS

+
Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 16.145584 KDa
SequenceString:
MTEAMIRNKP GMASVKDMPL LQDGPPPGGF APVRYARRIS NTGPSAMAMF LAVSGAFAWG MYQVGQGNKI RRALKEEKYA ARRTILPIL QAEEDERFVS EWKKYLEYEA DVMKDVPGWK VGENVYNSGR WMPPATGELR PDVW

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 7.349628 KDa
SequenceString:
MSLVWLEAML PLGIIGGMLC IMGNSQYYIH KAYHGRPKHI GHDEWDVAME RRDKKVVEKA AAPSS

+
Macromolecule #28: At2g46540/F11C10.23

MacromoleculeName: At2g46540/F11C10.23 / type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 6.810177 KDa
SequenceString:
MPVMEKLRMF VAQEPVVAAS CLIGGVGLFL PAVVRPILDS LEASKQVKAP PLTDVIAGVT GKKQS

+
Macromolecule #29: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 9.876422 KDa
SequenceString:
MGGGDHGHGA EGGDFRAKVW SMTGGPNCRP KHWRRNTAIA MFGVFLVCIP IAKLSAKLEQ RPHMPVRPIP SQIWCKNFGT KDDYEKEH

+
Macromolecule #30: Excitatory amino acid transporter

MacromoleculeName: Excitatory amino acid transporter / type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 9.220749 KDa
SequenceString:
MPISATMVGA LLGLGTQMYS NALRKLPYMR HPWEHVVGMG LGAVFANQLV KWDVKLKEDL DVMLAKARAA NERRYFDEDR D

+
Macromolecule #31: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 9.914133 KDa
SequenceString:
MASGWGITGN KGRCYDFWMD FSECMSHCRE PKDCTLLRED YLECLHHSKE FQRRNRIYKE EQRKLRAASR KGEETGDGTH THH

+
Macromolecule #32: At4g16450

MacromoleculeName: At4g16450 / type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 11.383019 KDa
SequenceString:
(FME)NTDITALEK AQYPVVDRNP AFTKVVGNFS TLDYLRFSTI TGISVTVGYL SGIKPGIKGP SMVTGGLIGL MGGFMY AYQ NSAGRLMGFF PNDGEVASYQ KRGGFSK

+
Macromolecule #33: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein

MacromoleculeName: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein
type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 12.648286 KDa
SequenceString:
MPSTQSLTVA AKTLRNRIFS RSGSTSAGPS RWATPGHEER PKGYFMNRTP PAPGQSRKWE DWELPCYITS FLTIVILGVG LNAKPDLSI ETWAHQKALE RLEMEKLATA GDSSD

+
Macromolecule #34: P1

MacromoleculeName: P1 / type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 11.808244 KDa
SequenceString:
MGFIMEFAEN LVLRLMENPE ERDRKAREHI YEMHERCKKI KEMWALPIRP YGFWTFERHN AQLRWDPQIS QVAGRRDPYD DLLEDNYTP PSSSSSSSD

+
Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2
type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 7.58259 KDa
SequenceString:
MGGGGHGGGI TYKGVTVHTP KTWHTVTGKG LCAVMWFWIL YRAKQDGPVV MGWRHPWDGH GDHGHGDHH

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A
type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.064313 KDa
SequenceString:
MAKPLGTTGE FFRRRDEWRK HPMLSNQMRH ALPGIGIGVG AFCVYLVGEQ IYSKLMAPSS QSSHQKQPAP SH

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 13.225222 KDa
SequenceString:
MAGRLSGVAS RIMGGNGVVA RSVGSSLRQR AGMGLPVGKH IVPDKPLSVN DELMWDNGTA FPEPCIDRIA DTVGKYEALA WLSGGLGFF VGLGLLAVLN DKASKVPFTP RVYPYDNLRV ELGGEP

+
Macromolecule #38: B15 -- 1 beta subcomplex subunit 4

MacromoleculeName: B15 -- 1 beta subcomplex subunit 4 / type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.305539 KDa
SequenceString:
MGGGMETNKN KFIEDWGSAR ENLEHNFRWT RRNFALIGIF GIALPIIVYK GIVKDFHMQD EDAGRPHRKF L

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 13.638335 KDa
SequenceString:
MSGVSTAAYF ARRAAQKERV RILYRRALKD TLNWAVHRHI FYRDASDLRE KFNVNQDVED VDRIDKLIAH GEAEYNKWRH PDPYIVPWA PGGSKFCRNP TPPAGIEIVY NYGLEDNP

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 11.757832 KDa
SequenceString:
MEVPGSSKKM IATQEEMSAA KIALGSRDMC AHLLIPLNKC RQAEFYLPWK CEDERHVYEK CEYELVMERM LAMKKIREEE ALAKQNKLQ GNAAVPLIPK TANA

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10-B
type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 12.462276 KDa
SequenceString:
MGRKKGLPEF EESAPDGFDP ENPYKDPVAM VEMREHIVRE KWIQIEKAKI LREKVKWCYR VEGVNHYQKC RHLVQQYLDS TRGVGWGKD HRPISLHGPK PEAVEAE

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

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale 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 #43: Uncharacterized protein At1g67785

MacromoleculeName: Uncharacterized protein At1g67785 / type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 7.54679 KDa
SequenceString:
MVKVLTYFGM TLAAFAFWQS MDKVHVWIAL HQDEKQERME KEAEVRRVRA ELLRKAREED PLA

+
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: thale cress (thale cress)
Molecular weightTheoretical: 11.96552 KDa
SequenceString:
MATRNALRIV SRRFSSGKVL SEEERAAENV FIKKMEQEKL QKLARQGPGE QAAGSASEAK VAGATASASA ESGPKVSEDK NRNYAVVAG VVAIVGSIGW YLKAGGKKQP EVQE

+
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: thale 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: thale 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: thale 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: Probable mitochondrial-processing peptidase subunit alpha-1, mito...

MacromoleculeName: Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
type: protein_or_peptide / ID: 48 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 54.459766 KDa
SequenceString: MYRTAASRAR ALKGVLTRSL RPARYASSSA VAETSSSTPA YLSWLSGGSR AALTSLDMPL QGVSLPPPLA DKVEPSKLQI TTLPNGLKI ASETTPNPAA SIGLYVDCGS IYEAPYFHGA THLLERMAFK STLNRTHFRL VREIEAIGGN TSASASREQM S YTIDALKT ...String:
MYRTAASRAR ALKGVLTRSL RPARYASSSA VAETSSSTPA YLSWLSGGSR AALTSLDMPL QGVSLPPPLA DKVEPSKLQI TTLPNGLKI ASETTPNPAA SIGLYVDCGS IYEAPYFHGA THLLERMAFK STLNRTHFRL VREIEAIGGN TSASASREQM S YTIDALKT YVPEMVEVLI DSVRNPAFLD WEVNEELRKM KVEIAELAKN PMGFLLEAIH SAGYSGPLAS PLYAPESALD RL NGELLEE FMTENFTAAR MVLAASGVEH EELLKVAEPL TSDLPNVPPQ LAPKSQYVGG DFRQHTGGEA THFAVAFEVP GWN NEKEAV TATVLQMLMG GGGSFSAGGP GKGMHSWLYR RVLNEYQEVQ SCTAFTSIFN DTGLFGIYGC SSPQFAAKAI ELAA KELKD VAGGKVNQAH LDRAKAATKS AVLMNLESRM IAAEDIGRQI LTYGERKPVD QFLKSVDQLT LKDIADFTSK VISKP LTMG SFGDVLAVPS YDTISSKFR

+
Macromolecule #49: Probable mitochondrial-processing peptidase subunit beta, mitocho...

MacromoleculeName: Probable mitochondrial-processing peptidase subunit beta, mitochondrial
type: protein_or_peptide / ID: 49 / Number of copies: 2 / Enantiomer: LEVO / EC number: mitochondrial processing peptidase
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 59.23475 KDa
SequenceString: MAMKNLLSLA RRSQRRLFLT QATRSSSSFS AIDSVPASAS PTALSPPPPH LMPYDHAAEI IKNKIKKLEN PDKRFLKYAS PHPILASHN HILSAPETRV TTLPNGLRVA TESNLSAKTA TVGVWIDAGS RFESDETNGT AHFLEHMIFK GTDRRTVRAL E EEIEDIGG ...String:
MAMKNLLSLA RRSQRRLFLT QATRSSSSFS AIDSVPASAS PTALSPPPPH LMPYDHAAEI IKNKIKKLEN PDKRFLKYAS PHPILASHN HILSAPETRV TTLPNGLRVA TESNLSAKTA TVGVWIDAGS RFESDETNGT AHFLEHMIFK GTDRRTVRAL E EEIEDIGG HLNAYTSREQ TTYYAKVLDS NVNQALDVLA DILQNSKFEE QRINRERDVI LREMQEVEGQ TDEVVLDHLH AT AFQYTPL GRTILGPAQN VKSITREDLQ NYIKTHYTAS RMVIAAAGAV KHEEVVEQVK KLFTKLSSDP TTTSQLVANE PAS FTGSEV RMIDDDLPLA QFAVAFEGAS WTDPDSVALM VMQTMLGSWN KNVGGGKHVG SDLTQRVAIN EIAESIMAFN TNYK DTGLF GVYAVAKADC LDDLSYAIMY EVTKLAYRVS DADVTRARNQ LKSSLLLHMD GTSPIAEDIG RQLLTYGRRI PTAEL FARI DAVDASTVKR VANKYIYDKD IAISAIGPIQ DLPDYNKFRR RTYWNRY

+
Macromolecule #50: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 50 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 44.310609 KDa
SequenceString: MTIRNQRFSL LKQPISSTLN QHLVDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY TPHVDLAFNS VEHIMRDVEG GWLLRYMHA NGASMFFIVV YLHIFRGLYY ASYSSPREFV WCLGVVIFLL MIVTAFIGYV LPWGQMSFWG ATVITSLASA I PVVGDTIV ...String:
MTIRNQRFSL LKQPISSTLN QHLVDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY TPHVDLAFNS VEHIMRDVEG GWLLRYMHA NGASMFFIVV YLHIFRGLYY ASYSSPREFV WCLGVVIFLL MIVTAFIGYV LPWGQMSFWG ATVITSLASA I PVVGDTIV TWLWGGFSVD NATLNRFFSL HYLLPFILVG ASLLHLAALH QYGSNNPLGV HSEMDKIAFY PYFYVKDLVG WV AFAIFFS IWIFYAPNVL GHPDNYIPAN PMSTPPHIVP EWYFLPIYAI LRSIPDKAGG VAAIALVFIC LLALPFFKSM YVR SSSFRP IYQGMFWLLL ADCLLLGWIG CQPVEAPFVT IGQISSLVFF LFFAITPILG RVGRGIPNSY TDETDHT

+
Macromolecule #51: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
type: protein_or_peptide / ID: 51 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 29.645584 KDa
SequenceString: MLRVAGRRLF SVSQRSSTAT SFVVSRDHTL SDGGGDSSSA PRSLPSADLS SYHRSLIRGF SSQVLAQGNE IGFGSEVPAT VEAVKTPNS KIVYDDHNHE RYPPGDPSKR AFAYFVLSGG RFVYASVLRL LVLKLIVSMS ASKDVLALAS LEVDLGSIEP G TTVTVKWR ...String:
MLRVAGRRLF SVSQRSSTAT SFVVSRDHTL SDGGGDSSSA PRSLPSADLS SYHRSLIRGF SSQVLAQGNE IGFGSEVPAT VEAVKTPNS KIVYDDHNHE RYPPGDPSKR AFAYFVLSGG RFVYASVLRL LVLKLIVSMS ASKDVLALAS LEVDLGSIEP G TTVTVKWR GKPVFIRRRT EDDIKLANSV DVGSLRDPQE DSVRVKNPEW LVVVGVCTHL GCIPLPNAGD YGGWFCPCHG SH YDISGRI RKGPAPYNLE VPTYSFLEEN KLLIG

+
Macromolecule #52: Cytochrome c1 2, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1 2, heme protein, mitochondrial / type: protein_or_peptide / ID: 52 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 33.728238 KDa
SequenceString: MVGGGVIRQL LRRKLHSQSV ATPVLSWLSS KKANEDAGSA GLRAFALMGA GITGLLSFST VASADEAEHG LECPNYPWPH EGILSSYDH ASIRRGHQVY QQVCASCHSM SLISYRDLVG VAYTEEEAKA MAAEIEVVDG PNDEGEMFTR PGKLSDRLPE P YSNESAAR ...String:
MVGGGVIRQL LRRKLHSQSV ATPVLSWLSS KKANEDAGSA GLRAFALMGA GITGLLSFST VASADEAEHG LECPNYPWPH EGILSSYDH ASIRRGHQVY QQVCASCHSM SLISYRDLVG VAYTEEEAKA MAAEIEVVDG PNDEGEMFTR PGKLSDRLPE P YSNESAAR FANGGAYPPD LSLVTKARHN GQNYVFALLT GYRDPPAGIS IREGLHYNPY FPGGAIAMPK MLNDEAVEYE DG TPATEAQ MGKDVVSFLS WAAEPEMEER KLMGFKWIFL LSLALLQAAY YRRLKWSVLK SRKLVLDVVN

+
Macromolecule #53: Cytochrome b-c1 complex subunit 7-2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 7-2, mitochondrial / type: protein_or_peptide / ID: 53 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 14.620021 KDa
SequenceString:
MASFLQRLVD PRKNFLARMH MKSVSNRLRR YGLRYDDLYD PLYDLDIKEA LNRLPREIVD ARNQRLMRAM DLSMKHEYLP DNLQAVQTP FRSYLQDMLA LVKRERAERE ALGALPLYQR TIP

+
Macromolecule #54: Cytochrome b-c1 complex subunit 8-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 8-1, mitochondrial / type: protein_or_peptide / ID: 54 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.517977 KDa
SequenceString:
MGKQPVKLKA VVYALSPFQQ KIMTGLWKDL PEKIHHKVSE NWISATLLVT PVVGTYWYAQ YFKEQEKLEH RF

+
Macromolecule #55: Cytochrome b-c1 complex subunit 6-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6-1, mitochondrial / type: protein_or_peptide / ID: 55 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 7.997315 KDa
SequenceString:
MADDEVVDPK KYLEESCKPK CVKPLLEYQA CVKRIQGDDS GHKHCTGQYF DYWQCIDKCV APKLFAKLK

+
Macromolecule #56: Cytochrome b-c1 complex subunit 9, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 9, mitochondrial / type: protein_or_peptide / ID: 56 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.461634 KDa
SequenceString:
MEYAARRNQK GAFEGFYKLI MRRNSVYVTF IIAGAFFGER AVDYGVHKLW ERNNVGKRYE DISVLGQRPV EE

+
Macromolecule #57: Cytochrome b-c1 complex subunit 10, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 10, mitochondrial / type: protein_or_peptide / ID: 57 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 5.980947 KDa
SequenceString:
MAGTSGLLNA VKPKIQTIDI QAAAGWGIAA AAGAIWVVQP FGWIKKTFID PPPTEEK

+
Macromolecule #58: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 58 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

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

+
Macromolecule #59: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 59 / Number of copies: 4 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

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

+
Macromolecule #60: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 60 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

+
Macromolecule #61: Ubiquinone-9

MacromoleculeName: Ubiquinone-9 / type: ligand / ID: 61 / Number of copies: 1 / Formula: UQ9
Molecular weightTheoretical: 795.226 Da
Chemical component information

ChemComp-UQ9:
Ubiquinone-9

+
Macromolecule #62: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 62 / Number of copies: 1 / Formula: FE
Molecular weightTheoretical: 55.845 Da

+
Macromolecule #63: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 63 / 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 #64: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 64 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #65: 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: 65 / 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

+
Macromolecule #66: CROTONYL COENZYME A

MacromoleculeName: CROTONYL COENZYME A / type: ligand / ID: 66 / Number of copies: 1 / Formula: COO
Molecular weightTheoretical: 835.608 Da
Chemical component information

ChemComp-COO:
CROTONYL COENZYME A

+
Macromolecule #67: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 67 / Number of copies: 6 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

+
Macromolecule #68: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14...

MacromoleculeName: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
type: ligand / ID: 68 / Number of copies: 3 / Formula: UQ5
Molecular weightTheoretical: 522.758 Da
Chemical component information

ChemComp-UQ5:
2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE

+
Macromolecule #69: UBIQUINONE-7

MacromoleculeName: UBIQUINONE-7 / type: ligand / ID: 69 / Number of copies: 1 / Formula: UQ7
Molecular weightTheoretical: 658.992 Da
Chemical component information

ChemComp-UQ7:
UBIQUINONE-7

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.18 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - #0 - Film type ID: 1 / Support film - #0 - Material: CARBON / Support film - #0 - topology: CONTINUOUS / Support film - #1 - Film type ID: 2 / Support film - #1 - Material: GRAPHENE / Support film - #1 - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 70 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV

-
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 / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 215000
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 1215138
Startup modelType of model: EMDB MAP
EMDB ID:

11878

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1.3)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1.3)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1.3) / Number images used: 50886
FSC plot (resolution estimation)

-
Atomic model buiding 1

RefinementSpace: REAL
Output model

PDB-8bq6:
Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more