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- EMDB-51527: NDH-PSI-LHCI supercomplex from S. oleracea: composite map -

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Basic information

Entry
Database: EMDB / ID: EMD-51527
TitleNDH-PSI-LHCI supercomplex from S. oleracea: composite map
Map dataComposite map
Sample
  • Complex: NDH-PSI-LHCI supercomplex from Spinacia oleracea
    • Protein or peptide: x 42 types
  • Ligand: x 13 types
KeywordsNDH / PSI / Supercomplex / photosynthesis / electron transport chain / lipids / proton translocation / plastoquinone / ELECTRON TRANSPORT
Function / homology
Function and homology information


glucose-6-phosphate 1-epimerase activity / NAD(P)H dehydrogenase complex (plastoquinone) / P450-containing electron transport chain / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / thylakoid / NADH dehydrogenase complex / chloroplast thylakoid lumen / photosynthesis, light harvesting / photosystem II oxygen evolving complex / photosystem I reaction center ...glucose-6-phosphate 1-epimerase activity / NAD(P)H dehydrogenase complex (plastoquinone) / P450-containing electron transport chain / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / thylakoid / NADH dehydrogenase complex / chloroplast thylakoid lumen / photosynthesis, light harvesting / photosystem II oxygen evolving complex / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosynthetic electron transport chain / photosystem I / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / photosystem II / extrinsic component of membrane / cyclosporin A binding / chlorophyll binding / photosynthesis, light reaction / chloroplast thylakoid membrane / ubiquinone binding / : / electron transport coupled proton transport / NADH dehydrogenase activity / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / photosynthesis / aerobic respiration / peptidyl-prolyl cis-trans isomerase activity / chloroplast / peptidylprolyl isomerase / phosphoprotein binding / 2 iron, 2 sulfur cluster binding / NAD binding / protein folding / 4 iron, 4 sulfur cluster binding / carbohydrate binding / molecular adaptor activity / response to oxidative stress / carbohydrate metabolic process / electron transfer activity / oxidoreductase activity / iron ion binding / calcium ion binding / magnesium ion binding / metal ion binding / membrane / plasma membrane / cytoplasm
Similarity search - Function
NAD(P)H-quinone oxidoreductase subunit U, chloroplastic / Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Photosynthetic NDH subunit of lumenal location 4-like / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / : / PsbP, C-terminal / PsbP / : / NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal ...NAD(P)H-quinone oxidoreductase subunit U, chloroplastic / Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / Photosynthetic NDH subunit of lumenal location 4-like / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / : / PsbP, C-terminal / PsbP / : / NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal / NAD(P)H-quinone oxidoreductase subunit O / NADH-dehyrogenase subunit F, TMs, (complex I) C-terminus / Cyanobacterial and plant NDH-1 subunit O / NAD(P)H-quinone oxidoreductase subunit M / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase, subunit N / NADH-quinone oxidoreductase chain 4 / Cyanobacterial and plastid NDH-1 subunit M / NADH dehydrogenase transmembrane subunit / NADH-quinone oxidoreductase cyanobacterial subunit N / NADH-plastoquinone oxidoreductase, subunit I / NAD(P)H-quinone oxidoreductase subunit 2, N-terminal / NAD(P)H-quinone oxidoreductase subunit 2 N-terminal / Mog1/PsbP, alpha/beta/alpha sandwich / Oxygen-evolving enhancer protein 3 / Oxygen evolving enhancer protein 3 / PsbQ-like domain superfamily / Photosystem I PsaH, reaction centre subunit VI / Photosystem I reaction centre subunit VI / Photosystem I reaction center subunit V / 4Fe-4S dicluster domain / Photosystem I reaction center subunit psaK, plant / Adrenodoxin / Photosystem I reaction center subunit V/PsaK, plant / Photosystem I PsaG/PsaK domain, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / Photosystem I reaction centre subunit PsaK superfamily / Photosystem I psaG and psaK proteins signature. / Photosystem I reaction center subunit V/PsaK / Photosystem I psaG / psaK / Photosystem I PsaL, reaction centre subunit XI / Photosystem I, reaction centre subunit XI / Photosystem I PsaL, reaction centre subunit XI superfamily / Photosystem I reaction centre subunit XI / Photosystem I reaction centre subunit VIII / Photosystem I reaction centre subunit VIII / Photosystem I reaction centre subunit VIII superfamily / Photosystem I PsaF, reaction centre subunit III / Photosystem I PsaF, reaction centre subunit III superfamily / Photosystem I reaction centre subunit III / Photosystem I PsaD / Photosystem I, reaction centre subunit PsaD superfamily / PsaD / Photosystem I PsaE, reaction centre subunit IV / Photosystem I PsaJ, reaction centre subunit IX superfamily / Photosystem I reaction centre subunit IV / PsaE / Chlorophyll A-B binding protein, plant and chromista / Photosystem I PsaJ, reaction centre subunit IX / Photosystem I reaction centre subunit IX / PsaJ / Chlorophyll A-B binding protein / Chlorophyll A-B binding protein / Photosystem I protein PsaC / Photosystem I PsaB / Photosystem I PsaA / Photosystem I PsaA/PsaB, conserved site / Photosystem I psaA and psaB proteins signature. / : / Photosystem I PsaA/PsaB / Photosystem I PsaA/PsaB superfamily / Photosystem I psaA/psaB protein / Electron transport accessory-like domain superfamily / Glycoside hydrolase-type carbohydrate-binding / Chaperone J-domain superfamily / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH-quinone oxidoreductase, chain M/4 / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / Galactose mutarotase-like domain superfamily / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NAD(P)H-quinone oxidoreductase subunit D/H / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH dehydrogenase, subunit C / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature.
Similarity search - Domain/homology
Photosystem I reaction center subunit IX / Photosynthetic NDH subunit of lumenal location 2, chloroplastic / Peptidyl-prolyl cis-trans isomerase / PSI-K / peptidylprolyl isomerase / Chlorophyll a-b binding protein, chloroplastic / Chlorophyll a-b binding protein, chloroplastic / Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / NAD(P)H-quinone oxidoreductase subunit N, chloroplastic / Chlorophyll a-b binding protein, chloroplastic ...Photosystem I reaction center subunit IX / Photosynthetic NDH subunit of lumenal location 2, chloroplastic / Peptidyl-prolyl cis-trans isomerase / PSI-K / peptidylprolyl isomerase / Chlorophyll a-b binding protein, chloroplastic / Chlorophyll a-b binding protein, chloroplastic / Photosynthetic NDH subunit of subcomplex B 4, chloroplastic / NAD(P)H-quinone oxidoreductase subunit N, chloroplastic / Chlorophyll a-b binding protein, chloroplastic / Photosynthetic NDH subunit of subcomplex B 3, chloroplastic / Photosynthetic NDH subunit of lumenal location 3, chloroplastic / Photosynthetic NDH subunit of subcomplex B 1, chloroplastic / NAD(P)H-quinone oxidoreductase subunit L, chloroplastic / Chlorophyll a-b binding protein, chloroplastic / Photosynthetic NDH subunit of lumenal location 1, chloroplastic / NAD(P)H-quinone oxidoreductase subunit M, chloroplastic / Photosynthetic NDH subunit of subcomplex B 5, chloroplastic / NAD(P)H-quinone oxidoreductase subunit U, chloroplastic / NAD(P)H-quinone oxidoreductase subunit O, chloroplastic / Photosynthetic NDH subunit of subcomplex B 2, chloroplastic / Photosystem I P700 chlorophyll a apoprotein A1 / Photosystem I P700 chlorophyll a apoprotein A2 / NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic / Photosystem I iron-sulfur center / Photosystem I reaction center subunit II, chloroplastic / Photosystem I reaction center subunit IV, chloroplastic / Photosystem I reaction center subunit III, chloroplastic / Photosystem I reaction center subunit V, chloroplastic / Photosystem I reaction center subunit VIII / Photosystem I reaction center subunit VI, chloroplastic / Photosystem I reaction center subunit XI, chloroplastic / NAD(P)H-quinone oxidoreductase subunit H, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic / NAD(P)H-quinone oxidoreductase subunit I, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic / NAD(P)H-quinone oxidoreductase chain 4, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic / NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic / NAD(P)H-quinone oxidoreductase subunit K, chloroplastic / NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
Similarity search - Component
Biological speciesSpinacia oleracea (spinach)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.19 Å
AuthorsIntroini B / Hahn A / Kuehlbrandt W
Funding support Germany, 1 items
OrganizationGrant numberCountry
Other private Germany
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: Cryo-EM structure of the NDH-PSI-LHCI supercomplex from Spinacia oleracea.
Authors: Bianca Introini / Alexander Hahn / Werner Kühlbrandt /
Abstract: The nicotinamide adenine dinucleotide phosphate (NADPH) dehydrogenase (NDH) complex is crucial for photosynthetic cyclic electron flow and respiration, transferring electrons from ferredoxin to ...The nicotinamide adenine dinucleotide phosphate (NADPH) dehydrogenase (NDH) complex is crucial for photosynthetic cyclic electron flow and respiration, transferring electrons from ferredoxin to plastoquinone while transporting H across the chloroplast membrane. This process boosts adenosine triphosphate production, regardless of NADPH levels. In flowering plants, NDH forms a supercomplex with photosystem I, enhancing its stability under high light. We report the cryo-electron microscopy structure of the NDH supercomplex in Spinacia oleracea at a resolution of 3.0-3.3 Å. The supercomplex consists of 41 protein subunits, 154 chlorophylls and 38 carotenoids. Subunit interactions are reinforced by 46 distinct lipids. The structure of NDH resembles that of mitochondrial complex I closely, including the quinol-binding site and an extensive internal aqueous passage for proton translocation. A well-resolved catalytic plastoquinone (PQ) occupies the PQ channel. The pronounced structural similarity to complex I sheds light on electron transfer and proton translocation within the NDH supercomplex.
History
DepositionSep 13, 2024-
Header (metadata) releaseFeb 12, 2025-
Map releaseFeb 12, 2025-
UpdateFeb 12, 2025-
Current statusFeb 12, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51527.png

Downloads & links

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Map

FileDownload / File: emd_51527.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 512 pix.
= 428.544 Å		0.84 Å/pix.
x 512 pix.
= 428.544 Å		0.84 Å/pix.
x 512 pix.
= 428.544 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: 0.3
Minimum - Maximum-0.38743252 - 3.7443235
Average (Standard dev.)0.043397125 (±0.08007511)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 428.544 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : NDH-PSI-LHCI supercomplex from Spinacia oleracea

EntireName: NDH-PSI-LHCI supercomplex from Spinacia oleracea
Components
  • Complex: NDH-PSI-LHCI supercomplex from Spinacia oleracea
    • Protein or peptide: Photosynthetic NDH subunit of lumenal location 1, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of lumenal location 2, chloroplastic
    • Protein or peptide: Photosynthetic NDH subunit of lumenal location 3, chloroplastic
    • Protein or peptide: peptidylprolyl isomerase
    • Protein or peptide: Peptidyl-prolyl cis-trans isomerase
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit O, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit U, chloroplastic
    • Protein or peptide: Photosystem I P700 chlorophyll a apoprotein A1
    • Protein or peptide: Photosystem I P700 chlorophyll a apoprotein A2
    • Protein or peptide: Photosystem I iron-sulfur center
    • Protein or peptide: Photosystem I reaction center subunit II, chloroplastic
    • Protein or peptide: Photosystem I reaction center subunit IV, chloroplastic
    • Protein or peptide: Photosystem I reaction center subunit III, chloroplastic
    • Protein or peptide: Photosystem I reaction center subunit V, chloroplastic
    • Protein or peptide: Photosystem I reaction center subunit VI, chloroplastic
    • Protein or peptide: Photosystem I reaction center subunit VIII
    • Protein or peptide: Photosystem I reaction center subunit IX
    • Protein or peptide: PSI-K
    • Protein or peptide: Photosystem I reaction center subunit XI, chloroplastic
    • Protein or peptide: Chlorophyll a-b binding protein, chloroplastic
    • Protein or peptide: Chlorophyll a-b binding protein, chloroplastic
    • Protein or peptide: Chlorophyll a-b binding protein, chloroplastic
    • Protein or peptide: Chlorophyll a-b binding protein, chloroplastic
  • Ligand: BETA-CAROTENE
  • Ligand: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
  • Ligand: 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl alpha-maltoside
  • Ligand: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
  • Ligand: 5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-HEPTAMETHYLOCTACOSA-2,6,10,14,18,22,26-HEPTAENYL]-2,3-DIMETHYLBENZO-1,4-QUINONE
  • Ligand: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: CHLOROPHYLL A
  • Ligand: DIGALACTOSYL DIACYL GLYCEROL (DGDG)
  • Ligand: CHLOROPHYLL A ISOMER
  • Ligand: PHYLLOQUINONE
  • Ligand: CHLOROPHYLL B
  • Ligand: (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL

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Supramolecule #1: NDH-PSI-LHCI supercomplex from Spinacia oleracea

SupramoleculeName: NDH-PSI-LHCI supercomplex from Spinacia oleracea / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#42
Source (natural)Organism: Spinacia oleracea (spinach)

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Macromolecule #1: Photosynthetic NDH subunit of lumenal location 1, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of lumenal location 1, chloroplastic
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 18.606793 KDa
SequenceString:
KETPERYTAF VDKADGYSYV YPSDWREFDF RAHDSAFKDR YLQLQNVRLS FIPTDKNDVH DLGPMEDVIQ TLVKNILAAP NQMTDIREI QERSVDGKNY WTFEYNLTSP NFSVTHFTTL AIANGRYYTL TVSANERRWK RYRNKLKVVA DSFKVFEI

UniProtKB: Photosynthetic NDH subunit of lumenal location 1, chloroplastic

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Macromolecule #2: Photosynthetic NDH subunit of subcomplex B 1, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 44.622605 KDa
SequenceString: NPWLDLFYDG EDEPETEYGS MFSDGKQDED PYPRDNPENP YGFLKFPQGY AVEMASLGSK VRGDVRRCCC VVSGGVYDNL LFFPAIQLI KDRYPGVQID IITSARGKQT YEMNKNVRWA TVYDLDDNFP DPAEYTDMLG LLKNRYYDMV LSTKLAGLGH A AFLFMTTA ...String:
NPWLDLFYDG EDEPETEYGS MFSDGKQDED PYPRDNPENP YGFLKFPQGY AVEMASLGSK VRGDVRRCCC VVSGGVYDNL LFFPAIQLI KDRYPGVQID IITSARGKQT YEMNKNVRWA TVYDLDDNFP DPAEYTDMLG LLKNRYYDMV LSTKLAGLGH A AFLFMTTA RDRVSYVYPN VNAAGAGLLL SETFTPDSMN LSEGGYNMYH QMIEWLGRPV KDIPQHLASP LKVSISRKLK EA VEAKYKE AGAEKGKYVV IHGIKCDSKA SMQSEGDTDS LLPIEIWAEI SQAIRGVTPI FVIPHEKLRE DVEEIVGEET SIV FITTPG QLAALINDSV GVIATNTAAI QLALAREKPS IALFCSEEKG KCFVPDAEGK KCTVIASKTG NLADIDVAVV KDTL KVF

UniProtKB: Photosynthetic NDH subunit of subcomplex B 1, chloroplastic

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Macromolecule #3: Photosynthetic NDH subunit of subcomplex B 2, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 40.259473 KDa
SequenceString: MASLLPFSLL KPTTICKASS TAAPPAALVE SLNDQFARKG INFLESTDTS TNISSPIVEL SVRNGSSLKL QLSNAHVTSY KPKVYWKDD GFEEVLYTLP LSKGGIGLVL NDVTQPVTTT KKPDPFRRSE PAAAAAAKGS LLAGAEWSVR DVDSDSFDAV Q VELSCTSG ...String:
MASLLPFSLL KPTTICKASS TAAPPAALVE SLNDQFARKG INFLESTDTS TNISSPIVEL SVRNGSSLKL QLSNAHVTSY KPKVYWKDD GFEEVLYTLP LSKGGIGLVL NDVTQPVTTT KKPDPFRRSE PAAAAAAKGS LLAGAEWSVR DVDSDSFDAV Q VELSCTSG SLEITYVVSL YPESMASAVL VKNNGNKAIG LTSAILSHIQ FKKRSGSGIQ GLQGCSYCSH PPLSSPFEIV SP AEAMKAE DPGMFSFSSE SPSKLGEWTT QEVPITILKN KLSRVYTAPP SERSKKFYRT TPSKYETVDQ GRELVFRVIR MGY DDILVS SPGSLSEKYG RDYFICTGPA SILVPVTVNP GEEWRGAQVI EHDNLT

UniProtKB: Photosynthetic NDH subunit of subcomplex B 2, chloroplastic

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Macromolecule #4: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 15.61484 KDa
SequenceString:
EEEELEPPYV GFAFVSSVLL PDGTPDMHLR SATGGQKLRD IMLDNDIDLY GPYARPLLNC AGGGTCASCM VEVIEGKELL NPRTEKEKE HLKKKPKNWR LACQITVGTP ESRGMVVIQQ LPEWKAHEWK YEKDGPIVSE

UniProtKB: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic

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Macromolecule #5: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 10.763025 KDa
SequenceString:
MAVLVEHVEG QRDLITHKSI WHLSDAAIKN VYLFYMMFTC WGCCVFGAAK DPYYDSEQYR GDGGDGTGHW VYEKQEDIEE AGRAALWRE ELIE

UniProtKB: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic

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Macromolecule #6: Photosynthetic NDH subunit of subcomplex B 5, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 17.77267 KDa
SequenceString:
GLTDIEPDLN EDPRDRWATN GVAPEDFVYG KYDEHHTFYE SSEKGSFWGA VAEEYNSMDP PTGFQGLISW LFLPAVAAGM YFNVPGDYL FIGAGLFVII FCIIEMDKPD QPHNFEPQIY NMERGARDKL IADYNTMDIW DFNEKYGDLW DFTLK

UniProtKB: Photosynthetic NDH subunit of subcomplex B 5, chloroplastic

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Macromolecule #7: Photosynthetic NDH subunit of lumenal location 2, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of lumenal location 2, chloroplastic
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 14.875953 KDa
SequenceString:
EFKWGTRSFI WERFFEPGLS PEDAVSRIKN TAEGLHSLRH MLETMSWRYV IFYIRLKQAY LKQDMKSAMI MVPEGRRDDY SNAANELVD NMAEFDYYVR TPKVYESYVS YEKTLKSIDN LLGFLA

UniProtKB: Photosynthetic NDH subunit of lumenal location 2, chloroplastic

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Macromolecule #8: Photosynthetic NDH subunit of lumenal location 3, chloroplastic

MacromoleculeName: Photosynthetic NDH subunit of lumenal location 3, chloroplastic
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 16.451979 KDa
SequenceString:
QLWLDGPLPG LRPAENKIGN EETGTRTFLK KGIYMANIGT KGSALRLRKY AFDLLAMEDL IGQDTLNYVR RYLRFKGTFM YYDFDKVIS AAPVADKPPL TNLANRLFDN FEKLQEAVKL KDVPLTRSCY DDTAVTLQEV MNRMA

UniProtKB: Photosynthetic NDH subunit of lumenal location 3, chloroplastic

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Macromolecule #9: peptidylprolyl isomerase

MacromoleculeName: peptidylprolyl isomerase / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 15.352496 KDa
SequenceString:
LRVEYYATTA EPSCELNLVR SGLGYCDLVV GSGVPAPYNT LINVHYTARF SDETVFDSSY KRGRPLTMRI GVGKVIKGLD QGIFGGDGV PPMQVGGKRK LRIPPHLGYG PEPAGCFSGD CNVPANATLL YDVTFMGVYS GNRA

UniProtKB: peptidylprolyl isomerase

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Macromolecule #10: Peptidyl-prolyl cis-trans isomerase

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 18.900408 KDa
SequenceString:
PLQSKVTNKV YFDISIGNPV GKLVGRVVIG LFGDDVPQTA ENFRALCTGE KGFGYKGSAF HRVIKDFMIQ GGDFDKGNGT GGKSIYGRT FKDENFNLTH TGPGTVSMAN AGPNTNGSQF FICTVKTPWL DNRHVVFGQV LEGMDIVKLI ESSETDRGDR P KKRVVISE CGELPA

UniProtKB: Peptidyl-prolyl cis-trans isomerase

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Macromolecule #11: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 38.985613 KDa
SequenceString: FSRLEFLKEV YETIWMLFPI LILVLGITIG VLVIVWLERE ISASIQQRIG PEYAGPLGIL QALADGTKLL FKENLLPSRG DTYLFSIGP SIAVISILLG YLIIPFGSRL VLADLSIGVF LWIAVSSIAP IGLLMSGYGS NNKYSFLGGL RAAAQSISYE I PLTLCVLS ...String:
FSRLEFLKEV YETIWMLFPI LILVLGITIG VLVIVWLERE ISASIQQRIG PEYAGPLGIL QALADGTKLL FKENLLPSRG DTYLFSIGP SIAVISILLG YLIIPFGSRL VLADLSIGVF LWIAVSSIAP IGLLMSGYGS NNKYSFLGGL RAAAQSISYE I PLTLCVLS ISLLSNSSST VDIVEAQSKY GFWGWNLWRQ PIGFIVFIIS SLAECERLPF DLPEAEEELV AGYQTEYSGI KF GLFYVAS YLNLLISSLF VTVLYLGGWN LSIPYIFISE FFEINKIDGV FGTTIGIFIT LAKTFLFLFI PITTRWTLPR LRM DQLLNL GWKFLLPISL GNLLLTTSSQ LFSL

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic

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Macromolecule #12: NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 54.026148 KDa
SequenceString: KAFHLLLFDG SLIFPECILI FGLILLLMID STSDQKDIPW LYFISSTSLV MSITALLFRW REEPMISFSG NFQTNNFNEI FQFLILLCS TLCIPLSVEY IECTEMALTE FLLFILTATL GGMFLCGAND LITIFVAPEC FSLCSYLLSG YTKKDVRSNE A TTKYLLMG ...String:
KAFHLLLFDG SLIFPECILI FGLILLLMID STSDQKDIPW LYFISSTSLV MSITALLFRW REEPMISFSG NFQTNNFNEI FQFLILLCS TLCIPLSVEY IECTEMALTE FLLFILTATL GGMFLCGAND LITIFVAPEC FSLCSYLLSG YTKKDVRSNE A TTKYLLMG GASSSILVHG FSWLYGSSGG EIELQEIVNG LINTQMYNSP GISIALIFIT VGIGFKLSPA PSHQWTPDVY EG SPTPVVA FLSVTSKVAA SASATRIFDI PFYFSSNEWH LLLEILAILS MILGNLIAIT QTSMKRMLAY SSIGQIGYVI IGI IVGDSN DGYASMITYM LFYISMNLGT FACIVLFGLR TGTDNIRDYA GLYTKDPFLA LSLALCLLSL GGLPPLAGFF GKIY LFWCG WQAGLYFLVL IGLLTSVLSI YYYLKIIKLL MTGRNQEITP HVRNYRRSPL RSKNSIEFSM IVCVIASTIP GISMN PIIT IAQD

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic

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Macromolecule #13: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 13.270651 KDa
SequenceString:
YEYDIFWAFL IISSVIPILA FLFSGILAPI SKGPEKLSSY ESGIEPMGDA WLQFRIRYYM FALVFVVFDV ETVFLYPWAM SFDILGVSV FIEALIFVLI LIVGLVYAWR KGALEW

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic

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Macromolecule #14: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 55.980191 KDa
SequenceString: SFPWLTTIVV LPIFAGSLIF LFPHRGNKVI RWYTICISMI ELLLMTYVFF YHFQPDDPLI QLVEDYKWIN FFDFHWRLGI DGLSIGPIL LTGFITTLAT LAAWPVTRNS QLFHFLMLAM YSAQIGLFSS RDLLLFFIMW ELELIPVYLL LSMWGGKKRL Y SATKFILY ...String:
SFPWLTTIVV LPIFAGSLIF LFPHRGNKVI RWYTICISMI ELLLMTYVFF YHFQPDDPLI QLVEDYKWIN FFDFHWRLGI DGLSIGPIL LTGFITTLAT LAAWPVTRNS QLFHFLMLAM YSAQIGLFSS RDLLLFFIMW ELELIPVYLL LSMWGGKKRL Y SATKFILY TAGGSIFLLM GVLGVGLYGS NEPTLNLETL VNQSYPVALE IIFYIGFFIA FAVKLPIIPL HTWLPDTHGE AH YSTCMLL AGILLKMGAY GLVRINMELL PHAHSIFSPW LMIIGTMQII YAASTSPGQR NLKKRIAYSS VSHMGFIIIG ISS ITDTGL NGAILQIISH GFIGAALFFL AGTSYDRIRL VYLDEMGGIA IPMPKIFTLF SSFSMASLAL PGMSGFIAEL IVFF GLITS QKYLLIPKLL ITFGMAIGMI LTPIYLLSMS RQMFYGYKLF NISNSSFFDS GPRELFVSTS IFLPVIGIGV YPDLV LSLS VEKVEAILSN YFYR

UniProtKB: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic

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Macromolecule #15: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 11.085047 KDa
SequenceString:
MILEHVLVLS AFLFSIGIYG LVTSRNLVRA LMCLELILNA VNLNFVTFSD FFDSRQLKGN IFSIFVIAIA AAEAAIGPAI VSSIYRNRK SIRINQSNLL N

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic

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Macromolecule #16: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 84.590094 KDa
SequenceString: MEHIYQYAWI IPFLPLPVPL LIGAGLLFFP TATKNLRRIW AFSSISLLSI VMIFSMKLAI QQINSNSIYQ YLWSWTINND FSLEFGYLM DPLTSIMSML ITTVAILVLI YSDNYMSHDQ GYLRFFAYMS FFNTSMLGLV TSSNLIQIYI FWELVGMCSY L LIGFWFTR ...String:
MEHIYQYAWI IPFLPLPVPL LIGAGLLFFP TATKNLRRIW AFSSISLLSI VMIFSMKLAI QQINSNSIYQ YLWSWTINND FSLEFGYLM DPLTSIMSML ITTVAILVLI YSDNYMSHDQ GYLRFFAYMS FFNTSMLGLV TSSNLIQIYI FWELVGMCSY L LIGFWFTR PIAANACQKA FVTNRVGDFG LLLGILGLYW ITGSFEFRDL FEIFNNLIKN NEVNSLFCIL CAFLLFAGAV AK SAQFPLH VWLPDAMEGP TPISALIHAA TMVAAGIFLV ARLLPLFVVI PYIMYVISFI GIITVLLGAT LALAQKDIKR SLA YYTMSQ LGYMMLALGM GSYRTALFHL ITHAYSKALL FLASGSLIHS MGTIVGYSPD KSQNMVLMGG LTKHVPITKT SFLI GTLSL CGIPPLACFW SKDEILNDSW VYSPIFAIIA YFTAGLTAFY MFRIYLLTFE GHLNFFCKNY SGKKSSSFYS ISLWG KKEL KTINQKISLL NLLTMNNKER ASFFSKKPYE INVKLTKLLR SFITITYFEN KNISLYPYES DNTMLFPLII LIMFTL FVG FIGIPFNQEG MDLDILTKWL TPSINLLHSN SENFVDWYEF VINAIFSISI AFFGIFIAFF FYKPIYSSLK NFDLINS FD KRGQKRILGD NIITIIYNWS ANRGYIDAFY STFLIKGIRS LSELVSFFDR RIIDGIPNGF GVTSFFVGEG IKYVGGGR I SSYLFWYLLY VSIFLFIFTF T

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic

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Macromolecule #17: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 19.193654 KDa
SequenceString:
MDLPGPIHDF LLVFLGSGLI LGALGVVLFT NPIFSAFSLG LVLVCISLFY ILANSHFVAS AQLLIYVGAI NVLIIFSVMF MSGPEYDKK FQLWTVGDGV TSLVCISLFV SLISTILNTS WYGIIWTTKS NQILEQDLIN ASQQIGIHLS TDFFLPFELI S IILLVSLI GAIAVARQ

UniProtKB: NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic

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Macromolecule #18: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 45.172309 KDa
SequenceString: TTRKDLMIVN MGPHHPSMHG VLRLIVTLDG EDVIDCEPIV GYLHRGMEKI AENRTIIQYL PYVTRWDYLA TMFTEAITVN GPEQLGNIQ VPKRASYIRV IMLELSRIAS HLLWLGPFMA DIGAQTPFFY ILRERELIYD LFEAATGMRM MHNYFRIGGV A ADLPYGWI ...String:
TTRKDLMIVN MGPHHPSMHG VLRLIVTLDG EDVIDCEPIV GYLHRGMEKI AENRTIIQYL PYVTRWDYLA TMFTEAITVN GPEQLGNIQ VPKRASYIRV IMLELSRIAS HLLWLGPFMA DIGAQTPFFY ILRERELIYD LFEAATGMRM MHNYFRIGGV A ADLPYGWI DKCLDFCDYF LIGLTEYQKL ITRNPIFLER VENVGIIGGE EAINWGLSGP MLRASGIQWD LRKVDHYECY DE FDWEVQW QKEGDSLARY LIRIGEMAES VKIIQQALEG IPGGPYENLE IRRFNRIKYP EWNDFEYRFI SKKPSPAFEL SKQ ELYVRV EAPKGELGIF LIGDQSVFPW RWKIRPPGFI NLQILPQLVK KMKLADIMTI LGSIDIIMGE VDR

UniProtKB: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic

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Macromolecule #19: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 19.004875 KDa
SequenceString:
MVTGFINYGQ QTIRAARYIG QSFMITLSHA NRLPVTIQYP YEKLITSERF RGRIHFEFDK CIACEVCVRA CPIDLPVVDW KLETDIRKK RLLNYSIDFG ICIFCGNCVE YCPTNCLSMT EEYELSTYDR HELNYNQIAL GRLPISITDD YTIRTILNSP Q TKE

UniProtKB: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic

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Macromolecule #20: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 18.687322 KDa
SequenceString:
MQGRLSAWLV KHGLVHRSLG FDYQGIETLQ IKPEDWHSIA VILYVYGYNY LRSQCAYDVA PGGLLASVYH LTRIEYGVDQ PEEVCIKVF APRRNPRIPS VFWVWKSADF QERESYDMFG ISYDNHPRLK RILMPESWIG WPLRKDYIVP NFYEIQDAY

UniProtKB: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic

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Macromolecule #21: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 22.789359 KDa
SequenceString: MNSIEFPLLD QIAQNSVIST TSNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR YGLVPRASPR QADLILTAGT VTMKMAPSL LRLYEQMPEP KYVIAMGACT ITGGMFSTDS YSTVRGVDKL IPVDVYLPGC PPKPEAVIDA ITKLRKKISR E IYEDRIKS ...String:
MNSIEFPLLD QIAQNSVIST TSNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR YGLVPRASPR QADLILTAGT VTMKMAPSL LRLYEQMPEP KYVIAMGACT ITGGMFSTDS YSTVRGVDKL IPVDVYLPGC PPKPEAVIDA ITKLRKKISR E IYEDRIKS QPKNRCFTIN HKFRVGRSIH TGNYDQALLY KYKS

UniProtKB: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic

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Macromolecule #22: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 13.194599 KDa
SequenceString:
AVTGVNNQED LIWVLLKAGV VGFCYFLIMP PIIMNWLRIR WYRRNLLEMY FQFMFVFIFF PGILVWAPFL NFRKFPRDPT MKYPWSKPE NPSEVKGGFL KYPWATIEDY

UniProtKB: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic

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Macromolecule #23: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 16.702113 KDa
SequenceString:
EMKEVLKRAT PIEAQVNVKS RNLEREYGGQ WLSSVTRHVR IYAAYIDPVT CAMDQTQMDK LTLMIDPTDE FLWNDETLNK VYVYFEELV DHYEGAPLTE YTLRLIGSDI EHYIRKMLYE GEIKYNMNSR VLNFSMGKPR MK

UniProtKB: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

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Macromolecule #24: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 18.727768 KDa
SequenceString:
IGIRDFIGGD LVKFDLGTWL SDVEEHKAIA MYSPHEGGYE GRYLNRLRYQ GYHFLDVSAR GLGDPETTLT KVHPVCPPHV GKQPIARWW FPPEVDYRLE ALPSDAKGLV VWVIEAKVLS KAELQFLAML PSLRPKVRVI AECGNWRKVM WKPLKEIAGL V PLQEA

UniProtKB: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic

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Macromolecule #25: NAD(P)H-quinone oxidoreductase subunit O, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit O, chloroplastic
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 11.127798 KDa
SequenceString:
PPPKKPPKPV YSMKKGQIVR VEREKYLDSV NYLSVGHPKY YKGLDYIYED RGEVLDLRFF ETGEYALVSW VGIPTSPAWL PTDMLIKSD KLNYER

UniProtKB: NAD(P)H-quinone oxidoreductase subunit O, chloroplastic

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Macromolecule #26: NAD(P)H-quinone oxidoreductase subunit U, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit U, chloroplastic
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 27.127314 KDa
SequenceString: MAVSSTCMPH RELMPTLVKS TNTSTLFWLN NNTNNNVNVN VITTNNYVTL TRKAPCSRFL ARSTEDASEM TATSTDQSWE GEGENSPME MPKGPPSIIS ALNVEKALRG IGITDVDHYA RLGLRRGCTY DQVGAAYEIQ VKELSSQGMD EEQFNKERDL L KESYNILS ...String:
MAVSSTCMPH RELMPTLVKS TNTSTLFWLN NNTNNNVNVN VITTNNYVTL TRKAPCSRFL ARSTEDASEM TATSTDQSWE GEGENSPME MPKGPPSIIS ALNVEKALRG IGITDVDHYA RLGLRRGCTY DQVGAAYEIQ VKELSSQGMD EEQFNKERDL L KESYNILS SEQERRLYDW SLARNSAPER YMWPFEADIT QTPRWGTPPP QEPEDVGPTT AVGYFLLAWF VFSFILSIAL NR

UniProtKB: NAD(P)H-quinone oxidoreductase subunit U, chloroplastic

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Macromolecule #27: Photosystem I P700 chlorophyll a apoprotein A1

MacromoleculeName: Photosystem I P700 chlorophyll a apoprotein A1 / type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO / EC number: photosystem I
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 82.144953 KDa
SequenceString: EVKILVDRDP VKTSFEAWAK PGHFSRTIAK GPETTTWIWN LHADAHDFDS HTSDLEEISR KIFSAHFGQL SIIFLWLSGM YFHGARFSN YEAWLSDPTH IGPSAQVVWP IVGQEILNGD VGGGFRGIQI TSGFFQIWRA SGITSELQLY CTAIGALVFA A LMLFAGWF ...String:
EVKILVDRDP VKTSFEAWAK PGHFSRTIAK GPETTTWIWN LHADAHDFDS HTSDLEEISR KIFSAHFGQL SIIFLWLSGM YFHGARFSN YEAWLSDPTH IGPSAQVVWP IVGQEILNGD VGGGFRGIQI TSGFFQIWRA SGITSELQLY CTAIGALVFA A LMLFAGWF HYHKAAPKLA WFQDVESMLN HHLAGLLGLG SLSWAGHQIH VSLPINQFLN AGVDPKEIPL PHELILNRDL LA QLYPSFA EGATPFFTLN WSKYADFLTF RGGLDPVTGG LWLTDTAHHH LAIAILFLIA GHMYRTNWGI GHGLKDILEA HKG PFTGQG HKGLYEILTT SWHAQLALNL AMLGSLTIVV AHHMYAMPPY PYLATDYGTQ LSLFTHHMWI GGFLIVGAAA HAAI FMVRD YDPTTRYNDL LDRVLRHRDA IISHLNWACI FLGFHSFGLY IHNDTMSALG RPQDMFSDTA IQLQPVFAQW IQNTH ALAP SATAPGATAS TSLTWGGSDL VAVGGKVALL PIPLGTADFL VHHIHAFTIH VTVLILLKGV LFARSSRLIP DKANLG FRF PCDGPGRGGT CQVSAWDHVF LGLFWMYNSI SVVIFHFSWK MQSDVWGSIS DQGVVTHITG GNFAQSSITI NGWLRDF LW AQASQVIQSY GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSIV QGRAVGVT H YLLGGIATTW AFFLARIIAV G

UniProtKB: Photosystem I P700 chlorophyll a apoprotein A1

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Macromolecule #28: Photosystem I P700 chlorophyll a apoprotein A2

MacromoleculeName: Photosystem I P700 chlorophyll a apoprotein A2 / type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO / EC number: photosystem I
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 82.377547 KDa
SequenceString: ALRFPRFSQG LAQDPTTRRI WFGIATAHDF ESHDDITEER LYQNIFASHF GQLAIIFLWT SGNLFHVAWQ GNFESWVQDP LHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSVISL LGGWLHLQPK W KPSVSWFK ...String:
ALRFPRFSQG LAQDPTTRRI WFGIATAHDF ESHDDITEER LYQNIFASHF GQLAIIFLWT SGNLFHVAWQ GNFESWVQDP LHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSVISL LGGWLHLQPK W KPSVSWFK NAESRLNHHL SGLFGVSSLA WTGHLVHVAI PGSRGEYVRW NNFLDVLPHP QGLGPLFTGQ WNLYAQNPDS SS HLFGTSQ GAGTAILTLL GGFHPQTQSL WLTDMAHHHL AIAFVFLVAG HMYRTNFGIG HSMKDLLEAH IPPGGRLGRG HKG LYDTIN NSLHFQLGLA LASLGVITSL VAQHMYSLPA YAFIAQDFTT QAALYTHHQY IAGFIMTGAF AHGAIFFIRD YNPE QNEDN VLARMLDHKE AIISHLSWAS LFLGFHTLGL YVHNDVMLAF GTPEKQILIE PIFAQWIQSA HGKTSYGFDV LLSST SGPA FNAGRSIWLP GWLNAVNENS NSLFLTIGPG DFLVHHAIAL GLHTTTLILV KGALDARGSK LMPDKKDFGY SFPCDG PGR GGTCDISAWD AFYLAVFWML NTIGWVTFYW HWKHITLWQG NVSQFNESST YLMGWLRDYL WLNSSQLING YNPFGMN SL SVWAWMFLFG HLVWATGFMF LISWRGYWQE LIETLAWAHE RTPLANLIRW RDKPVALSIV QARLVGLAHF SVGYIFTY A AFLIASTSGK FG

UniProtKB: Photosystem I P700 chlorophyll a apoprotein A2

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Macromolecule #29: Photosystem I iron-sulfur center

MacromoleculeName: Photosystem I iron-sulfur center / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO / EC number: photosystem I
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 9.035483 KDa
SequenceString:
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT DFLSVRVYLW HETTRSMGLG Y

UniProtKB: Photosystem I iron-sulfur center

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Macromolecule #30: Photosystem I reaction center subunit II, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit II, chloroplastic
type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 16.05348 KDa
SequenceString:
GFTPPELDPN TPSPIFAGST GGLLRKAQVE EFYVITWESP KEQIFEMPTG GAAIMREGPN LLKLARKEQC LALGTRLRSK YKIKYQFYR VFPSGEVQYL HPKDGVYPEK VNPGRQGVGL NMRSIGKNVS PIEVKFTGKQ PYDL

UniProtKB: Photosystem I reaction center subunit II, chloroplastic

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Macromolecule #31: Photosystem I reaction center subunit IV, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit IV, chloroplastic
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 7.736863 KDa
SequenceString:
KPPPIGPKRG SKVRIMRKES YWYKGVGSVV AVDQDPKTRY PVVVRFNKVN YANVSTNNYA LDEIQEVA

UniProtKB: Photosystem I reaction center subunit IV, chloroplastic

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Macromolecule #32: Photosystem I reaction center subunit III, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit III, chloroplastic
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 17.151859 KDa
SequenceString:
DIAGLTPCKE SKQFAKREKQ ALKKLQASLK LYADDSAPAL AIKATMEKTK KRFDNYGKYG LLCGSDGLPH LIVSGDQRHW GEFITPGIL FLYIAGWIGW VGRSYLIAIR DEKKPTQKEI IIDVPLASSL LFRGFSWPVA AYRELLNGEL VDNN

UniProtKB: Photosystem I reaction center subunit III, chloroplastic

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Macromolecule #33: Photosystem I reaction center subunit V, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit V, chloroplastic
type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 10.719099 KDa
SequenceString:
LSPSLVISLS TGLSLFLGRF VFFNFQRENM AKQVPEQNGM SHFEAGDTRA KEYVSLLKSN DPVGFNIVDV LAWGSIGHIV AYYILATAS NGYDPSFF

UniProtKB: Photosystem I reaction center subunit V, chloroplastic

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Macromolecule #34: Photosystem I reaction center subunit VI, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit VI, chloroplastic
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 10.391756 KDa
SequenceString:
KYGDKSVYFD LEDIANTTGQ WDVYGSDAPS PYNSLQSKFF ETFAAPFTKR GLLLKFLILG GGSLLTYVSA NAPQDVLPIT RGPQQPPKL GPRGKI

UniProtKB: Photosystem I reaction center subunit VI, chloroplastic

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Macromolecule #35: Photosystem I reaction center subunit VIII

MacromoleculeName: Photosystem I reaction center subunit VIII / type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 3.458225 KDa
SequenceString:
MNFPSIFVPL VGLVFPAIAM ASLFLYVQKN K

UniProtKB: Photosystem I reaction center subunit VIII

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Macromolecule #36: Photosystem I reaction center subunit IX

MacromoleculeName: Photosystem I reaction center subunit IX / type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 4.845679 KDa
SequenceString:
MRDFKTYLSV APVLSTLWFG SLAGLLIEIN RFFPDALTFP FF

UniProtKB: Photosystem I reaction center subunit IX

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Macromolecule #37: PSI-K

MacromoleculeName: PSI-K / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 13.229404 KDa
SequenceString:
MASVMMTSLP QFTGLRSQQA SFPVKSLSAG LPLRGKGKGA LGARCGDFIG SSTNLIMVTS TTLMLFAGRF GLAPSANRKS TAGLRLEVR DSGLQTGDPA GFTLADTLAC GSFGHIIGVG VVLGLKNIGA I

UniProtKB: PSI-K

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Macromolecule #38: Photosystem I reaction center subunit XI, chloroplastic

MacromoleculeName: Photosystem I reaction center subunit XI, chloroplastic
type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 16.988656 KDa
SequenceString:
QVIQPLNGDP FIGGLETPVT SSPLIAWYLS NLPAYRTAVN PLLRGVEVGL AHGFLLVGPF VKAGPLRNTE YAGAAGSLAA AGLVVILSM CLTMYGIASF KEGEPSIAPA LTLTGRKKQP DQLQSADGWA KFTGGFFFGG VSGVTWACFL MYVLDLPYYF K

UniProtKB: Photosystem I reaction center subunit XI, chloroplastic

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Macromolecule #39: Chlorophyll a-b binding protein, chloroplastic

MacromoleculeName: Chlorophyll a-b binding protein, chloroplastic / type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 23.94734 KDa
SequenceString: GGISSVCEPL PPDRPLWFPG STPPQWLDGS LPGDFGFDPL GLGSDPETLR WFAQAELMHS RWAMLAVAGI LIPEWLESIG LMENFNWYD AGSREYFADP TTLFVVQLAL MGWVEGRRWA DYVNPGCVDI EPKLPNRKNP KPDVGYPGGL WFDFMMWGRG S PEPVMVLR ...String:
GGISSVCEPL PPDRPLWFPG STPPQWLDGS LPGDFGFDPL GLGSDPETLR WFAQAELMHS RWAMLAVAGI LIPEWLESIG LMENFNWYD AGSREYFADP TTLFVVQLAL MGWVEGRRWA DYVNPGCVDI EPKLPNRKNP KPDVGYPGGL WFDFMMWGRG S PEPVMVLR TKEIKNGRLA MLAFVGLCFQ AVYTGEGPLE NLSRHVADPG HCNIFSA

UniProtKB: Chlorophyll a-b binding protein, chloroplastic

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Macromolecule #40: Chlorophyll a-b binding protein, chloroplastic

MacromoleculeName: Chlorophyll a-b binding protein, chloroplastic / type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 22.135113 KDa
SequenceString: KKGEWLPGLA SPGYLTGSLP GDNGFDPLAL AEDPENLRWF VQAELVNGRW AMLGVAGMLL PEVFTSIGII DVPKWYDAGK SEYFASSST LFVIEFILFH YVEIRRWQDI KNPGCVNQDP IFKQYSLPPN ECGYPGGIFN PLNFAPTTEA KEKELANGRL A MLAFLGFI ...String:
KKGEWLPGLA SPGYLTGSLP GDNGFDPLAL AEDPENLRWF VQAELVNGRW AMLGVAGMLL PEVFTSIGII DVPKWYDAGK SEYFASSST LFVIEFILFH YVEIRRWQDI KNPGCVNQDP IFKQYSLPPN ECGYPGGIFN PLNFAPTTEA KEKELANGRL A MLAFLGFI VQHNVTGKGP FDNLQQHLSD PWHNTIIQTF

UniProtKB: Chlorophyll a-b binding protein, chloroplastic

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Macromolecule #41: Chlorophyll a-b binding protein, chloroplastic

MacromoleculeName: Chlorophyll a-b binding protein, chloroplastic / type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 24.168625 KDa
SequenceString: RPLWFASKQS LSYLDGSLPG DFGFDPLGLS DPEGTGGFIE PRWLAYGEII NGRYAMLGAV GAIAPEILGK AGLIPQETAL PWFQTGVIP PAGTYNYWAD PFTLFVFEMA LMGFAEHRRL QDWYNPGSMG KQYFLGLEKG FAGSGEPAYP GGPIFNPLGF G KDEKSLKE ...String:
RPLWFASKQS LSYLDGSLPG DFGFDPLGLS DPEGTGGFIE PRWLAYGEII NGRYAMLGAV GAIAPEILGK AGLIPQETAL PWFQTGVIP PAGTYNYWAD PFTLFVFEMA LMGFAEHRRL QDWYNPGSMG KQYFLGLEKG FAGSGEPAYP GGPIFNPLGF G KDEKSLKE LKLKEVKNGR LAMLAILGYF IQGLVTGVGP YQNLLDHLAD PVNNNILTSL KFH

UniProtKB: Chlorophyll a-b binding protein, chloroplastic

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Macromolecule #42: Chlorophyll a-b binding protein, chloroplastic

MacromoleculeName: Chlorophyll a-b binding protein, chloroplastic / type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 21.184209 KDa
SequenceString: EWMPGQPRPA HLDGSAPGDF GFDPLGLGEV PENLERFKES ELIHCRWAML AVPGILVPEA LGLGNWVKAQ EWAALPGGQA TYLGNPVPW GNLPTILAIE FLAIAFVEHQ RSMEKDSEKK KYPGGAFDPL GYSKDPKKFE ELKLKEIKNG RLALLAFVGF C IQQSAYPG ...String:
EWMPGQPRPA HLDGSAPGDF GFDPLGLGEV PENLERFKES ELIHCRWAML AVPGILVPEA LGLGNWVKAQ EWAALPGGQA TYLGNPVPW GNLPTILAIE FLAIAFVEHQ RSMEKDSEKK KYPGGAFDPL GYSKDPKKFE ELKLKEIKNG RLALLAFVGF C IQQSAYPG TGPLENLATH LADPWHNNIG DIVIP

UniProtKB: Chlorophyll a-b binding protein, chloroplastic

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Macromolecule #43: BETA-CAROTENE

MacromoleculeName: BETA-CAROTENE / type: ligand / ID: 43 / Number of copies: 29 / Formula: BCR
Molecular weightTheoretical: 536.873 Da
Chemical component information

ChemComp-BCR:
BETA-CAROTENE

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Macromolecule #44: (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: 44 / Number of copies: 24 / 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

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Macromolecule #45: 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl alpha-maltoside

MacromoleculeName: 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl alpha-maltoside
type: ligand / ID: 45 / Number of copies: 2 / Formula: A1H1M
Molecular weightTheoretical: 548.663 Da

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Macromolecule #46: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE

MacromoleculeName: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE / type: ligand / ID: 46 / Number of copies: 12 / Formula: LMG
Molecular weightTheoretical: 787.158 Da
Chemical component information

ChemComp-LMG:
1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE

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Macromolecule #47: 5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-HEPTAMETHYLOCTACOSA...

MacromoleculeName: 5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-HEPTAMETHYLOCTACOSA-2,6,10,14,18,22,26-HEPTAENYL]-2,3-DIMETHYLBENZO-1,4-QUINONE
type: ligand / ID: 47 / Number of copies: 1 / Formula: PQ9
Molecular weightTheoretical: 612.967 Da
Chemical component information

ChemComp-PQ9:
5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-HEPTAMETHYLOCTACOSA-2,6,10,14,18,22,26-HEPTAENYL]-2,3-DIMETHYLBENZO-1,4-QUINONE

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Macromolecule #48: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL

MacromoleculeName: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL
type: ligand / ID: 48 / Number of copies: 7 / Formula: SQD
Molecular weightTheoretical: 795.116 Da
Chemical component information

ChemComp-SQD:
1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL

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Macromolecule #49: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 49 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

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Macromolecule #50: CHLOROPHYLL A

MacromoleculeName: CHLOROPHYLL A / type: ligand / ID: 50 / Number of copies: 144 / Formula: CLA
Molecular weightTheoretical: 893.489 Da
Chemical component information

ChemComp-CLA:
CHLOROPHYLL A

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Macromolecule #51: DIGALACTOSYL DIACYL GLYCEROL (DGDG)

MacromoleculeName: DIGALACTOSYL DIACYL GLYCEROL (DGDG) / type: ligand / ID: 51 / Number of copies: 3 / Formula: DGD
Molecular weightTheoretical: 949.299 Da
Chemical component information

ChemComp-DGD:
DIGALACTOSYL DIACYL GLYCEROL (DGDG)

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Macromolecule #52: CHLOROPHYLL A ISOMER

MacromoleculeName: CHLOROPHYLL A ISOMER / type: ligand / ID: 52 / Number of copies: 1 / Formula: CL0
Molecular weightTheoretical: 893.489 Da
Chemical component information

ChemComp-CL0:
CHLOROPHYLL A ISOMER

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Macromolecule #53: PHYLLOQUINONE

MacromoleculeName: PHYLLOQUINONE / type: ligand / ID: 53 / Number of copies: 2 / Formula: PQN
Molecular weightTheoretical: 450.696 Da
Chemical component information

ChemComp-PQN:
PHYLLOQUINONE

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Macromolecule #54: CHLOROPHYLL B

MacromoleculeName: CHLOROPHYLL B / type: ligand / ID: 54 / Number of copies: 9 / Formula: CHL
Molecular weightTheoretical: 907.472 Da
Chemical component information

ChemComp-CHL:
CHLOROPHYLL B

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Macromolecule #55: (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL

MacromoleculeName: (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL
type: ligand / ID: 55 / Number of copies: 8 / Formula: LUT
Molecular weightTheoretical: 568.871 Da
Chemical component information

ChemComp-LUT:
(3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
DetailsTitan Krios G3i microscope at 300 kV, equipped with a K3 (Gatan) detector operating in electron counting mode, Bioquantum energy filter (Gatan)
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.19 Å / Resolution method: OTHER / Details: This is a composite map / Number images used: 38385
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial model
ChainPDB ID
source_name: AlphaFold, initial_model_type: in silico model
source_name: PDB, initial_model_type: experimental model

4y28

source_name: PDB, initial_model_type: experimental model

6khj

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-9grx:
NDH-PSI-LHCI supercomplex from S. oleracea

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