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

Basic information

Entry

Database: EMDB / ID: EMD-51527

• Title: NDH-PSI-LHCI supercomplex from S. oleracea: composite map
• Map data: Composite map

Sample

• Complex: NDH-PSI-LHCI supercomplex from Spinacia oleracea
  • Protein or peptide: x 42 types
• Ligand: x 13 types

• Keywords: NDH / PSI / Supercomplex / photosynthesis / electron transport chain / lipids / proton translocation / plastoquinone / ELECTRON TRANSPORT

Function / homology

Function:

glucose-6-phosphate 1-epimerase activity / NAD(P)H dehydrogenase complex (plastoquinone) / P450-containing electron transport chain / photosynthesis, light harvesting in photosystem I / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / thylakoid / NADH dehydrogenase complex / chloroplast thylakoid lumen / 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 / response to light stimulus / 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 / electron transport chain / 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

Domain/homology:

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.

Component:

Photosystem I reaction center subunit IX / Photosynthetic NDH subunit of lumenal location 2, chloroplastic / Peptidyl-prolyl cis-trans isomerase / Photosystem I reaction center subunit psaK, chloroplastic / 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

• Biological species: Spinacia oleracea (spinach)
• Method: single particle reconstruction / cryo EM / Resolution: 3.19 Å
• Authors: Introini B / Hahn A / Kuehlbrandt W

Funding support

Germany, 1 items

Organization	Grant number	Country
Other private		Germany

• Citation: Journal: 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 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

Deposition	Sep 13, 2024	-
Header (metadata) release	Feb 12, 2025	-
Map release	Feb 12, 2025	-
Update	Jun 25, 2025	-
Current status	Jun 25, 2025	Processing site: PDBe / Status: Released

Map

• File: Download / File: emd_51527.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Composite map
• Voxel size: X=Y=Z: 0.837 Å

Density

Contour Level	By AUTHOR: 0.3
Minimum - Maximum	-0.38743252 - 3.7443235
Average (Standard dev.)	0.043397125 (±0.08007511)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 512 512 512 Spacing 512 512 512
Cell	A=B=C: 428.544 Å α=β=γ: 90.0 °

Supplemental data

Sample components

Entire : NDH-PSI-LHCI supercomplex from Spinacia oleracea

• Entire: Name: 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

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

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

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

• Macromolecule: Name: 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 weight: Theoretical: 18.606793 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 44.622605 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 40.259473 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 15.61484 KDa

Sequence

String:

EEEELEPPYV GFAFVSSVLL PDGTPDMHLR SATGGQKLRD IMLDNDIDLY GPYARPLLNC AGGGTCASCM VEVIEGKELL NPRTEKEKE HLKKKPKNWR LACQITVGTP ESRGMVVIQQ LPEWKAHEWK YEKDGPIVSE

UniProtKB: Photosynthetic NDH subunit of subcomplex B 3, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 10.763025 KDa

Sequence

String:

MAVLVEHVEG QRDLITHKSI WHLSDAAIKN VYLFYMMFTC WGCCVFGAAK DPYYDSEQYR GDGGDGTGHW VYEKQEDIEE AGRAALWRE ELIE

UniProtKB: Photosynthetic NDH subunit of subcomplex B 4, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 17.77267 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 14.875953 KDa

Sequence

String:

EFKWGTRSFI WERFFEPGLS PEDAVSRIKN TAEGLHSLRH MLETMSWRYV IFYIRLKQAY LKQDMKSAMI MVPEGRRDDY SNAANELVD NMAEFDYYVR TPKVYESYVS YEKTLKSIDN LLGFLA

UniProtKB: Photosynthetic NDH subunit of lumenal location 2, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 16.451979 KDa

Sequence

String:

QLWLDGPLPG LRPAENKIGN EETGTRTFLK KGIYMANIGT KGSALRLRKY AFDLLAMEDL IGQDTLNYVR RYLRFKGTFM YYDFDKVIS AAPVADKPPL TNLANRLFDN FEKLQEAVKL KDVPLTRSCY DDTAVTLQEV MNRMA

UniProtKB: Photosynthetic NDH subunit of lumenal location 3, chloroplastic

Macromolecule #9: peptidylprolyl isomerase

• Macromolecule: Name: 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 weight: Theoretical: 15.352496 KDa

Sequence

String:

LRVEYYATTA EPSCELNLVR SGLGYCDLVV GSGVPAPYNT LINVHYTARF SDETVFDSSY KRGRPLTMRI GVGKVIKGLD QGIFGGDGV PPMQVGGKRK LRIPPHLGYG PEPAGCFSGD CNVPANATLL YDVTFMGVYS GNRA

UniProtKB: peptidylprolyl isomerase

Macromolecule #10: Peptidyl-prolyl cis-trans isomerase

• Macromolecule: Name: 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 weight: Theoretical: 18.900408 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 38.985613 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 54.026148 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 13.270651 KDa

Sequence

String:

YEYDIFWAFL IISSVIPILA FLFSGILAPI SKGPEKLSSY ESGIEPMGDA WLQFRIRYYM FALVFVVFDV ETVFLYPWAM SFDILGVSV FIEALIFVLI LIVGLVYAWR KGALEW

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

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

• Macromolecule: Name: 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 weight: Theoretical: 55.980191 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 11.085047 KDa

Sequence

String:

MILEHVLVLS AFLFSIGIYG LVTSRNLVRA LMCLELILNA VNLNFVTFSD FFDSRQLKGN IFSIFVIAIA AAEAAIGPAI VSSIYRNRK SIRINQSNLL N

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

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

• Macromolecule: Name: 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 weight: Theoretical: 84.590094 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 19.193654 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 45.172309 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 19.004875 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 18.687322 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 22.789359 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 13.194599 KDa

Sequence

String:

AVTGVNNQED LIWVLLKAGV VGFCYFLIMP PIIMNWLRIR WYRRNLLEMY FQFMFVFIFF PGILVWAPFL NFRKFPRDPT MKYPWSKPE NPSEVKGGFL KYPWATIEDY

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

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

• Macromolecule: Name: 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 weight: Theoretical: 16.702113 KDa

Sequence

String:

EMKEVLKRAT PIEAQVNVKS RNLEREYGGQ WLSSVTRHVR IYAAYIDPVT CAMDQTQMDK LTLMIDPTDE FLWNDETLNK VYVYFEELV DHYEGAPLTE YTLRLIGSDI EHYIRKMLYE GEIKYNMNSR VLNFSMGKPR MK

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

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

• Macromolecule: Name: 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 weight: Theoretical: 18.727768 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 11.127798 KDa

Sequence

String:

PPPKKPPKPV YSMKKGQIVR VEREKYLDSV NYLSVGHPKY YKGLDYIYED RGEVLDLRFF ETGEYALVSW VGIPTSPAWL PTDMLIKSD KLNYER

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

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

• Macromolecule: Name: 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 weight: Theoretical: 27.127314 KDa

Sequence

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

Macromolecule #27: Photosystem I P700 chlorophyll a apoprotein A1

• Macromolecule: Name: 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 weight: Theoretical: 82.144953 KDa

Sequence

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

Macromolecule #28: Photosystem I P700 chlorophyll a apoprotein A2

• Macromolecule: Name: 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 weight: Theoretical: 82.377547 KDa

Sequence

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

Macromolecule #29: Photosystem I iron-sulfur center

• Macromolecule: Name: 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 weight: Theoretical: 9.035483 KDa

Sequence

String:

MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT DFLSVRVYLW HETTRSMGLG Y

UniProtKB: Photosystem I iron-sulfur center

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

• Macromolecule: Name: 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 weight: Theoretical: 16.05348 KDa

Sequence

String:

GFTPPELDPN TPSPIFAGST GGLLRKAQVE EFYVITWESP KEQIFEMPTG GAAIMREGPN LLKLARKEQC LALGTRLRSK YKIKYQFYR VFPSGEVQYL HPKDGVYPEK VNPGRQGVGL NMRSIGKNVS PIEVKFTGKQ PYDL

UniProtKB: Photosystem I reaction center subunit II, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 7.736863 KDa

Sequence

String:

KPPPIGPKRG SKVRIMRKES YWYKGVGSVV AVDQDPKTRY PVVVRFNKVN YANVSTNNYA LDEIQEVA

UniProtKB: Photosystem I reaction center subunit IV, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 17.151859 KDa

Sequence

String:

DIAGLTPCKE SKQFAKREKQ ALKKLQASLK LYADDSAPAL AIKATMEKTK KRFDNYGKYG LLCGSDGLPH LIVSGDQRHW GEFITPGIL FLYIAGWIGW VGRSYLIAIR DEKKPTQKEI IIDVPLASSL LFRGFSWPVA AYRELLNGEL VDNN

UniProtKB: Photosystem I reaction center subunit III, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 10.719099 KDa

Sequence

String:

LSPSLVISLS TGLSLFLGRF VFFNFQRENM AKQVPEQNGM SHFEAGDTRA KEYVSLLKSN DPVGFNIVDV LAWGSIGHIV AYYILATAS NGYDPSFF

UniProtKB: Photosystem I reaction center subunit V, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 10.391756 KDa

Sequence

String:

KYGDKSVYFD LEDIANTTGQ WDVYGSDAPS PYNSLQSKFF ETFAAPFTKR GLLLKFLILG GGSLLTYVSA NAPQDVLPIT RGPQQPPKL GPRGKI

UniProtKB: Photosystem I reaction center subunit VI, chloroplastic

Macromolecule #35: Photosystem I reaction center subunit VIII

• Macromolecule: Name: 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 weight: Theoretical: 3.458225 KDa

Sequence

String:

MNFPSIFVPL VGLVFPAIAM ASLFLYVQKN K

UniProtKB: Photosystem I reaction center subunit VIII

Macromolecule #36: Photosystem I reaction center subunit IX

• Macromolecule: Name: 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 weight: Theoretical: 4.845679 KDa

Sequence

String:

MRDFKTYLSV APVLSTLWFG SLAGLLIEIN RFFPDALTFP FF

UniProtKB: Photosystem I reaction center subunit IX

Macromolecule #37: PSI-K

• Macromolecule: Name: PSI-K / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Spinacia oleracea (spinach)
• Molecular weight: Theoretical: 13.229404 KDa

Sequence

String:

MASVMMTSLP QFTGLRSQQA SFPVKSLSAG LPLRGKGKGA LGARCGDFIG SSTNLIMVTS TTLMLFAGRF GLAPSANRKS TAGLRLEVR DSGLQTGDPA GFTLADTLAC GSFGHIIGVG VVLGLKNIGA I

UniProtKB: Photosystem I reaction center subunit psaK, chloroplastic

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

• Macromolecule: Name: 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 weight: Theoretical: 16.988656 KDa

Sequence

String:

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

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

• Macromolecule: Name: 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 weight: Theoretical: 23.94734 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 22.135113 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 24.168625 KDa

Sequence

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

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

• Macromolecule: Name: 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 weight: Theoretical: 21.184209 KDa

Sequence

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

Macromolecule #43: BETA-CAROTENE

• Macromolecule: Name: BETA-CAROTENE / type: ligand / ID: 43 / Number of copies: 29 / Formula: BCR
• Molecular weight: Theoretical: 536.873 Da

Chemical component information

ChemComp-BCR:
BETA-CAROTENE

Macromolecule #44: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

• Macromolecule: Name: (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 weight: Theoretical: 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

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

• Macromolecule: Name: 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl alpha-maltoside; type: ligand / ID: 45 / Number of copies: 2 / Formula: A1H1M
• Molecular weight: Theoretical: 548.663 Da

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

• Macromolecule: Name: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE / type: ligand / ID: 46 / Number of copies: 12 / Formula: LMG
• Molecular weight: Theoretical: 787.158 Da

Chemical component information

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

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

• Macromolecule: Name: 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 weight: Theoretical: 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

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

• Macromolecule: Name: 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 weight: Theoretical: 795.116 Da

Chemical component information

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

Macromolecule #49: IRON/SULFUR CLUSTER

• Macromolecule: Name: IRON/SULFUR CLUSTER / type: ligand / ID: 49 / Number of copies: 6 / Formula: SF4
• Molecular weight: Theoretical: 351.64 Da

Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

Macromolecule #50: CHLOROPHYLL A

• Macromolecule: Name: CHLOROPHYLL A / type: ligand / ID: 50 / Number of copies: 144 / Formula: CLA
• Molecular weight: Theoretical: 893.489 Da

Chemical component information

ChemComp-CLA:
CHLOROPHYLL A

Macromolecule #51: DIGALACTOSYL DIACYL GLYCEROL (DGDG)

• Macromolecule: Name: DIGALACTOSYL DIACYL GLYCEROL (DGDG) / type: ligand / ID: 51 / Number of copies: 3 / Formula: DGD
• Molecular weight: Theoretical: 949.299 Da

Chemical component information

ChemComp-DGD:
DIGALACTOSYL DIACYL GLYCEROL (DGDG)

Macromolecule #52: CHLOROPHYLL A ISOMER

• Macromolecule: Name: CHLOROPHYLL A ISOMER / type: ligand / ID: 52 / Number of copies: 1 / Formula: CL0
• Molecular weight: Theoretical: 893.489 Da

Chemical component information

ChemComp-CL0:
CHLOROPHYLL A ISOMER

Macromolecule #53: PHYLLOQUINONE

• Macromolecule: Name: PHYLLOQUINONE / type: ligand / ID: 53 / Number of copies: 2 / Formula: PQN
• Molecular weight: Theoretical: 450.696 Da

Chemical component information

ChemComp-PQN:
PHYLLOQUINONE

Macromolecule #54: CHLOROPHYLL B

• Macromolecule: Name: CHLOROPHYLL B / type: ligand / ID: 54 / Number of copies: 9 / Formula: CHL
• Molecular weight: Theoretical: 907.472 Da

Chemical component information

ChemComp-CHL:
CHLOROPHYLL B

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

• Macromolecule: Name: (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 weight: Theoretical: 568.871 Da

Chemical component information

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

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Buffer: pH: 7.8
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: TFS KRIOS
• Details: Titan Krios G3i microscope at 300 kV, equipped with a K3 (Gatan) detector operating in electron counting mode, Bioquantum energy filter (Gatan)
• Image recording: Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination 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

Image processing

• CTF correction: Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
• Startup model: Type of model: INSILICO MODEL
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 3.19 Å / Resolution method: OTHER / Details: This is a composite map / Number images used: 38385
• Initial angle assignment: Type: ANGULAR RECONSTITUTION
• Final angle assignment: Type: MAXIMUM LIKELIHOOD

Atomic model buiding 1

Initial model

Chain	PDB 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

• Refinement: Space: REAL / Protocol: AB INITIO MODEL

Output model

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