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- EMDB-15865: Cryo-EM structure of NADH:ubiquinone oxidoreductase (complex-I) f... -

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Basic information

Entry
Database: EMDB / ID: EMD-15865
TitleCryo-EM structure of NADH:ubiquinone oxidoreductase (complex-I) from respiratory supercomplex of Tetrahymena thermophila
Map dataSharpened mask refined map
Sample
  • Complex: NADH:ubiquinone oxidoreductase complex (complex-I) from respiratory supercomplex of Tetrahymena thermophila
    • Protein or peptide: x 69 types
  • Ligand: x 13 types
Function / homology
Function and homology information


NADH:ubiquinone reductase (H+-translocating) / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / medium-chain fatty acid-CoA ligase activity / P450-containing electron transport chain / ubiquinone-6 biosynthetic process / oxidoreductase activity, acting on NAD(P)H / lipid A biosynthetic process / NADH dehydrogenase activity / NADH:ubiquinone reductase (H+-translocating) ...NADH:ubiquinone reductase (H+-translocating) / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / medium-chain fatty acid-CoA ligase activity / P450-containing electron transport chain / ubiquinone-6 biosynthetic process / oxidoreductase activity, acting on NAD(P)H / lipid A biosynthetic process / NADH dehydrogenase activity / NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / chloroplast thylakoid membrane / respirasome / acyl binding / electron transport coupled proton transport / NADH dehydrogenase (ubiquinone) activity / acyl carrier activity / quinone binding / ATP synthesis coupled electron transport / aerobic respiration / respiratory electron transport chain / mitochondrion organization / chloroplast / fatty acid metabolic process / electron transport chain / mitochondrial membrane / phospholipid binding / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / oxidoreductase activity / ribosome / protein-containing complex binding / negative regulation of apoptotic process / protein kinase binding / mitochondrion / membrane / metal ion binding / cytosol
Similarity search - Function
Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : / Dynactin subunit 5 / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. ...Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : / Dynactin subunit 5 / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / Hexapeptide repeat / Soluble ligand binding domain / SLBB domain / 2Fe-2S iron-sulfur cluster binding domain / Zinc finger, CHCC-type / Zinc-finger domain / Bacterial transferase hexapeptide (six repeats) / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH-ubiquinone oxidoreductase, 20 Kd subunit / Thioredoxin / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Trimeric LpxA-like superfamily / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / NuoE domain / NADH:ubiquinone oxidoreductase / AMP-dependent synthetase/ligase / AMP-binding enzyme / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / NAD-dependent epimerase/dehydratase / NAD dependent epimerase/dehydratase family / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / [NiFe]-hydrogenase, large subunit / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Acyl carrier protein (ACP) / Beta-grasp domain superfamily / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain
Similarity search - Domain/homology
Transmembrane protein, putative / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Transmembrane protein, putative / Uncharacterized protein / Uncharacterized protein / Transmembrane protein / NADH dehydrogenase, putative / Gamma-carbonic anhydrase / Transmembrane protein ...Transmembrane protein, putative / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Transmembrane protein, putative / Uncharacterized protein / Uncharacterized protein / Transmembrane protein / NADH dehydrogenase, putative / Gamma-carbonic anhydrase / Transmembrane protein / Transcription factor apfi protein, putative / Transmembrane protein, putative / Ribosomal protein L51/S25/CI-B8 domain protein / Transmembrane protein / Acyl carrier protein / NADH-ubiquinone oxidoreductase 1, chain, putative / NADH-ubiquinone oxidoreductase 24 kDa subunit / Transmembrane protein / Transmembrane protein, putative / Transmembrane protein / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / Zinc-finger protein / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NAD-dependent epimerase/dehydratase family protein / Transmembrane protein / Thioredoxin / Transmembrane protein, putative / DnaJ domain protein / lipid-A-disaccharide synthase / Transmembrane protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein, putative / 2 iron, 2 sulfur cluster-binding protein / Transmembrane protein / Acyl carrier protein / Gamma-carbonic anhydrase / Transmembrane protein, putative / Transmembrane protein / Uncharacterized protein / Uncharacterized protein / NADH-ubiquinone oxidoreductase 75 kDa subunit / Uncharacterized protein / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / Uncharacterized protein / ETC complex I subunit motif protein / Transmembrane protein, putative / Transmembrane protein, putative / Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II / NADH-ubiquinone oxidoreductase chain 4 / Ymf62 / NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase subunit 5 / NADH dehydrogenase subunit 9 / Ymf58 / NADH-ubiquinone oxidoreductase chain 3 / Ymf65 / NADH dehydrogenase subunit 7 / NADH dehydrogenase subunit 2 / NADH dehydrogenase subunit 10 / Ymf57 / GRAM domain protein
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote) / Tetrahymena thermophila SB210 (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsMuhleip A / Kock Flygaard R / Amunts A
Funding support Sweden, European Union, 4 items
OrganizationGrant numberCountry
The Swedish Foundation for Strategic ResearchFFL15:0325 Sweden
Cancerfonden2017/1041 Sweden
European Research Council (ERC)ERC-2018-StG-805230European Union
Knut and Alice Wallenberg Foundation2018.0080 Sweden
Citation
Journal: Nature / Year: 2023
Title: Structural basis of mitochondrial membrane bending by the I-II-III-IV supercomplex.
Authors: Alexander Mühleip / Rasmus Kock Flygaard / Rozbeh Baradaran / Outi Haapanen / Thomas Gruhl / Victor Tobiasson / Amandine Maréchal / Vivek Sharma / Alexey Amunts /
Abstract: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes ...Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III-IV supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization.
#1: Journal: Biorxiv / Year: 2022
Title: Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplex
Authors: Muhleip A / Flygaard RK / Haapanen O / Baradaran R / Gruhl T / Tobiasson V / Marechal A / Sharma V / Amunts A
History
DepositionSep 27, 2022-
Header (metadata) releaseMar 29, 2023-
Map releaseMar 29, 2023-
UpdateApr 12, 2023-
Current statusApr 12, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_15865.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened mask refined map
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.25 Å/pix.
x 480 pix.
= 600. Å
1.25 Å/pix.
x 480 pix.
= 600. Å
1.25 Å/pix.
x 480 pix.
= 600. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.25 Å
Density
Contour LevelBy AUTHOR: 0.9
Minimum - Maximum-2.720985 - 5.836473
Average (Standard dev.)0.0026114804 (±0.17868203)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 600.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_15865_msk_1.map
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Additional map: Unsharpened mask refined map

Fileemd_15865_additional_1.map
AnnotationUnsharpened mask refined map
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Half map: Half-map A

Fileemd_15865_half_map_1.map
AnnotationHalf-map A
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Half map: Half-map B

Fileemd_15865_half_map_2.map
AnnotationHalf-map B
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Sample components

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Entire : NADH:ubiquinone oxidoreductase complex (complex-I) from respirato...

EntireName: NADH:ubiquinone oxidoreductase complex (complex-I) from respiratory supercomplex of Tetrahymena thermophila
Components
  • Complex: NADH:ubiquinone oxidoreductase complex (complex-I) from respiratory supercomplex of Tetrahymena thermophila
    • Protein or peptide: Lipid-A-disaccharide synthase
    • Protein or peptide: NAD-dependent epimerase/dehydratase family protein
    • Protein or peptide: DnaJ domain protein
    • Protein or peptide: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
    • Protein or peptide: RNase III domain-containing protein
    • Protein or peptide: 37S ribosomal protein S25, mitochondrialRibosome
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: CX9C domain-containing protein
    • Protein or peptide: NDUTT15
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: NADH dehydrogenase subunit 5
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase subunit 7
    • Protein or peptide: Ymf65
    • Protein or peptide: Transcription factor apfi protein, putative
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH-ubiquinone oxidoreductase 24 kDa subunit
    • Protein or peptide: Ymf62
    • Protein or peptide: Gamma-carbonic anhydrase
    • Protein or peptide: NADH-ubiquinone oxidoreductase 1, chain, putative
    • Protein or peptide: Gamma-carbonic anhydrase
    • Protein or peptide: ETC complex I subunit motif protein
    • Protein or peptide: NADH dehydrogenase subunit 9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase, putative
    • Protein or peptide: NADH dehydrogenase subunit 10
    • Protein or peptide: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: Ymf58
    • Protein or peptide: Ribosomal protein L51/S25/CI-B8 domain proteinRibosome
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: ATP synthase subunit e, mitochondrial
    • Protein or peptide: GRAM domain protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: ND1b
    • Protein or peptide: Transmembrane protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: NDUB8
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: NDUPH2
    • Protein or peptide: NDUB10
    • Protein or peptide: NDUA13
    • Protein or peptide: NADH dehydrogenase subunit 2
    • Protein or peptide: 2 iron, 2 sulfur cluster-binding protein
    • Protein or peptide: Thioredoxin
    • Protein or peptide: COX assembly mitochondrial protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: PH domain-containing protein
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NDUB6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
    • Protein or peptide: Zinc-finger proteinZinc finger
    • Protein or peptide: NDUB4
    • Protein or peptide: NDUB15
    • Protein or peptide: NDUTT16
    • Protein or peptide: NDUTT17
    • Protein or peptide: CHCH domain-containing protein
    • Protein or peptide: Transmembrane protein, putativeTransmembrane protein
    • Protein or peptide: Ymf57
    • Protein or peptide: Complex I-MNLL
  • Ligand: CARDIOLIPIN
  • Ligand: URIDINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • Ligand: ZINC ION

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Supramolecule #1: NADH:ubiquinone oxidoreductase complex (complex-I) from respirato...

SupramoleculeName: NADH:ubiquinone oxidoreductase complex (complex-I) from respiratory supercomplex of Tetrahymena thermophila
type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#69
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 1.52 MDa

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Macromolecule #1: Lipid-A-disaccharide synthase

MacromoleculeName: Lipid-A-disaccharide synthase / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: lipid-A-disaccharide synthase
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 59.307289 KDa
SequenceString: MLTHISRRYF SFTGRKTIFV AAGSPSHDLQ AANFMRDLKK KSNNNYDFVG IGGPLMQAEG LNQSYADINK FIDKPFFPLK NFIRFHVAR CYHPYMAPLH FFNKQVLNQV DKSSLLKDQV ELSIPSAIIT FGNEFFMKKL YVRLCDQYEL HNKIRPPTFF Y DRSHINQR ...String:
MLTHISRRYF SFTGRKTIFV AAGSPSHDLQ AANFMRDLKK KSNNNYDFVG IGGPLMQAEG LNQSYADINK FIDKPFFPLK NFIRFHVAR CYHPYMAPLH FFNKQVLNQV DKSSLLKDQV ELSIPSAIIT FGNEFFMKKL YVRLCDQYEL HNKIRPPTFF Y DRSHINQR FEFQDYLDHF FYTIPMKQIN FQSFTYPSTC VGHEGVGRAI QYLFQNSKQY ANVKSLVTAN GLKIASNPKQ HR EIIEKLV EEQRGIQRAR LGINESKNVF LLAPGNTKAE INFAVNLLSR SLEEFFKKPQ LTNVSRDHFT IIITADNAQN AEF VNQAVS NTKYLKTLQT IVTTGEKEKF GAMCAADVGI PLNGELVSEC AALQLPSVII SNMNLFYAYI TQLYNNFYSD INFA IQGEA YHELVSTAAN PYKLSDEIFD LYSDPKLRYH FAERYQNVVH EMIPQANSQD NIVTTDVATL HGVEVQERAF TYETI AAKV LKAARAYESL DKNIPNHQID QHRKEKLIKA AF

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Macromolecule #2: NAD-dependent epimerase/dehydratase family protein

MacromoleculeName: NAD-dependent epimerase/dehydratase family protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 41.37509 KDa
SequenceString: MIGKTQQRLN KCLIQVIQKQ FSQQRSTQLK FYDGGNRQSI SGIRATIFGA TGFMGPYIGA ALGYIGSDVI FPHNHVYAYD DYVKELKLC AGSGQSYIMR HFNYDDDNMY DMAIKNSNVV INLVGSRLQN KNFQKAAYAN IHVAKKIAEA CARNPNVRRL I HFSAAGAD ...String:
MIGKTQQRLN KCLIQVIQKQ FSQQRSTQLK FYDGGNRQSI SGIRATIFGA TGFMGPYIGA ALGYIGSDVI FPHNHVYAYD DYVKELKLC AGSGQSYIMR HFNYDDDNMY DMAIKNSNVV INLVGSRLQN KNFQKAAYAN IHVAKKIAEA CARNPNVRRL I HFSAAGAD TKSPSPDLHT KFHGEEAVLN AFPNATIFRP CTVYGMQDYF IRHWIKERDW WYHFNIVTDD CTAKRQPILI ND VAQCVLN ALKLQESAGQ IYELGGPHVY SRLEVFEMLA NLSGRPPKLA HIPHDIALKI TQNFYNWEFF NMEKVIKDKL DLI VTGKHK TISDLYVQPV SFPQGAEQFI DDVRYRGVET HDNLEK

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Macromolecule #3: DnaJ domain protein

MacromoleculeName: DnaJ domain protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 36.878367 KDa
SequenceString: MIVNRLFRQQ FRNISYGFAT QKLDYYAVLG VDRLATAEQI KDSYRKLAMK YHPDVNTTVT EAHEPSARKF QEIAEAYAVL SVEEQRRAY DFLNQPSPYD RYTEDSALED ELLRRRSVDG NAIRQPHKVG TYAAEKQRLL AEERAKFNVD HLGRYKGGLP V KGKGSIRK ...String:
MIVNRLFRQQ FRNISYGFAT QKLDYYAVLG VDRLATAEQI KDSYRKLAMK YHPDVNTTVT EAHEPSARKF QEIAEAYAVL SVEEQRRAY DFLNQPSPYD RYTEDSALED ELLRRRSVDG NAIRQPHKVG TYAAEKQRLL AEERAKFNVD HLGRYKGGLP V KGKGSIRK GIHGEGFGAP SHAHDALIHQ IKQSKDTMDY QNITNEVAQN FANHQNNDRW VYERRKSNFI AQVDYEYFKF NH WRTAWRY FRNIFLLTAG VSFLYNMELD EGLGGLSLKY KEFVKTNPGQ DLLIGNIRVT QRPNGLLVAV DAHQKQHHHH

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Macromolecule #4: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II

MacromoleculeName: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 36.709441 KDa
SequenceString: MKLFSQVNRF AFSTANKAAS PLAAQLAING NRNAVRYENQ NRTWTFNELD AHTNAFAYGL TELGWKAGDK LLLWVEKNHT SEITTAQVG AAKAGVTLVP IYAHSAEELE KALNDTKAKG LLLSPNSKAG NSKYIEVVNK VIPELYNTGR GSTLKTKFAN L QHIIHTGF ...String:
MKLFSQVNRF AFSTANKAAS PLAAQLAING NRNAVRYENQ NRTWTFNELD AHTNAFAYGL TELGWKAGDK LLLWVEKNHT SEITTAQVG AAKAGVTLVP IYAHSAEELE KALNDTKAKG LLLSPNSKAG NSKYIEVVNK VIPELYNTGR GSTLKTKFAN L QHIIHTGF YTFPGTYKFR QIMVYASKNF NTLTLPNVEL NAPLFISGNQ TYTLKDLISK TEENRKTSKL NDNTPVFVTG DS RSPLSFS LGILNSLLHG NYSVYTGAQD LNEVGQTIRF YDNALLLVDG DIVKATQSLK HSENFAKLGG VAANENIPKD SLN QLFGGK LVQQLKI

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Macromolecule #5: RNase III domain-containing protein

MacromoleculeName: RNase III domain-containing protein / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 35.409246 KDa
SequenceString: MSGLLRNFEK LVCQSQLSKA GHKLLLRSPN STLHPTAFYY KRNSSQRLAN EMDVFQLGLA AAALTRQANN YAQLLDQVDK EAVREEVQE RITQNHSDLN VYFGEILSLF KIGKKECPVQ TVADISYVLA FGPIQVPNAA AIITENLLPV LKEKLDYASI H NLQDILSA ...String:
MSGLLRNFEK LVCQSQLSKA GHKLLLRSPN STLHPTAFYY KRNSSQRLAN EMDVFQLGLA AAALTRQANN YAQLLDQVDK EAVREEVQE RITQNHSDLN VYFGEILSLF KIGKKECPVQ TVADISYVLA FGPIQVPNAA AIITENLLPV LKEKLDYASI H NLQDILSA FVKLNYVSDK ELLKRLITAL SQKDFPNQLQ PVTNHAWNID QYEYSDCNSW NIVSCGDNTF EKYIHEGGCE NS LAKAKFA VHELLDHISF NFVNPFLFRE NRINHRFAKR NADLDHEVLM QTLSKLQEIV PETSEAIATI KARL

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Macromolecule #6: 37S ribosomal protein S25, mitochondrial

MacromoleculeName: 37S ribosomal protein S25, mitochondrial / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 33.201797 KDa
SequenceString: MRKALERFNE IIFNPAIRWY QLPKPTVRRT RYPAPGSEPI NREVHQIDYK TAFRDSPHNI RYHHEIHTSD QTYHSSYDPV GETTTERLV RYGYLNKDQV NNAEAVAAAA KEFQEKEKRS PSNNIIIDEI SNSDKPITKE NRESVAHHVR QQFEFFREVN A EEVWSVSI ...String:
MRKALERFNE IIFNPAIRWY QLPKPTVRRT RYPAPGSEPI NREVHQIDYK TAFRDSPHNI RYHHEIHTSD QTYHSSYDPV GETTTERLV RYGYLNKDQV NNAEAVAAAA KEFQEKEKRS PSNNIIIDEI SNSDKPITKE NRESVAHHVR QQFEFFREVN A EEVWSVSI EEKYNPELYI YKTYDMAADD PVWRQVKLDL EWTFENIAER RESLGYMPTF KGDPNFWQAL DNSFSPENIA QV QSSIGDK VTNIDTKALA LNHQTEEYHK TSKLVYPIRT NLVVE

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Macromolecule #7: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 29.38966 KDa
SequenceString: MIARRLFKRS LYYIPRAGFG GGDIRHKFSN EITDDDYDYQ RAMHVKPPKE ESLFQLTNIL SSVPVFKTRF FLDFIARNLD TNSAVSTSD FVAPPRVHEN SFFVYHSREL GNVIRKYRSL ESIVLPGALL TFTYPLFAAF VAIPSYYFMF NAKIYEMSRR F VVRMDVLP ...String:
MIARRLFKRS LYYIPRAGFG GGDIRHKFSN EITDDDYDYQ RAMHVKPPKE ESLFQLTNIL SSVPVFKTRF FLDFIARNLD TNSAVSTSD FVAPPRVHEN SFFVYHSREL GNVIRKYRSL ESIVLPGALL TFTYPLFAAF VAIPSYYFMF NAKIYEMSRR F VVRMDVLP HLEMISVQRI GAFGILYTKL HRIQDLEYVP FDQVKEQENY LWAIGGHGVD NQLIFKDRST GEFFYFERQG VW DAKGLNH PLLN

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Macromolecule #8: CX9C domain-containing protein

MacromoleculeName: CX9C domain-containing protein / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 28.412805 KDa
SequenceString: MSILNLIKNV LNMLINIYIF VQYFKQLKYN NKVGLIYQND IYECLYVYMN ESNIFIQCQE YVSVFFNAIR KEKEKEKDQF DRQIDKQRK KQRLLKKANQ ILKRISKMNT KSFEVLIHSQ YAFDVCREQV YNFEDCRQTD TPLPKDPIHC KAQAKEVLSC Y KEAEKMDP ...String:
MSILNLIKNV LNMLINIYIF VQYFKQLKYN NKVGLIYQND IYECLYVYMN ESNIFIQCQE YVSVFFNAIR KEKEKEKDQF DRQIDKQRK KQRLLKKANQ ILKRISKMNT KSFEVLIHSQ YAFDVCREQV YNFEDCRQTD TPLPKDPIHC KAQAKEVLSC Y KEAEKMDP ICLSSFNDSR ECMFKSDGNL YNCKTWINQY VTCQKNPAAF AEFLEASTAE QLKSKKFDFV KNRGHSDKYL

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Macromolecule #9: NDUTT15

MacromoleculeName: NDUTT15 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 25.493336 KDa
SequenceString: QRGRDYTPSN KKYLQPWELE RKEYVELSLA IQSAYSCKML SEILKDNLYM LTDYQLSFAM FHLWNHEIPI DNYFYNVISP ILKEYITRF DRECNKSLAE IATFLGRMNV QDDAALWKVI ETKLVQERLY RYIPLNDLID LAHGMATANR GSQEFYNIVE N VIIKHRLR ...String:
QRGRDYTPSN KKYLQPWELE RKEYVELSLA IQSAYSCKML SEILKDNLYM LTDYQLSFAM FHLWNHEIPI DNYFYNVISP ILKEYITRF DRECNKSLAE IATFLGRMNV QDDAALWKVI ETKLVQERLY RYIPLNDLID LAHGMATANR GSQEFYNIVE N VIIKHRLR LIPDKIAVAK DCFTARKIGS PLLYQVLENP QAEAHELAGL KEHEQLKIS

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Macromolecule #10: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 26.545146 KDa
SequenceString: MELNSSAKED SHYVGVLGYP SQHDPHTLHP KKHDSTFTKV YACRDMLWDH HWEVRNTLYA GFKGALLGVA YASGFGLISK TVPSIVLKK MFRFVRNNNF GHIRIMQDLL TPYALTGFGL GSVYYLYQHN VWENRSNKWL AEVLSNALFF QVATAVCVNP G FHIYGMVG ...String:
MELNSSAKED SHYVGVLGYP SQHDPHTLHP KKHDSTFTKV YACRDMLWDH HWEVRNTLYA GFKGALLGVA YASGFGLISK TVPSIVLKK MFRFVRNNNF GHIRIMQDLL TPYALTGFGL GSVYYLYQHN VWENRSNKWL AEVLSNALFF QVATAVCVNP G FHIYGMVG GILFGTLKYA FYNSSFFQEK ESIGSYTTFG DLSEEERKKQ EYKDYIQFLG NYHKVRNGQL VDL

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Macromolecule #11: NADH dehydrogenase subunit 5

MacromoleculeName: NADH dehydrogenase subunit 5 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 88.179844 KDa
SequenceString: MIRNLIKNYF DFSFKKQNLN FDKYNYYNII NIFKHLNFNS ILFLLFFIVN LYWFNSGLIF FNSVYKIHHD AWTLIFQTDS ILNKLKIYF FLLPLYISSF IHSISTWYYN YILNFLLFSE NLNTNTNFVD YITYNTLLLS KFEDFNLFVY IKTLLITFDI R QINLDFLN ...String:
MIRNLIKNYF DFSFKKQNLN FDKYNYYNII NIFKHLNFNS ILFLLFFIVN LYWFNSGLIF FNSVYKIHHD AWTLIFQTDS ILNKLKIYF FLLPLYISSF IHSISTWYYN YILNFLLFSE NLNTNTNFVD YITYNTLLLS KFEDFNLFVY IKTLLITFDI R QINLDFLN EYPIILLTGL LFLFTTIFSL ICLSYLGLYG VFILNLASIL LFWLSMLYYF NLIVSENYYY YISLGKWMYL SN GFRVSFD LLIDLTSISF SFLTLTIGVF VYIYTFSYFR YEPLVERLIL FLNSFMISMI LLVSSGNFIV LFLGWELIGL TSF FLINFW STRVGTLKAA FKAFSFNKLS DLFLFFAILI IFSTTYNLDI LSFNNQIYLY ESYNIDMFYW SINLIEIISF FFIS CAFIK SAQFGAHIWL PDSMEAPVPA SALIHSATLV SAGIYLLLRL SPLFELSKYA YFILPLIGSV TAFYGGLVSA FQSDT KKTL AYSTISHCGF LMVSYSTGVL EFVILYLYVH GFFKAATFLC VGNVNRFNRN IQDFKRMGGF YKYLPFECLA SFVCMI NLS GLPLTLGFYI KHLLFIGLVE SYTLYPLIFS SLILGAIAGV FYSYRLFYSI FFDTKKGKKA IYLQASRIIL NSKFYSN TS LASNLSITFL VLISYTVILY LYCTTLNNYY SLSDLKSIYI NNAYSYFYKP DYNFLNAVSI LNWFVIILLI SVIYLNWR W SYYYTKSIDS LSKFILFSFF FFIFSKYIL

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Macromolecule #12: NADH-ubiquinone oxidoreductase 75 kDa subunit

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 80.580789 KDa
SequenceString: MMKVLQKYGK QFYGLTHIQK KQFRSTQVLN KQIEIFIDGK PAKVDDSYTI FQACYENGVI VPRFCYHERL SVAGNCRMCL VEVENVPKP VAACASQVVP GMKIKTKSEK TRIHRGNVME FLLANHPLDC PICDQGGECD LQDISSVYGY GISRYNEYKR A VEDKNYGP ...String:
MMKVLQKYGK QFYGLTHIQK KQFRSTQVLN KQIEIFIDGK PAKVDDSYTI FQACYENGVI VPRFCYHERL SVAGNCRMCL VEVENVPKP VAACASQVVP GMKIKTKSEK TRIHRGNVME FLLANHPLDC PICDQGGECD LQDISSVYGY GISRYNEYKR A VEDKNYGP LVATSMNRCI HCTRCVRFAT QIAGVEDLGK TGRGKAAEIG TYVEKTFNTE LSGNVVDVCP VGALTNAPYA FT SRPWELK SFYTSDVFDT LGSAIQVDTR GPEIMRVLPR IHEEINEEWI SDKTRHAFDG LKRQRINSPM KRSKDGNYED IFW EEAIQT ISKKCLNTPS DQIGAIIGEF ADIESITALK DFLNRLDVDN FEVRQHGNLK VSPDFRANYL MNSKITGVED ADVL LLVGC NPRYEAPVLN ARILKSTRKN LKVFNIGTNQ DLNYKNVHLG NSTKVLKEIA DGTHPFAERL KKAKLPMIMV GASAL ERED GAELYNTLKV ISNKTGVISE EKSWNGFNIL HKEMGRINAL ELGINPTSVN KNAKLVFILG ADNNLRPEDI PADAFV VYF GTHGDEGAYY ADIILPTAAY TEKNATWVNT EGRVQQGRLV VMPPGDARED WQIIRALSEE AGVPLPYDSL EELRYRV AE LAPHLLKYDY IEPTIFGKVA LSAQQGVKTT LSPTPITDYI DNFYMTDAIS RASVTMAKCS TAFNHEKFSN FKNLAK

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 58.690043 KDa
SequenceString: MFNLNTIYLS RIFIEFNFYF LFFLFLISSI IFYFSKIISI QNLNQNSVFN FLKLANIFGI LISFFIHIIS FWFYCIYSYN LSLNIFSDI NLYNSNSIEL LNNSLLPNYF KSNITIDFFG LILLTLAYIV GFVSILALDT RLYWKNIKYI FSFTIFLLIV Y VYVTVSNI ...String:
MFNLNTIYLS RIFIEFNFYF LFFLFLISSI IFYFSKIISI QNLNQNSVFN FLKLANIFGI LISFFIHIIS FWFYCIYSYN LSLNIFSDI NLYNSNSIEL LNNSLLPNYF KSNITIDFFG LILLTLAYIV GFVSILALDT RLYWKNIKYI FSFTIFLLIV Y VYVTVSNI LLFFMCYELL LIPSFLIVYF VSPSRRAIQA SLYFVIWTQL GSLLVLIAIS YIISITNTYE FNDLKYFNFT NS ESTIIIF LIFLGFGFKA PIWPFHYWLT KTHVEAPSGF SIYLSGFLVK TALYGFYKFN TSIFIDIDSS IFIAICIMGV VDS SLKMWG QTDLKKLVAY GTIQEMNIIY LAFCWGDSCA ILGGILFSAT HAFLSALMFF LVDCIYRRYH TRSLVEVNGI LHIT PNLGL SILFMLVFFS GIPGTIKFIS EFYIFSGLLE ASPFICFILM LVANVLGLIG FSKSWFNATF GMPKKNTKYL PMDLS FKES YIILYCFFFL FIFSYFSSIF F

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Macromolecule #14: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 52.313699 KDa
SequenceString: MLSKIFKTTV IANKKFLNSK NLSMVISYNR SYGNLKDQDR IFTNLYRDGD PFVKGALKRG DWHQTKEILS NGPEWIIDEI KKSGLRGRG GAGFLSGLKY SFMPKVNPDG RPSYLVINSD ESEPGTCKDR EILRNDPHKL VEGALVVGFS MRARAAYIYI R GEFWVEAN ...String:
MLSKIFKTTV IANKKFLNSK NLSMVISYNR SYGNLKDQDR IFTNLYRDGD PFVKGALKRG DWHQTKEILS NGPEWIIDEI KKSGLRGRG GAGFLSGLKY SFMPKVNPDG RPSYLVINSD ESEPGTCKDR EILRNDPHKL VEGALVVGFS MRARAAYIYI R GEFWVEAN ILQQAIDEAY AKGFIGKNAC GSGYDFDVYI HRGAGAYICG EETGLIESIE GKAGQPRVKP PFPANAGLYG CP TTVTNVE TVAVCPTIMR RGASWFASFG RPNNAGTKLY CISGHVNNPC TVEEEMSIPL RELLEKHCGG VRGGWDNLLA VIP GGSSVP MMPKNVCDDV LMDFDALKAV GSGLGTAAVI VMDKSTDPID AILRLSKFYK HESCGQCTPC REGTGWIVDV MERL LVGNA DYAEIDMLQQ VTQQIEMHTI CALGDAAAWP VQGLIKNFRE EIEDRIDSYH AKHPQLKKSR KSNPQIGHH

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Macromolecule #15: NADH dehydrogenase subunit 7

MacromoleculeName: NADH dehydrogenase subunit 7 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 51.227477 KDa
SequenceString: MNRSIFQLWK PESPRSNVNS KQIKTMNVNF GPQHPAAHGV LRLILQLNGE IAERFDPHIG LLHRGSEKLI EDRPYLQGMP YFDRFDYVS MMVQEHAYCL GIESLLGTTN YSATFTQIRT MYDELTRILN HLLAVACHAL DVGSMSSVFW AFEEREKLME F YERVCGAR ...String:
MNRSIFQLWK PESPRSNVNS KQIKTMNVNF GPQHPAAHGV LRLILQLNGE IAERFDPHIG LLHRGSEKLI EDRPYLQGMP YFDRFDYVS MMVQEHAYCL GIESLLGTTN YSATFTQIRT MYDELTRILN HLLAVACHAL DVGSMSSVFW AFEEREKLME F YERVCGAR MHAAFYRPNE VNLNAVSSFL MEDILEFSRN FFTTLNEMHN VLTYNKIWKQ RLINIGTYSF QTCLDYGLTG VM ARSCGLK RDLRLSKTET YANYYYLNFR SYTGQHGDCY DRFLIRMNEM CESLNIVNQS INKISKFNNI VSINTKKNIL NKE NFNRQT TVLPHLVLSY LNKNDYNLKN TKNDYNSMEE LITHFKYWSK GLKVESGYTY QSVESPKGEF GVSMLSDGSN KPYK CKVRS PALHHLQVLP KIGKGHFLAD LVALVGTVDI VFGEIDR

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Macromolecule #16: Ymf65

MacromoleculeName: Ymf65 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 43.14616 KDa
SequenceString: MLLRLLVSEY IFFLPVFTNL FIYWHIFFKN NINLVNKKNN WDKSISVKNI IIKQNPSFII RLNLLLNSLM VLYLITFNGY SSTFWWSHF KLNNYSLYMY LLVIIFNNYF LYITEKHIKI LNNYSIDYFF SIINITLFIP MIFLSNTLFT FFFLIELVSC A IFYKFIVS ...String:
MLLRLLVSEY IFFLPVFTNL FIYWHIFFKN NINLVNKKNN WDKSISVKNI IIKQNPSFII RLNLLLNSLM VLYLITFNGY SSTFWWSHF KLNNYSLYMY LLVIIFNNYF LYITEKHIKI LNNYSIDYFF SIINITLFIP MIFLSNTLFT FFFLIELVSC A IFYKFIVS KISFKNSNYK DNYFSIFSKN YLNVLFYQYW SSFFSSVMIV FCIIYLFSLT GSTEWSIINF IVASNNQINY YT NNITLLF ICLTLIIGFI IKLGIAPIQL YKIEIYKGLP FLSIFFYTTF YFLIFFLFFS LLFIYYLSAL NNFFWIILLI ISI IGIFYI ISIIFDINLF KAFLAYSTII NSISFILLII AIIF

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Macromolecule #17: Transcription factor apfi protein, putative

MacromoleculeName: Transcription factor apfi protein, putative / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 39.793414 KDa
SequenceString: MLRLRLFDAY EKISMTFLGP LYRRIGKSLA QTGLNIQQPY TSDDRLVPSL RNIRVTNKIP SINDSEFIAP NSVVIGDVIT KEGSSIWYG ATLRGELGPI EIGKQTVIQD LVNIQSGKQN QKTQIGDNVF IGPNSYIQSS KINDNSFVGM GSTVSTGCNL A SNAVVAAG ...String:
MLRLRLFDAY EKISMTFLGP LYRRIGKSLA QTGLNIQQPY TSDDRLVPSL RNIRVTNKIP SINDSEFIAP NSVVIGDVIT KEGSSIWYG ATLRGELGPI EIGKQTVIQD LVNIQSGKQN QKTQIGDNVF IGPNSYIQSS KINDNSFVGM GSTVSTGCNL A SNAVVAAG SVVPENTQVP SNQIWAGSPA QYLRDITPEE RQVLQEHHQE CVQLARIHAE ETEKSFREVL NDFDRITAEA EY DHESLAL QKMRDLGFPM EGEEEEYIEQ RVFMREQLPP LESEFWKKNY DPYEQDLFHF PDSFKAYQQQ YKRYDEAKKY FEE NPNVEA TIIDREFKEP TNKKPWTRKY

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Macromolecule #18: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 32.63677 KDa
SequenceString: MGFWIAPLFV NILSLPLYLV MLVYNIVCML LITLVIASIT LIERKVLSLV QRRVGPHYVG YRGRLQYIAD ALKLFIKGIV VPEGSNKFW FVAIPSAAGA ICYTFWINSM WGPSVSIFDL EYNLVYATIL SILFSFCIML TGYFSKSKYA FMASIRCAIL M LNIEIFLG ...String:
MGFWIAPLFV NILSLPLYLV MLVYNIVCML LITLVIASIT LIERKVLSLV QRRVGPHYVG YRGRLQYIAD ALKLFIKGIV VPEGSNKFW FVAIPSAAGA ICYTFWINSM WGPSVSIFDL EYNLVYATIL SILFSFCIML TGYFSKSKYA FMASIRCAIL M LNIEIFLG LLVINLIFIS ESFCFSVFVI YQEIIWLIFI FFGVSGLIFI TFLLETNRAP FDLAEAESEL VTGYSVEYGG FY FALYYLG EYFHLFFFSM VISIVLFGGW ELPNFLYLFL LNDFNIL

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Macromolecule #19: NADH-ubiquinone oxidoreductase 24 kDa subunit

MacromoleculeName: NADH-ubiquinone oxidoreductase 24 kDa subunit / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 31.216697 KDa
SequenceString: MLSKGFKQLF GLTKATNFYN KNFFSRLAAH RKNDDNSDSV PFEFTPENYK EIEKILAKYP LKQKRSAVMP LLYLVQEQNN NWVPLSAMK KIAKLLEMPE IDVYEVATFY TMYNREPVGK FHLQICGTTP CQLCGSREIT KAIEEYTQTK LGHTSADGKW T LEEVECLG ...String:
MLSKGFKQLF GLTKATNFYN KNFFSRLAAH RKNDDNSDSV PFEFTPENYK EIEKILAKYP LKQKRSAVMP LLYLVQEQNN NWVPLSAMK KIAKLLEMPE IDVYEVATFY TMYNREPVGK FHLQICGTTP CQLCGSREIT KAIEEYTQTK LGHTSADGKW T LEEVECLG ACSNAPMIQV NNKWVYEDLT TENVVKLLKD LESGTDKKGP QNHRNQVEGP LGRSTLKEKD FLSGEIRFSR DF AKAKQDW VAQKEQERIE AEKKKAATAA AAAAAKK

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Macromolecule #20: Ymf62

MacromoleculeName: Ymf62 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 30.448471 KDa
SequenceString: MFLITITSYF SNIIEFNSYI INLIDFITPL FFIENFVIQF FILYLFYLLI VNNNLYYILL YIFLEIVFFG LFLCLYQLEL FTGFLWVAE FAIVFIAVVL LFYLNIDGLH LKYNHNINNV LYYTPSLVLF LIFFNIDYFS ELELFLPLEL SFIDIYDDYY E GFNNSIMN ...String:
MFLITITSYF SNIIEFNSYI INLIDFITPL FFIENFVIQF FILYLFYLLI VNNNLYYILL YIFLEIVFFG LFLCLYQLEL FTGFLWVAE FAIVFIAVVL LFYLNIDGLH LKYNHNINNV LYYTPSLVLF LIFFNIDYFS ELELFLPLEL SFIDIYDDYY E GFNNSIMN DFTPLTLSYY SINSAEFIII GLLLLLGSVA CVNLYKSNKN YTIVKQSNLL TMFDFFKDFI NFSFIRKQDL NN QTNFNPS LRSIKKKY

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Macromolecule #21: Gamma-carbonic anhydrase

MacromoleculeName: Gamma-carbonic anhydrase / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 28.216734 KDa
SequenceString: MKLFRALTKS GLIQKIRQAT GSEISTATKY GENISKHRSL MSLYDLHPQI GYQSYIAPNS TVIGEVTIGN ETTVWYNSVI RGDVNAVQI GNNVSIGENV VIHTAGSLPT GQPASVDIGH YVIIGSKSTI YSCTIQDEVV IGQGCVILEG ARIEKGAMIA A NSVVPPGR ...String:
MKLFRALTKS GLIQKIRQAT GSEISTATKY GENISKHRSL MSLYDLHPQI GYQSYIAPNS TVIGEVTIGN ETTVWYNSVI RGDVNAVQI GNNVSIGENV VIHTAGSLPT GQPASVDIGH YVIIGSKSTI YSCTIQDEVV IGQGCVILEG ARIEKGAMIA A NSVVPPGR LIPAGTLWAG NPCTFVRNLT KSELATNIDH AKKQLHLAQQ HRYEYLPYNS AYLQKSNSEE DLNPTKYDDV TI NYNFGDE ERAQENPLKY

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Macromolecule #22: NADH-ubiquinone oxidoreductase 1, chain, putative

MacromoleculeName: NADH-ubiquinone oxidoreductase 1, chain, putative / type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 28.053535 KDa
SequenceString: MKICLNRNNQ IIFYWYNLGY IQRSNIHEEA PNTSVEAKHH NKTFYDPILD IDEDLKDDIR LYGRDKPDEL DFTDVWESSY QNIICPEYF YHFWFCGIVY SFEPEWTINY PFEKGPLSPL FRGEHALRRY PTGEERCIAC KLCQSACPAR AITIETEPRP D GSRRTVRY ...String:
MKICLNRNNQ IIFYWYNLGY IQRSNIHEEA PNTSVEAKHH NKTFYDPILD IDEDLKDDIR LYGRDKPDEL DFTDVWESSY QNIICPEYF YHFWFCGIVY SFEPEWTINY PFEKGPLSPL FRGEHALRRY PTGEERCIAC KLCQSACPAR AITIETEPRP D GSRRTVRY DIDMTKCIYC GFCQEACPVD AIVEGPNYEQ TAYLHEDLFY DKYKLLENGD KWEPQIARNI EYLINQPL

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Macromolecule #23: Gamma-carbonic anhydrase

MacromoleculeName: Gamma-carbonic anhydrase / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 25.395969 KDa
SequenceString: MKLFQAMWTR TIYSIGRMVR ETGLALDRYG CKLEQDISCY EPLSRHRNIL PIYDLVPTFY HSTFIAPNSS LIGAVYLGQN TVVGYGSTL RGDNHAIRVG HNTVIGDKVA ISNVATLAAG IPVSTNIGNH VNIGAGCVLQ SCVVDDNVTV GHNTVILEGS V LERGSVIA ...String:
MKLFQAMWTR TIYSIGRMVR ETGLALDRYG CKLEQDISCY EPLSRHRNIL PIYDLVPTFY HSTFIAPNSS LIGAVYLGQN TVVGYGSTL RGDNHAIRVG HNTVIGDKVA ISNVATLAAG IPVSTNIGNH VNIGAGCVLQ SCVVDDNVTV GHNTVILEGS V LERGSVIA PNSLVPAGRL IPSGQLWAGS PVRYVRDLKE EEIKLNLEQT EQNLSIGKTH KSSLIQQEAY DRLLA

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Macromolecule #24: ETC complex I subunit motif protein

MacromoleculeName: ETC complex I subunit motif protein / type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 24.277859 KDa
SequenceString: MLQRGLAKFL LRNTRQTFGV VRNGFSSTQI EKAAEKSDEV PIHLRPYNKE KYEVPSTKLK YSTGYALLDV EPMPRAKIMK ISYNILHKL KEIPETAMYR IYTEEKVKYI MKLTDEIEDV RQLEEEFGQD SIELFIYSYG KELELVEYMK HSKPWESRPG D EEQNEMIR ...String:
MLQRGLAKFL LRNTRQTFGV VRNGFSSTQI EKAAEKSDEV PIHLRPYNKE KYEVPSTKLK YSTGYALLDV EPMPRAKIMK ISYNILHKL KEIPETAMYR IYTEEKVKYI MKLTDEIEDV RQLEEEFGQD SIELFIYSYG KELELVEYMK HSKPWESRPG D EEQNEMIR IASQKRVYLK HQRVDRPARQ EAAFISSNAK PQLEAGKQ

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Macromolecule #25: NADH dehydrogenase subunit 9

MacromoleculeName: NADH dehydrogenase subunit 9 / type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 23.830291 KDa
SequenceString: MQNKYMQPIQ LFIVFEKLNS KMWISKKLNS NHSIALIPSN WFYSINLFLK RELLFSNITL IENSAIDTIS YNLETNQNDL DKTNIENYF FKNKMLVFYN YYNYFLKSKL TLFIILNNLN KNIDSIDRIF ANANWLERET SEMYGINYKW KIDTRKLLLD Y SKIENPML ...String:
MQNKYMQPIQ LFIVFEKLNS KMWISKKLNS NHSIALIPSN WFYSINLFLK RELLFSNITL IENSAIDTIS YNLETNQNDL DKTNIENYF FKNKMLVFYN YYNYFLKSKL TLFIILNNLN KNIDSIDRIF ANANWLERET SEMYGINYKW KIDTRKLLLD Y SKIENPML KEFQSEGTQD AFYNIFENQV VVLKNETVEL

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Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 22.89057 KDa
SequenceString: MGLWSWTINQ MLTPKFWVHL RREGFIKTWT RGHKASRHAH YVGGNRTDGY TKQVGEDEFG NRYYEDFDVD HKNQRRWVEF SDYFMQMWS NGDKVPVGWH GWLSHQYDDF PTRTGNSAFV KHHYLKQHTA NLSNTPLNHV PQGAPQNLNR MRFITAQRDR S RAPWQSPK ...String:
MGLWSWTINQ MLTPKFWVHL RREGFIKTWT RGHKASRHAH YVGGNRTDGY TKQVGEDEFG NRYYEDFDVD HKNQRRWVEF SDYFMQMWS NGDKVPVGWH GWLSHQYDDF PTRTGNSAFV KHHYLKQHTA NLSNTPLNHV PQGAPQNLNR MRFITAQRDR S RAPWQSPK GEGVFQGKKL IVASNSPFID DMSIRD

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Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 22.698301 KDa
SequenceString:
MSKAYYFVKN FSWAEVSNLL CYGTKYPTVL NHQQKVTRLY RATLRRVYAH QVEGYKTDFK QYNENITDIG KDFNKMLALK PESLELQAY FKKYEDLQEE LFDPAMIIDE SRPYAASSGR YYIFDDYLLK FDPFGFYSPK LLSENRPEEA MPFYEDYPQN D SHWNLWEQ FPEDFEDSNA EREAILKSNK H

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Macromolecule #28: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 21.642377 KDa
SequenceString:
MLLPKNAIQS ARYFEIQKIP AKIAKTANEK ILSVGVAQKN NIQPKTVTAQ GQIGFVQHPQ LDSSCQYTQF YTPQRRDIRG RVARIYIQD TNHMHDTPQI PEGYKWTLEF ERQAQYKTPW MGWSFNGDTF SKRNHYFCTL EDAISYCKQM GFGYEVSFPR S RYHTRKSY ADNMLWPGHD NAVDEDC

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Macromolecule #29: NADH dehydrogenase, putative

MacromoleculeName: NADH dehydrogenase, putative / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 20.167854 KDa
SequenceString:
MNHYWGSSNT IPASSTQNNN YFSGGGNNVT IRGNEIMERL PSQTPSQNMV QASMKTLRFY RKFCRLIPFI LRIHNIGTKF TAQQAMINF GNYIRERNHY RDPGLIDHRI QLGYELLYEA EMHFSQHTIL MQYLSPYNTP LSDRGYSYLE KVKYGNKSKF L QGFYKGNK PTEF

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Macromolecule #30: NADH dehydrogenase subunit 10

MacromoleculeName: NADH dehydrogenase subunit 10 / type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 18.32426 KDa
SequenceString:
MRVDYIVTPI NAVVSWARQG SFWPLTFGLA CCAVEMMHAT VSRYDFDRFG VIFRATPRQA DLILVAGTLT NKMAPGLRRL YEQTLDPKW VLSMGSCANG GGYYHYSYSV VRGCNRIIPV DIYVPGCPPT AEALMFGVLQ LQKSLYRQIN EGEKKYNKKD L TY

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Macromolecule #31: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit

MacromoleculeName: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 17.381809 KDa
SequenceString:
MSQTFAHDSF LGGLNLFKRR DPRFVLDQGE RPPYPIINSN SSFVDVLSNF NKADFGLVLF SAAIGFPLSR WVLKGLTFSS LNYRRGLFS SVYGGVILWG LVLGFNNSYY RLNGFVDNGL VWKRKERKLN KYDFTSEFED NSFFKKLRIR D

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Macromolecule #32: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 16.249438 KDa
SequenceString:
MLRQVLRFSK QLVLSAPKLQ FRPVYFFQDN QDRSRVETNS ATWAHNLPKE NKFNTETLEK QEVESRILKV LSNFEQVNLK NLRWEQNFK KLGLDSLDQT ALLASIEHEF TILFPDGVFE GFENLEQVVN YILKNINAV

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Macromolecule #33: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.428433 KDa
SequenceString:
MFGLTKNLLK FAQQANKMNS ILNKTNTLQW ASVYNYAPQK VVLRNEKSGY YANPDDVARR LIRLISLHDK VQNPSAITLK STWSEIGVD PLSYVEIMLE AENEFYIELA DEDLERFRTV EDAVEFIARN FFTN

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Macromolecule #34: NADH-ubiquinone oxidoreductase chain 3

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 3 / type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 14.416898 KDa
SequenceString:
MGDAVVIHLI QNVLIFGIIF WLLTWGAEYF YTVKQQLTKK QFYECGFKSI SELNIQINFN FFMLAVFLIL YDVEFTFLFP VLFNFSMFS TTELFLAFFF IFLILVSLLY DWLNNVLSWS AE

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Macromolecule #35: Ymf58

MacromoleculeName: Ymf58 / type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 13.509949 KDa
SequenceString:
MLTWISFWSL IFWLILIILV LKPKNFISIL FMSELTWLAL YCLSLLFGAI YCDITLLSIS FFILGVAGLE FSFGILIAIL YKNLNESLN TDLNNNNNNQ NIFDKNFKTP LEKINWQ

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Macromolecule #36: Ribosomal protein L51/S25/CI-B8 domain protein

MacromoleculeName: Ribosomal protein L51/S25/CI-B8 domain protein / type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 12.157782 KDa
SequenceString:
MSSWQKLIGT NLRELRFVFC QNSQRSLGLR NYIAKNYWNL KNQNPNFPLI VRECEEADPY IIARYQYGVE KKAFAANNNE AEIENIIKT LVEQSNKVNN QMQK

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Macromolecule #37: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 11.451183 KDa
SequenceString:
MVNTAYPTPL KTILKTTPAF VVYFVFGLGF STVIYDVVYH PKDRIERFYF RSSKFERLSR KRDEKLRHYF KPAIEWQPWY NTSTNNNTR PLLRY

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Macromolecule #38: ATP synthase subunit e, mitochondrial

MacromoleculeName: ATP synthase subunit e, mitochondrial / type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 11.283534 KDa
SequenceString:
MVYQGFKVLR RNPTFYNPRS AGMVALSYFA YSYYVNKYYK PQNSNFEEYN SSHPHNHDEK VRQYHEKTNQ AIRDAVLEKR AEHDQRLRE EAKL

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Macromolecule #39: GRAM domain protein

MacromoleculeName: GRAM domain protein / type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 10.920431 KDa
SequenceString:
MSYSGYSLNG GVHPCLPFYE RMLQCAKSEA LPIKMCTAQT EDYLECHHRK KQYALNYAIK KELNNIRIVA LPRYDEENDT FVPFSQATA DHIFQ

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Macromolecule #40: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 9.942366 KDa
SequenceString:
MNSPQKVAQG AGRKLFKHYI NENIKSNNEQ KLFFYRVNRW RWNTKDNTTA PKFLRLKYPL LVTGVCLFAY DWTYGFTQVD AHH

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Macromolecule #41: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 8.787116 KDa
SequenceString:
MNLPWFVRWG TDVALFFIPA YTFANYPTTF FVFAAEKRRQ RRRKDFSDVK LRDDAAFSVD QVKQLQTKLH LKQ

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Macromolecule #42: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 8.445937 KDa
SequenceString:
MDKYIQQAKC AYNFSLKAVR FVGPLNIVFA GVAFLMFYEN NYKKLYLNPR YSYTMPYLQS AKITKNLYEK L

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Macromolecule #43: ND1b

MacromoleculeName: ND1b / type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 7.238754 KDa
SequenceString:
MPYFVLLFKI LIFCVVAIAT RGTLPRYRFD QFTQLNWKHF IYIWLGFLVF NLCFVTFFI

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Macromolecule #44: Transmembrane protein

MacromoleculeName: Transmembrane protein / type: protein_or_peptide / ID: 44 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 24.823297 KDa
SequenceString: MGGDHHHEDS HHKSNVDQHE LKAEMIKELS HYYDHHDLSL FGKVQHFVEH LLEEKHHAKI NTSNFDQKKL ENFSESKQIS RTVFALKKI KTFNHDFFTS EEEMILEPLP LGILTYGLKY AFAGVDAALL TYFWRNWNFN VRTIGLLGGL VGIQMATLHI P NLVNEVVI ...String:
MGGDHHHEDS HHKSNVDQHE LKAEMIKELS HYYDHHDLSL FGKVQHFVEH LLEEKHHAKI NTSNFDQKKL ENFSESKQIS RTVFALKKI KTFNHDFFTS EEEMILEPLP LGILTYGLKY AFAGVDAALL TYFWRNWNFN VRTIGLLGGL VGIQMATLHI P NLVNEVVI QTPRRRALAK KYISAYGPQF FHDIVNPKYD IEHLRHLQNK LNPY

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Macromolecule #45: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 45 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 24.41915 KDa
SequenceString: MNPRNIFNLA KKVQNFNSIT QKAFKRFGGA AAHHDDHHDD HHGHGGHGYE VHLVKDKNLI GNKSFKDDLV AVYGFTDVND HHHHDETDP YHHLRGVPTL SFERMYFADA YYHDDTHEGL MNEPHGYLTM DDPMDLRPNY EKSALELLFL VSGGAILALM L GYQGLNLA ...String:
MNPRNIFNLA KKVQNFNSIT QKAFKRFGGA AAHHDDHHDD HHGHGGHGYE VHLVKDKNLI GNKSFKDDLV AVYGFTDVND HHHHDETDP YHHLRGVPTL SFERMYFADA YYHDDTHEGL MNEPHGYLTM DDPMDLRPNY EKSALELLFL VSGGAILALM L GYQGLNLA NPAESLFSLN TAAEEIEDKI RQIRIDNDKL LQRKAQLEEE LASLNN

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Macromolecule #46: NDUB8

MacromoleculeName: NDUB8 / type: protein_or_peptide / ID: 46 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 24.150469 KDa
SequenceString: MALRRVLKNQ FNLIHKGQAQ AVRGGHGWDR PDVPLSFNPL YVHKRELSIF DTNMWMYDQV YPEYVISYNE IHLVDQWKGL KESFSQSAY WWAMMAMVFG FYFINTTPRQ LGIDTNDLKG FLGEYYGQYK KRSGIRSNFL GLDVTGENSI IQPNYDRKNG I RDVIDSLN ...String:
MALRRVLKNQ FNLIHKGQAQ AVRGGHGWDR PDVPLSFNPL YVHKRELSIF DTNMWMYDQV YPEYVISYNE IHLVDQWKGL KESFSQSAY WWAMMAMVFG FYFINTTPRQ LGIDTNDLKG FLGEYYGQYK KRSGIRSNFL GLDVTGENSI IQPNYDRKNG I RDVIDSLN ADAGKRKLIN LEAKNFIERV EKECEQRILK KGGATQSHH

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Macromolecule #47: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 47 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 23.971033 KDa
SequenceString: MFLYKKILSI YKQSFSFFLS FNFSFFLYAL LAIFLLINFC QHIHKFLYYC KEKIQKEMQN AYPEITDQHR EFLKKQGLKV YEPKPLPDQ INPFSKTYWI TNAFIIGVSF LARRHALKVG APRIFWSGCI VGVPLAAIIS RGKSDQLDEL VGARKTLEQK L EYAPITRR ...String:
MFLYKKILSI YKQSFSFFLS FNFSFFLYAL LAIFLLINFC QHIHKFLYYC KEKIQKEMQN AYPEITDQHR EFLKKQGLKV YEPKPLPDQ INPFSKTYWI TNAFIIGVSF LARRHALKVG APRIFWSGCI VGVPLAAIIS RGKSDQLDEL VGARKTLEQK L EYAPITRR AWERALATNQ EYQNEIKTQI QDLQAEIAAK KVAAKLE

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Macromolecule #48: NDUPH2

MacromoleculeName: NDUPH2 / type: protein_or_peptide / ID: 48 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 22.446637 KDa
SequenceString:
MFNILKGAQL SFRSITNKSV NNYYNIMRQV SLDSNPIVLY QSSTFTGNGL QEFYENADAL TKYLKLVPFF LEKNLYDHPK QFVIKMEFH PQNKVLSLDC LTHQGVLKKT VNLENLIPVP YEDYVQFCRR KLFNAPLFLD TEMIYFNTFQ NEFYVFDKNA K WNEEGINH PELDISKLYN EKAWFDSLRI I

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Macromolecule #49: NDUB10

MacromoleculeName: NDUB10 / type: protein_or_peptide / ID: 49 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 22.167137 KDa
SequenceString:
MAFGGFRQTD NSLIIDDRRK IILNTRSLND FQQKIYLRNF FTNYRPDLSS YDYFAFKEKL RIGELFLNEY RKRINNEVRR AAILTPTSS LREKMNHKIA DQILDLSSPH VRGAHFQAVR SWTDASKIVN YVEEKQTKIN KYGLQFPLLG NMTEEQCASK E DEVYQRLL KEMQKPPKKA SEPVEESSDE

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Macromolecule #50: NDUA13

MacromoleculeName: NDUA13 / type: protein_or_peptide / ID: 50 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 21.045617 KDa
SequenceString:
MQFFRPDFIA TQVLRRADMA HSPFHKAIHD LEDKRSKLFP DRRRIPGRKA KLLLAASLLL QMWGVGKIIE IKKFMKRRDI ELKGLQRKA APFMQSMNDV RHLALRERND MLYNELLSVH GEEYAQKMQK RFHQTDIWAP FRHRYAYMYN SSNKNVKDYK Q VTLSRYIN GFDKFNV

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Macromolecule #51: NADH dehydrogenase subunit 2

MacromoleculeName: NADH dehydrogenase subunit 2 / type: protein_or_peptide / ID: 51 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 20.899889 KDa
SequenceString:
MSIFSNIWIN NDLNSYGLSI LLLNIINYLI VFMLILSVIL LTNLSKFKSL NQFKEFNSYN FILYSLIFSL LSMAGIPPLL GFTGKFLAI LYSSFKSQYL LILFMTILNI FGMYFYIQNL RFVVKKNKSS ILNYKNYYVN INYSITLNII LLNFFNFFGI L FLSDLIII LNYISSYIYI

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Macromolecule #52: 2 iron, 2 sulfur cluster-binding protein

MacromoleculeName: 2 iron, 2 sulfur cluster-binding protein / type: protein_or_peptide / ID: 52 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 19.564221 KDa
SequenceString:
MQGLLSKFAK FSNKQLTNSI RRFAGNHHHH AGDQADRVAD KIIWINIQNR IGQFERISAF EGESLLEALQ RNKVAGIVAT CEGGEDINT MLEKPIDPVT YGPFCSSCQV VVSNPWRNKM GNLHYLEERN LVRSSYPTTE NSRLACCILV EKWMNEMIIS I PQNPNSVY EDNM

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Macromolecule #53: Thioredoxin

MacromoleculeName: Thioredoxin / type: protein_or_peptide / ID: 53 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 19.540191 KDa
SequenceString:
MINISKSASK VLKLNQALNA QFSRVRSFND FKAAKTYIDT LKPKLACLYF RADWNPLCEQ ADKDFDKLSD THLEYEFVKI DIDKAPQAK GYFAVRCEPE FLLLCLGQEM TRQTGQNQRN LEHRLFKVQE YVKGLNFPAG MDTYEEFHEQ YMAEHTQLDK E INEWAR

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Macromolecule #54: COX assembly mitochondrial protein

MacromoleculeName: COX assembly mitochondrial protein / type: protein_or_peptide / ID: 54 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 17.078342 KDa
SequenceString:
MKSQEKIFIK KIQSLAQSNY LIKSNQLKRY QIEVKMEFSN ALLSQTKLPG QQYDYKRCFQ ASNTHFECLD SIRDAYDNHH KCPQTYQAW QSSCDVGIRR YQMDNREQQK KDQLLYSKEQ LKNYNAAKNK EAYGITAPKN LSFAF

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Macromolecule #55: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 55 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 16.909242 KDa
SequenceString:
MTNFGSPFRN TDSGIVIRDP ENEKRLKLAF QNFWKSKQED KEFQAQIKTA VSKDTVNFMF YASPLFGALL GKTYIDMFCN PRYFYFRAF TLSMFALAGY CVGNGFRNRY EHSLYTRNYH LFPKDLQDAL VNGDARYCIS WWKQ

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Macromolecule #56: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 56 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.831701 KDa
SequenceString:
MSNNNQGDFF VDKYNFSRRV VDHRQPYDLN FSINNPVGSR VWFKAWKQKA IGNFLNLVGV HYAFYGAGFC LLFVLADAWG REKYAQPYK SQILHGRQPF GHTFVQNYRN QATDLGRWNH NFACYEKQPG CGRDFD

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Macromolecule #57: PH domain-containing protein

MacromoleculeName: PH domain-containing protein / type: protein_or_peptide / ID: 57 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.785234 KDa
SequenceString:
MTHQFENVLL SNRKNLTPQE SVQKVINYAL LQDAKQRSRT LRHIKASWVI PALLFTYPAW YLAKGAVNGV WSNIHPTDKV TLSFANIGR PFRLIYRPEI FLRDQQAKFI QLEKEHIEKS KKGEFVETTS PLVLWN

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Macromolecule #58: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 58 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.689792 KDa
SequenceString:
MFLNPVKDSE FDDEVKGFVP SEGEVRFVAN KNKECGYYLQ GIEQCRRKMV QLAGDSSSQF HSLGFLPCKR LVDAHYRCMT DDKFGSTIE EVPEIGLDSA QKFFDCTFQQ LKPMQSCRRF FDQVVRDVYR ANGSQLI

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Macromolecule #59: NDUB6

MacromoleculeName: NDUB6 / type: protein_or_peptide / ID: 59 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.444344 KDa
SequenceString:
MLLIEMAFNA MKMKIFSLRK IKVKSKEQYL YNYQQKLLIL GQGKEKNNKQ YKKDIEMGGF QKYPIPRYLH VGQWIVNKNW KWNTFHMFF PTAILCFMVW RNSMISTAKP PNYGEYVDPQ SPVAPKAIKY

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Macromolecule #60: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
type: protein_or_peptide / ID: 60 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.193583 KDa
SequenceString:
MLARTLKNYM RVQQNLRFSR ANIEKSPAPP TIGQVELEPF KFNHERDQLI YGYTMEELYG KKFGLKHSAT VLREIKKDTI MMILFIIGG FTYCYHMRET RFQLDDDFNE YVNTNKQTFR PIPDHVKL

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Macromolecule #61: Zinc-finger protein

MacromoleculeName: Zinc-finger protein / type: protein_or_peptide / ID: 61 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 15.141296 KDa
SequenceString:
MIAQGLKRLS LLKNLKKSAQ LYYFNKQAFG SDVDKNLNPY SYEALKENHW LVSDSSKKNS EWTHKSNAEQ LIAKVPIIYV DSNIVRCIG GTEINAGHPQ VYIQLDTRKH GTPQTCKYCG LRYAKKMDGH HHH

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Macromolecule #62: NDUB4

MacromoleculeName: NDUB4 / type: protein_or_peptide / ID: 62 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 14.410395 KDa
SequenceString:
MSLRKGTSIF SRQFKKAFND AKYQNLTAAQ GETYSHLGWI SNVDLRLGRA IFTFGVVGIA FCIYLEPSYF HETFGHMSQP PKYDLIDSN INGVEKKLNK QILHREHNEH KLDGFVSMFK GSDVAKN

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Macromolecule #63: NDUB15

MacromoleculeName: NDUB15 / type: protein_or_peptide / ID: 63 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 14.963529 KDa
SequenceString:
NYHYDFCGRA YMGNPAVQSP PKEFFNYHYV PDNYPDALSG FRIAYRDPFE VQHVFAYENW EYQYDGQWWS MGSLACNVLF FCTPLFLYL ILQVEELNSE KRGGTSNKFY HNNAGFFHFQ IYDNKQ

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Macromolecule #64: NDUTT16

MacromoleculeName: NDUTT16 / type: protein_or_peptide / ID: 64 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 15.334371 KDa
SequenceString:
ASQLQREQKL VQSLQQESLQ PHLFKIIVDS QSDLVCEADR REYIKHYTRA NEKSSTSQLL QVGALLGYIY AVGRYVSNPS TRKFSYGLA ALLGSFSLLN PSKNLHHNHS LREIYSKYNI STNPQALEIL KSRIY

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Macromolecule #65: NDUTT17

MacromoleculeName: NDUTT17 / type: protein_or_peptide / ID: 65 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 13.983049 KDa
SequenceString:
MNISYTGLKL EDYSDEVIRK YKFPNSNELE RFLNREQTLT VQQHKSAIKL AQQDFFAVAG LLSVGSLSYI FYNSVGGKVI RDRIRASRT KAQKVIVLAL AFVANAAALI IARNAITAHN FGWQAA

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Macromolecule #66: CHCH domain-containing protein

MacromoleculeName: CHCH domain-containing protein / type: protein_or_peptide / ID: 66 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 13.747362 KDa
SequenceString:
MGGHGAWNEN QQHYKYSKEE IEAYQVPMRI KAGPCVDTYI PLKKCFQENP TSFAAKMLDG RKGKCAKEFK YYNTCLNHWQ TYENNSHVT NAYWADTSKA NADGISNTYG GSFRKGLAWL N

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Macromolecule #67: Transmembrane protein, putative

MacromoleculeName: Transmembrane protein, putative / type: protein_or_peptide / ID: 67 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 13.340979 KDa
SequenceString:
MFWRNVVRGL NCQQALRRQN FAKNITTTDI PKDSHHFAAK RSGFTQTEQA PFAYNDVYQY PKDYKPWNYN YKGNGVLLAL FLGSAFSLV AYERSYASKT GRYQRKVQQN YYQI

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Macromolecule #68: Ymf57

MacromoleculeName: Ymf57 / type: protein_or_peptide / ID: 68 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote)
Molecular weightTheoretical: 12.473938 KDa
SequenceString:
MLKNKLIKFK FFRFVQSGFY VDFIFKKFSE MFIRNIFIYS SIFFGEKFMI EYLTKKTIDS FIFNNNRFNF INLVESKYFL QILTLILYL FFITIFILFY I

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Macromolecule #69: Complex I-MNLL

MacromoleculeName: Complex I-MNLL / type: protein_or_peptide / ID: 69 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila SB210 (eukaryote) / Strain: SB210
Molecular weightTheoretical: 12.103036 KDa
SequenceString:
MSSMLIWGAC FGLFTRAAAC KASMIPLTTS PWKYPKYMIV SAVTFYYFDW YRRMALEQLC YNEEKLERYQ IRAKLQSLKI GEELSDAYR ESFFEHAVQK NNI

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Macromolecule #70: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 70 / Number of copies: 22 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #71: URIDINE-5'-DIPHOSPHATE

MacromoleculeName: URIDINE-5'-DIPHOSPHATE / type: ligand / ID: 71 / Number of copies: 1 / Formula: UDP
Molecular weightTheoretical: 404.161 Da
Chemical component information

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM / Uridine diphosphate

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Macromolecule #72: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 72 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #73: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 73 / Number of copies: 27 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

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Macromolecule #74: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 74 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

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Macromolecule #75: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 75 / Number of copies: 6 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

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Macromolecule #76: 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE

MacromoleculeName: 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE
type: ligand / ID: 76 / Number of copies: 4 / Formula: LPP
Molecular weightTheoretical: 648.891 Da
Chemical component information

ChemComp-LPP:
2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE / phospholipid*YM

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Macromolecule #77: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 77 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

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Macromolecule #78: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 78 / Number of copies: 3 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

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

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Macromolecule #79: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 79 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

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

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Macromolecule #80: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 80 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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Macromolecule #81: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 81 / Number of copies: 1 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

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

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Macromolecule #82: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 82 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.6 µm / Nominal defocus min: 0.6 µm
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 25.66 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 138746
FSC plot (resolution estimation)

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