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- PDB-2ybb: Fitted model for bovine mitochondrial supercomplex I1III2IV1 by s... -

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Basic information

Entry
Database: PDB / ID: 2ybb
TitleFitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)
Components
  • (CYTOCHROME B-C1 COMPLEX SUBUNIT ...) x 9
  • (CYTOCHROME C OXIDASE SUBUNIT ...) x 12
  • (NADH-QUINONE OXIDOREDUCTASE SUBUNIT ...NADH dehydrogenase (quinone)) x 10
  • (NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT ...) x 2
  • CYTOCHROME B
  • CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB
  • CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
  • CYTOCHROME C
KeywordsOXIDOREDUCTASE / SUPERCOMPLEX B / MITOCHONDRIA / RESPIRATORY CHAIN / AMPHIPOL A8-35 / RANDOM CONICAL TILT
Function / homology
Function and homology information


Release of apoptotic factors from the mitochondria / Formation of apoptosome / Activation of caspases through apoptosome-mediated cleavage / Pyroptosis / Regulation of the apoptosome activity / Transcriptional activation of mitochondrial biogenesis / Detoxification of Reactive Oxygen Species / TP53 Regulates Metabolic Genes / respiratory chain complex IV assembly / mitochondrial respirasome assembly ...Release of apoptotic factors from the mitochondria / Formation of apoptosome / Activation of caspases through apoptosome-mediated cleavage / Pyroptosis / Regulation of the apoptosome activity / Transcriptional activation of mitochondrial biogenesis / Detoxification of Reactive Oxygen Species / TP53 Regulates Metabolic Genes / respiratory chain complex IV assembly / mitochondrial respirasome assembly / Cytoprotection by HMOX1 / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / respiratory chain complex IV / NADH dehydrogenase (quinone) activity / mitochondrial respiratory chain complex III assembly / regulation of oxidative phosphorylation / Respiratory electron transport / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / mitochondrial respirasome / respiratory chain complex I / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinone binding / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / molybdopterin cofactor binding / mitochondrial electron transport, cytochrome c to oxygen / electron transport coupled proton transport / iron-sulfur cluster assembly / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / enzyme regulator activity / respirasome / respiratory electron transport chain / ferric iron binding / central nervous system development / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / oxidoreductase activity / iron ion binding / copper ion binding / apoptotic process / heme binding / mitochondrion / proteolysis / nucleoplasm / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
NADH-quinone oxidoreductase, subunit15 / NADH-quinone oxidoreductase, subunit 15 superfamily / NADH-quinone oxidoreductase chain 15 / Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Frataxin/CyaY superfamily / Cytochrome c oxidase, subunit 8 / Cytochrome c oxidase, subunit 8 superfamily / Cytochrome oxidase c subunit VIII ...NADH-quinone oxidoreductase, subunit15 / NADH-quinone oxidoreductase, subunit 15 superfamily / NADH-quinone oxidoreductase chain 15 / Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Frataxin/CyaY superfamily / Cytochrome c oxidase, subunit 8 / Cytochrome c oxidase, subunit 8 superfamily / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB / Cytochrome c oxidase subunit IV / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Cytochrome C oxidase, subunit VIIB domain superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit VIIa superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / Cytochrome c oxidase subunit VIc / Cytochrome C oxidase chain VIIB / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / : / Cytochrome b-c1 complex, subunit 6 / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase subunit VIIc superfamily / Cytochrome c oxidase subunit IV superfamily / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit Va/VI / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase subunit Va / Cytochrome c oxidase, subunit VIb / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Molybdopterin oxidoreductase Fe4S4 domain / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase subunit I domain / Molybdopterin oxidoreductase Fe4S4 domain / Cytochrome c oxidase, subunit II / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / 4Fe-4S binding domain / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome b-c1 complex subunit 9 / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Cytochrome c oxidase subunit III / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Heme-copper oxidase subunit III family profile. / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Molybdopterin dinucleotide-binding domain / Cytochrome c oxidase subunit III-like superfamily / Molydopterin dinucleotide binding domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c, class IA/ IB / Cytochrome b / : / : / Cytochrome c/quinol oxidase subunit II / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Copper centre Cu(A) / Cytochrome C oxidase subunit II, transmembrane domain superfamily / CO II and nitrous oxide reductase dinuclear copper centers signature.
Similarity search - Domain/homology
CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / IRON/SULFUR CLUSTER / STIGMATELLIN A ...CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / IRON/SULFUR CLUSTER / STIGMATELLIN A / UBIQUINONE-1 / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 9 / Cytochrome b / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 4 isoform 1, mitochondrial / Cytochrome c oxidase subunit 5A, mitochondrial / Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase subunit 6B1 / Cytochrome c oxidase subunit 7C, mitochondrial / Cytochrome c oxidase subunit 6C / Cytochrome c oxidase subunit 7A1, mitochondrial / Cytochrome c oxidase subunit 6A2, mitochondrial / Cytochrome b-c1 complex subunit 10 / Cytochrome c oxidase subunit 8B, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome c / Cytochrome c oxidase subunit 2 / NADH-quinone oxidoreductase subunit 6 / NADH-quinone oxidoreductase subunit 5 / NADH-quinone oxidoreductase subunit 4 / NADH-quinone oxidoreductase subunit 2 / NADH-quinone oxidoreductase subunit 1 / NADH-quinone oxidoreductase subunit 3 / NADH-quinone oxidoreductase subunit 9 / NADH-quinone oxidoreductase subunit 15
Similarity search - Component
Biological speciesTHERMUS THERMOPHILUS (bacteria)
BOS TAURUS (cattle)
ESCHERICHIA COLI (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 19 Å
AuthorsAlthoff, T. / Mills, D.J. / Popot, J.-L. / Kuehlbrandt, W.
Citation
Journal: EMBO J / Year: 2011
Title: Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1.
Authors: Thorsten Althoff / Deryck J Mills / Jean-Luc Popot / Werner Kühlbrandt /
Abstract: The respiratory chain in the inner mitochondrial membrane contains three large multi-enzyme complexes that together establish the proton gradient for ATP synthesis, and assemble into a supercomplex. ...The respiratory chain in the inner mitochondrial membrane contains three large multi-enzyme complexes that together establish the proton gradient for ATP synthesis, and assemble into a supercomplex. A 19-Å 3D map of the 1.7-MDa amphipol-solubilized supercomplex I(1)III(2)IV(1) from bovine heart obtained by single-particle electron cryo-microscopy reveals an amphipol belt replacing the membrane lipid bilayer. A precise fit of the X-ray structures of complex I, the complex III dimer, and monomeric complex IV indicates distances of 13 nm between the ubiquinol-binding sites of complexes I and III, and of 10-11 nm between the cytochrome c binding sites of complexes III and IV. The arrangement of respiratory chain complexes suggests two possible pathways for efficient electron transfer through the supercomplex, of which the shorter branch through the complex III monomer proximal to complex I may be preferred.
#1: Journal: Ph D Thesis / Year: 2011
Title: Strukturelle Untersuchungen Am Superkomplex I1III2Iv1 Der Atmungskette Mittels Kryoelektronenmikroskopie
Authors: Althoff, T.
History
DepositionMar 2, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 19, 2011Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2012Group: Other
Revision 1.2Aug 30, 2017Group: Advisory / Data collection / Category: em_software / pdbx_distant_solvent_atoms
Item: _em_software.fitting_id / _em_software.image_processing_id
Revision 1.3Oct 23, 2019Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: cell / struct_conn / struct_ref_seq
Item: _cell.Z_PDB / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq.db_align_beg

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Structure visualization

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Assembly

Deposited unit
1: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1
2: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2
3: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3
4: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4
5: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5
6: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6
7: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15
8: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9
A: CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL
B: CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL
C: CYTOCHROME B
D: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
E: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
F: CYTOCHROME B-C1 COMPLEX SUBUNIT 7
G: CYTOCHROME B-C1 COMPLEX SUBUNIT 8
H: CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL
I: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
J: CYTOCHROME B-C1 COMPLEX SUBUNIT 9
K: CYTOCHROME B-C1 COMPLEX SUBUNIT 10
L: CYTOCHROME C OXIDASE SUBUNIT 1
M: CYTOCHROME C OXIDASE SUBUNIT 2
N: CYTOCHROME C OXIDASE SUBUNIT 3
O: CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL
P: CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL
Q: CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL
R: CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB
S: CYTOCHROME C OXIDASE SUBUNIT 6B1
T: CYTOCHROME C OXIDASE SUBUNIT 6C
U: CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL
V: CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL
W: CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL
X: CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL
Y: CYTOCHROME C
a: CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL
b: CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL
c: CYTOCHROME B
d: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
e: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
f: CYTOCHROME B-C1 COMPLEX SUBUNIT 7
g: CYTOCHROME B-C1 COMPLEX SUBUNIT 8
h: CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL
i: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
j: CYTOCHROME B-C1 COMPLEX SUBUNIT 9
k: CYTOCHROME B-C1 COMPLEX SUBUNIT 10
m: NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L,
n: NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M,
o: NADH-QUINONE OXIDOREDUCTASE SUBUNIT N
p: NADH-QUINONE OXIDOREDUCTASE SUBUNIT K
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,125,22490
Polymers1,107,06048
Non-polymers18,16442
Water28,7881598
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA

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Components

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NADH-QUINONE OXIDOREDUCTASE SUBUNIT ... , 10 types, 10 molecules 12345678op

#1: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 1 / NDH-1 SUBUNIT 1


Mass: 48693.715 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO1 (51KDA) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56222, NADH dehydrogenase (quinone)
#2: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 2 / NDH-1 SUBUNIT 2


Mass: 20309.162 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO2 (24KDA) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56221, NADH dehydrogenase (quinone)
#3: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 3 / NDH-1 SUBUNIT 3


Mass: 86656.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO3 (75KDA) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56223, NADH dehydrogenase (quinone)
#4: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 4 / NDH-1 SUBUNIT 4


Mass: 46428.027 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO4 (49KDA) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56220, NADH dehydrogenase (quinone)
#5: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 5 / NDH-1 SUBUNIT 5


Mass: 23893.254 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO5 (30KDA) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56219, NADH dehydrogenase (quinone)
#6: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I SUBUNIT 6 / NDH-1 SUBUNIT 6


Mass: 20262.564 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO6 (PSST) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56218, NADH dehydrogenase (quinone)
#7: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I CHAIN 15 / NDH-1 SUBUNIT 15


Mass: 14812.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO15 / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q5SKZ7, NADH dehydrogenase (quinone)
#8: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I SUBUNIT 9 / NDH-1 SUBUNIT 9


Mass: 20106.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: NQO9 (TYKY) / Source: (natural) THERMUS THERMOPHILUS (bacteria) / Strain: HB8 / References: UniProt: Q56224, NADH dehydrogenase (quinone)
#36: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT N / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I SUBUNIT N / NDH-1 SUBUNIT N


Mass: 32187.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SUBUNIT NUON (CHAIN2) / Source: (natural) ESCHERICHIA COLI (E. coli) / Strain: BL21List of strains of Escherichia coli / References: NADH:ubiquinone reductase (H+-translocating)
#37: Protein NADH-QUINONE OXIDOREDUCTASE SUBUNIT K / NADH dehydrogenase (quinone) / NADH DEHYDROGENASE I SUBUNIT K / NDH-1 SUBUNIT K


Mass: 23932.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SUBUNITS NUOA, J AND K (CHAIN3,6 AND 4L) / Source: (natural) ESCHERICHIA COLI (E. coli) / Strain: BL21List of strains of Escherichia coli / References: NADH:ubiquinone reductase (H+-translocating)

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CYTOCHROME B-C1 COMPLEX SUBUNIT ... , 9 types, 18 molecules AaBbEeFfGgHhIiJjKk

#9: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL / COMPLEX III SUBUNIT 1 / CORE PROTEIN I / UBIQUINOL-CYTOCHROME- C REDUCTASE COMPLEX CORE PROTEIN 1


Mass: 49266.254 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P31800, quinol-cytochrome-c reductase
#10: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL / COMPLEX III SUBUNIT 2 / CORE PROTEIN II / UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2


Mass: 46575.469 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P23004, quinol-cytochrome-c reductase
#13: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL / COMPLEX III SUBUNIT 5 / CYTOCHROME B-C1 COMPLEX SUBUNIT 5 / RIESKE IRON-SULFUR PROTEIN / UBIQUINOL- ...COMPLEX III SUBUNIT 5 / CYTOCHROME B-C1 COMPLEX SUBUNIT 5 / RIESKE IRON-SULFUR PROTEIN / UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT


Mass: 21640.580 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P13272, quinol-cytochrome-c reductase
#14: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 7 / COMPLEX III SUBUNIT 7 / UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KDA PROTEIN / COMPLEX III SUBUNIT VII


Mass: 13371.190 Da / Num. of mol.: 2 / Mutation: YES / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00129, quinol-cytochrome-c reductase
#15: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 8 / COMPLEX III SUBUNIT 8 / COMPLEX III SUBUNIT VIII / UBIQUINOL- CYTOCHROME C REDUCTASE COMPLEX 9.5 ...COMPLEX III SUBUNIT 8 / COMPLEX III SUBUNIT VIII / UBIQUINOL- CYTOCHROME C REDUCTASE COMPLEX 9.5 KDA PROTEIN / UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C


Mass: 9606.027 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P13271, quinol-cytochrome-c reductase
#16: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL / COMPLEX III SUBUNIT 6 / COMPLEX III SUBUNIT VIII / CYTOCHROME C1 NON-HEME 11 KDA PROTEIN / ...COMPLEX III SUBUNIT 6 / COMPLEX III SUBUNIT VIII / CYTOCHROME C1 NON-HEME 11 KDA PROTEIN / MITOCHONDRIAL HINGE PROTEIN / UBIQUINOL- CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN


Mass: 9189.116 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00126, quinol-cytochrome-c reductase
#17: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL / COMPLEX III SUBUNIT 5 / CYTOCHROME B-C1 COMPLEX SUBUNIT 5 / RIESKE IRON-SULFUR PROTEIN / UBIQUINOL- ...COMPLEX III SUBUNIT 5 / CYTOCHROME B-C1 COMPLEX SUBUNIT 5 / RIESKE IRON-SULFUR PROTEIN / UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT / CYTOCHROME B-C1 COMPLEX SUBUNIT 11 / COMPLEX III SUBUNIT IX / UBIQUINOL-CYTOCHROME C REDUCTASE 8 KDA PROTEIN / RISP


Mass: 6677.736 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P13272, quinol-cytochrome-c reductase
#18: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 9 / COMPLEX III SUBUNIT 9 / COMPLEX III SUBUNIT X / CYTOCHROME C1 NON-HEME 7 KDA PROTEIN / UBIQUINOL- ...COMPLEX III SUBUNIT 9 / COMPLEX III SUBUNIT X / CYTOCHROME C1 NON-HEME 7 KDA PROTEIN / UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.2 KDA PROTEIN


Mass: 7209.311 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00130, quinol-cytochrome-c reductase
#19: Protein CYTOCHROME B-C1 COMPLEX SUBUNIT 10 / COMPLEX III SUBUNIT 10 / COMPLEX III SUBUNIT XI / UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 6.4 KDA PROTEIN


Mass: 6370.390 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P07552, quinol-cytochrome-c reductase

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Protein , 4 types, 6 molecules CcDdRY

#11: Protein CYTOCHROME B / / COMPLEX III SUBUNIT 3 / COMPLEX III SUBUNIT III / CYTOCHROME B-C1 COMPLEX SUBUNIT 3 / UBIQUINOL- ...COMPLEX III SUBUNIT 3 / COMPLEX III SUBUNIT III / CYTOCHROME B-C1 COMPLEX SUBUNIT 3 / UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME B SUBUNIT


Mass: 42620.340 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00157, quinol-cytochrome-c reductase
#12: Protein CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL / / COMPLEX III SUBUNIT 4 / COMPLEX III SUBUNIT IV / CYTOCHROME B- C1 COMPLEX SUBUNIT 4 / UBIQUINOL- ...COMPLEX III SUBUNIT 4 / COMPLEX III SUBUNIT IV / CYTOCHROME B- C1 COMPLEX SUBUNIT 4 / UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME C1 SUBUNIT


Mass: 27323.277 Da / Num. of mol.: 2 / Fragment: RESIDUES 85-325 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00125, quinol-cytochrome-c reductase
#26: Protein CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB / CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART / CYTOCHROME C OXIDASE POLYPEPTIDE VIB / COXVIAH


Mass: 9452.687 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P07471, cytochrome-c oxidase
#33: Protein CYTOCHROME C /


Mass: 11595.392 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P62894

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CYTOCHROME C OXIDASE SUBUNIT ... , 12 types, 12 molecules LMNOPQSTUVWX

#20: Protein CYTOCHROME C OXIDASE SUBUNIT 1 / / CYTOCHROME C OXIDASE POLYPEPTIDE I


Mass: 57065.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00396, cytochrome-c oxidase
#21: Protein CYTOCHROME C OXIDASE SUBUNIT 2 / / CYTOCHROME C OXIDASE POLYPEPTIDE II


Mass: 26040.393 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P68530, cytochrome-c oxidase
#22: Protein CYTOCHROME C OXIDASE SUBUNIT 3 / / CYTOCHROME C OXIDASE POLYPEPTIDE III


Mass: 29957.627 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00415, cytochrome-c oxidase
#23: Protein CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE IV / CYTOCHROME C OXIDASE SUBUNIT IV ISOFORM 1 / COX IV-1


Mass: 17179.646 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00423, cytochrome-c oxidase
#24: Protein CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE VA


Mass: 12453.081 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00426, cytochrome-c oxidase
#25: Protein CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE VIA / CYTOCHROME C OXIDASE POLYPEPTIDE VB


Mass: 10684.038 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00428, cytochrome-c oxidase
#27: Protein CYTOCHROME C OXIDASE SUBUNIT 6B1 / / CYTOCHROME C OXIDASE POLYPEPTIDE VII / CYTOCHROME C OXIDASE SUBUNIT AED / CYTOCHROME C OXIDASE ...CYTOCHROME C OXIDASE POLYPEPTIDE VII / CYTOCHROME C OXIDASE SUBUNIT AED / CYTOCHROME C OXIDASE SUBUNIT VIB ISOFORM 1 / COX VIB-1


Mass: 10039.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00429, cytochrome-c oxidase
#28: Protein CYTOCHROME C OXIDASE SUBUNIT 6C / / CYTOCHROME C OXIDASE POLYPEPTIDE VIC / CYTOCHROME C OXIDASE SUBUNIT STA


Mass: 8494.982 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P04038, cytochrome-c oxidase
#29: Protein CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL / / CYTOCHROME C OXIDASE SUBUNIT VIIIC / CYTOCHROME C OXIDASE SUBUNIT VIIA-HEART / CYTOCHROME C OXIDASE ...CYTOCHROME C OXIDASE SUBUNIT VIIIC / CYTOCHROME C OXIDASE SUBUNIT VIIA-HEART / CYTOCHROME C OXIDASE SUBUNIT VIIA-MUSCLE / VIIIC / CYTOCHROME C OXIDASE SUBUNIT VIIA-H / CYTOCHROME C OXIDASE SUBUNIT VIIA-M


Mass: 6682.726 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P07470, cytochrome-c oxidase
#30: Protein CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE VIIB / IHQ


Mass: 6365.217 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P13183, cytochrome-c oxidase
#31: Protein/peptide CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE VIIIA / CYTOCHROME C OXIDASE POLYPEPTIDE VIIC


Mass: 5449.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P00430, cytochrome-c oxidase
#32: Protein/peptide CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL / / CYTOCHROME C OXIDASE POLYPEPTIDE VIII-HEART / CYTOCHROME C OXIDASE SUBUNIT 8-1 / CYTOCHROME C ...CYTOCHROME C OXIDASE POLYPEPTIDE VIII-HEART / CYTOCHROME C OXIDASE SUBUNIT 8-1 / CYTOCHROME C OXIDASE SUBUNIT 8H / IX / VIIIB


Mass: 4967.756 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Tissue: MUSCLESkeletal muscle / References: UniProt: P10175, cytochrome-c oxidase

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NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT ... , 2 types, 2 molecules mn

#34: Protein NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L,


Mass: 40357.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SUBUNIT NUOL (CHAIN5) / Source: (natural) ESCHERICHIA COLI (E. coli) / Strain: BL21List of strains of Escherichia coli / References: NADH:ubiquinone reductase (H+-translocating)
#35: Protein NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, / SUBUNIT OF NADH\: UBIQUINONE OXIDOREDUCTASE I


Mass: 33293.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SUBUNIT NUOM (CHAIN4) / Source: (natural) ESCHERICHIA COLI (E. coli) / Strain: BL21List of strains of Escherichia coli / References: NADH:ubiquinone reductase (H+-translocating)

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Non-polymers , 15 types, 1640 molecules

#38: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Fe4S4
#39: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE / Flavin mononucleotide


Mass: 456.344 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H21N4O9P
#40: Chemical ChemComp-NAI / 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / NADH / Nicotinamide adenine dinucleotide


Mass: 665.441 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H29N7O14P2
#41: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
#42: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe2S2
#43: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#44: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#45: Chemical ChemComp-SMA / STIGMATELLIN A


Mass: 514.650 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C30H42O7
#46: Chemical ChemComp-UQ1 / UBIQUINONE-1


Mass: 250.290 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H18O4
#47: Chemical ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#48: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL / Cardiolipin


Mass: 1464.043 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#49: Chemical ChemComp-HEA / HEME-A / Heme A


Mass: 852.837 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C49H56FeN4O6
#50: Chemical ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cu
#51: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#52: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1598 / Source method: isolated from a natural source / Formula: H2O

-
Details

Sequence detailsDUE TO THE AMBIGUITY ABOUT THE REGISTER OF THE SEQUENCE, THESE CHAINS WERE BUILT WITH UNK RESIDUES ...DUE TO THE AMBIGUITY ABOUT THE REGISTER OF THE SEQUENCE, THESE CHAINS WERE BUILT WITH UNK RESIDUES ONLY. THE UNIPROT REFERENCES FOR CHAINS m, n, o, p ARE C6E9S4, C6E9S5, C6E9S6, C6E9S2 RESPECTIVELY.

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: RESPIRATORY SUPERCOMPLEX B (I1III2IV1) COMPOSED OF COMPLEX I, DIMERIC COMPLEX III AND COMPLEX IV FROM BOVINE HEART MITOCHONDRIA
Type: COMPLEX
Details: THE SUPERCOMPLEXES WERE KEPT SOLUBLE BY AMPHIPOLS A8-35
Buffer solutionName: 10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE / pH: 7.7 / Details: 10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE
SpecimenConc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: CARBON
VitrificationInstrument: HOMEMADE PLUNGER / Cryogen name: ETHANE
Details: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ...Details: VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING

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Electron microscopy imaging

Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI F30
Details: LOW DOSE CONDITIONS. FOR RANDOM CONICAL TILT EACH AREA WAS IMAGED TWICE WITH THE FIRST IMAGE TAKEN AT A TILT ANGLE OF -45 OR -50 DEGREE
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 59000 X / Calibrated magnification: 58829 X / Nominal defocus max: 6000 nm / Nominal defocus min: 500 nm / Cs: 2 mm
Specimen holderTemperature: 78 K / Tilt angle max: 0 ° / Tilt angle min: -50 °
Image recordingElectron dose: 25 e/Å2 / Film or detector model: KODAK SO-163 FILM
Image scansNum. digital images: 154
Radiation wavelengthRelative weight: 1

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Processing

EM software
IDNameCategory
1UCSF Chimeramodel fitting
2IMAGIC3D reconstruction
3SPIDER3D reconstruction
CTF correctionDetails: PHASE-FLIPPPING ON EACH PARTICLE
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionMethod: RANDOM CONICAL TILT AND PROJECTION MATCHING WITH DIRECT FOURIER BACKPROJECTION AND SIRT
Resolution: 19 Å / Num. of particles: 10684 / Nominal pixel size: 4.76 Å / Actual pixel size: 4.76 Å
Details: FINAL MAP WAS CALCULATED WITH SIRT FROM COMBINED TILTED AND UNTILTED DATASETS WITH 10684 PARTICLES EACH AND OMITTING 30 PER CENT OF IMAGES WITH LOWEST CROSS CORRELATION. THIS ENTRY IS BASED ...Details: FINAL MAP WAS CALCULATED WITH SIRT FROM COMBINED TILTED AND UNTILTED DATASETS WITH 10684 PARTICLES EACH AND OMITTING 30 PER CENT OF IMAGES WITH LOWEST CROSS CORRELATION. THIS ENTRY IS BASED ON PDBS 3IAM,3M9C,1PP9,1BGY,1OCC AND 2B4Z WHICH WERE FITTED MANUALLY INTO THE EM DENSITY MAP OF BOVINE SUPERCOMPLEX I1III2IV1. THE POSITION OF 2B4Z WAS INFERRED FROM PDB 3CX5. THE CHAIN NAMES ARE CASE SENSITIVE. CHAINS A-K AND a-k DENOTE IDENTICAL CHAINS WITHIN A DIMER. CHAINS L-X AND M-P BELONG TO DIFFERENT PROTEINS. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-1876.
Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Details: METHOD--RIGID BODY REFINEMENT PROTOCOL--X-RAY
Atomic model building
IDPDB-ID 3D fitting-ID
13IAM

3iam

1
23M9C

3m9c

1
31PP9

1pp9

1
41BGY

1bgy

1
51OCC

1occ

1
62B4Z

2b4z

1
RefinementHighest resolution: 19 Å
Refinement stepCycle: LAST / Highest resolution: 19 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms70092 0 875 1598 72565

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