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- PDB-1kyo: YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C -

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Entry
Database: PDB / ID: 1kyo
TitleYEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C
Components
  • (UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX ...) x 6
  • CYTOCHROME B
  • CYTOCHROME C, ISO-1
  • CYTOCHROME C1, HEME PROTEIN
  • HEAVY CHAIN (VH) OF FV-FRAGMENT
  • LIGHT CHAIN (VL) OF FV-FRAGMENT
  • UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT
KeywordsOXIDOREDUCTASE/ELECTRON TRANSPORT / multisubunit membrane protein complex / enzyme substrate complex / electron transfer complex / antibody Fv fragment mediated crystallization / OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX
Function / homology
Function and homology information


matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / Pyroptosis / Release of apoptotic factors from the mitochondria / Detoxification of Reactive Oxygen Species / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / quinol-cytochrome-c reductase / cellular respiration ...matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / Pyroptosis / Release of apoptotic factors from the mitochondria / Detoxification of Reactive Oxygen Species / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / quinol-cytochrome-c reductase / cellular respiration / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial crista / respirasome / aerobic respiration / proton transmembrane transport / nuclear periphery / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / electron transfer activity / oxidoreductase activity / heme binding / mitochondrion / proteolysis / metal ion binding / cytosol
Similarity search - Function
Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Ubiquinol-cytochrome C reductase hinge domain / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome Bc1 Complex; Chain A, domain 1 ...Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Ubiquinol-cytochrome C reductase hinge domain / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / 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 / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / 3-layer Sandwich / Cytochrome c, class IA/ IB / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Cytochrome c / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix Hairpins / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
FE2/S2 (INORGANIC) CLUSTER / HEME C / STIGMATELLIN A / Cytochrome c isoform 1 / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial ...FE2/S2 (INORGANIC) CLUSTER / HEME C / STIGMATELLIN A / Cytochrome c isoform 1 / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 8, mitochondrial / Cytochrome b-c1 complex subunit 9, mitochondrial
Similarity search - Component
Biological speciesMus musculus (house mouse)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.97 Å
AuthorsLange, C. / Hunte, C.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2002
Title: Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.
Authors: Lange, C. / Hunte, C.
History
DepositionFeb 5, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 6, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Mar 3, 2021Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _chem_comp.pdbx_synonyms / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 2.1Aug 16, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Remark 999SEQUENCE Residue 270 (chains C and N) is in conflict in swissprot entry P00163 as being either ASP or VAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I
B: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2
C: CYTOCHROME B
D: CYTOCHROME C1, HEME PROTEIN
E: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT
F: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN
G: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN
H: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C
I: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN
J: HEAVY CHAIN (VH) OF FV-FRAGMENT
K: LIGHT CHAIN (VL) OF FV-FRAGMENT
L: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I
M: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2
N: CYTOCHROME B
O: CYTOCHROME C1, HEME PROTEIN
P: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT
Q: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN
R: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN
S: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C
T: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN
U: HEAVY CHAIN (VH) OF FV-FRAGMENT
V: LIGHT CHAIN (VL) OF FV-FRAGMENT
W: CYTOCHROME C, ISO-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)507,21534
Polymers501,50423
Non-polymers5,71011
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)147.224, 165.531, 195.889
Angle α, β, γ (deg.)90.00, 104.19, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX ... , 6 types, 12 molecules ALBMFQGRHSIT

#1: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I


Mass: 47358.168 Da / Num. of mol.: 2 / Fragment: RESIDUES 27-457 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P07256, quinol-cytochrome-c reductase
#2: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2


Mass: 38751.918 Da / Num. of mol.: 2 / Fragment: RESIDUES 17-368 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P07257, quinol-cytochrome-c reductase
#6: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN / MITOCHONDRIAL HINGE PROTEIN / COMPLEX III POLYPEPTIDE VI


Mass: 8870.749 Da / Num. of mol.: 2 / Fragment: RESIDUES 74-147 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P00127, quinol-cytochrome-c reductase
#7: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN / COMPLEX III SUBUNIT VII


Mass: 14452.557 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-127 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P00128, quinol-cytochrome-c reductase
#8: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C / UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN / COMPLEX III SUBUNIT VIII


Mass: 10856.314 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-94 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P08525, quinol-cytochrome-c reductase
#9: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN / COMPLEX III POLYPEPTIDE IX


Mass: 6507.470 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-57 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P22289, quinol-cytochrome-c reductase

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Protein , 4 types, 7 molecules CNDOEPW

#3: Protein CYTOCHROME B /


Mass: 43674.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P00163
#4: Protein CYTOCHROME C1, HEME PROTEIN /


Mass: 27807.395 Da / Num. of mol.: 2 / Fragment: RESIDUES 62-309 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P07143
#5: Protein UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT / RIESKE IRON-SULFUR PROTEIN / RISP


Mass: 20122.955 Da / Num. of mol.: 2 / Fragment: RESIDUES 31-215 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P08067, quinol-cytochrome-c reductase
#12: Protein CYTOCHROME C, ISO-1 /


Mass: 12115.915 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Organelle: MITOCHONDRIAMitochondrion / References: UniProt: P00044

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Antibody , 2 types, 4 molecules JUKV

#10: Antibody HEAVY CHAIN (VH) OF FV-FRAGMENT


Mass: 14365.817 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-127
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pASK68 / Production host: Escherichia coli (E. coli) / Strain (production host): JM83
#11: Antibody LIGHT CHAIN (VL) OF FV-FRAGMENT


Mass: 11926.350 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-107
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pASK68 / Production host: Escherichia coli (E. coli) / Strain (production host): JM83

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Non-polymers , 3 types, 11 molecules

#13: Chemical
ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#14: Chemical ChemComp-SMA / STIGMATELLIN A


Mass: 514.650 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C30H42O7
#15: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.61 Å3/Da / Density % sol: 73.33 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PEG4000, 20 mM Tris, 0.05 % Undecyl-maltopyranoside, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 277 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Feb 26, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.931 Å / Relative weight: 1
ReflectionResolution: 2.94→29.64 Å / Num. all: 187312 / Num. obs: 175444 / % possible obs: 92.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 43.7 Å2 / Limit h max: 48 / Limit h min: -49 / Limit k max: 56 / Limit k min: -49 / Limit l max: 66 / Limit l min: 0 / Observed criterion F max: 81215.36 / Observed criterion F min: 0.32 / Rsym value: 0.106 / Net I/σ(I): 6.8
Reflection shellResolution: 2.97→3.08 Å / Mean I/σ(I) obs: 2.3 / Num. unique all: 14711 / Rsym value: 0.395 / % possible all: 76.5
Reflection
*PLUS
Highest resolution: 2.97 Å / Lowest resolution: 30 Å / Rmerge(I) obs: 0.106
Reflection shell
*PLUS
% possible obs: 76.5 %

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Processing

Software
NameVersionClassificationNB
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1EZV

1ezv


Resolution: 2.97→29.64 Å / Rfactor Rfree error: 0.002 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.268 17442 9.9 %random
Rwork0.229 ---
all-187312 --
obs-175444 93.7 %-
Solvent computationSolvent model: CNS bulk solvent model used / Bsol: 10 Å2 / ksol: 0.228013 e/Å3
Displacement parametersBiso max: 162.05 Å2 / Biso mean: 59.66 Å2 / Biso min: 0.22 Å2
Baniso -1Baniso -2Baniso -3
1-13.53 Å20 Å24.85 Å2
2---6.64 Å20 Å2
3----6.89 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.44 Å0.38 Å
Luzzati d res low-5 Å
Luzzati sigma a0.84 Å0.97 Å
Luzzati d res high-2.97
Refinement stepCycle: LAST / Resolution: 2.97→29.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms35264 0 383 0 35647
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_angle_deg1.4
X-RAY DIFFRACTIONx_torsion_deg23.7
X-RAY DIFFRACTIONx_torsion_impr_deg1.25
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8

Resolution (Å)Rfactor RfreeNum. reflection Rfree% reflection Rfree (%)Rfactor RworkNum. reflection RworkRfactor Rfree errorNum. reflection allNum. reflection obs% reflection obs (%)
2.97-3.10.39319838.50.393176250.009233571960883.9
3.1-3.270.34420358.70.345184150.008233752045087.5
3.27-3.470.28620158.60.288192910.006232982130691.4
3.47-3.740.2321999.40.232198230.005233722202294.2
3.74-4.120.19721829.30.197204510.004234172263396.7
4.12-4.710.1832347100.18206130.004234322296098
4.71-5.930.1862340100.189207610.004234772310198.4
5.93-29.640.20723419.90.205210230.004237022336498.6
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refinement
*PLUS
σ(F): 0 / % reflection Rfree: 9.3 % / Rfactor obs: 0.228 / Rfactor Rfree: 0.267
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.42
LS refinement shell
*PLUS
Rfactor Rfree: 0.393 / % reflection Rfree: 8.5 % / Rfactor Rwork: 0.393

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