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- PDB-1bcc: CYTOCHROME BC1 COMPLEX FROM CHICKEN -

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Basic information

Entry
Database: PDB / ID: 1bcc
TitleCYTOCHROME BC1 COMPLEX FROM CHICKEN
Components(UBIQUINOL CYTOCHROME C ...) x 10
KeywordsOXIDOREDUCTASE / UBIQUINONE / REDOX ENZYME / MEMBRANE PROTEIN / RESPIRATORY CHAIN / ELECTRON TRANSPORT
Function / homology
Function and homology information


Respiratory electron transport / mitochondrial respiratory chain complex III assembly / Respiratory electron transport / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain ...Respiratory electron transport / mitochondrial respiratory chain complex III assembly / Respiratory electron transport / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / response to oxidative stress / oxidoreductase activity / heme binding / mitochondrion / proteolysis / metal ion binding / cytoplasm
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 / Ubiquinol-cytochrome c reductase 8kDa, N-terminal ...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 / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / 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 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-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 / Up-down Bundle / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / UBIQUINONE-10 / 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-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial ...FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / UBIQUINONE-10 / 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-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIR, NCS AVERAGING / Resolution: 3.16 Å
AuthorsZhang, Z. / Huang, L. / Shulmeister, V.M. / Chi, Y.-I. / Kim, K.K. / Hung, L.-W. / Crofts, A.R. / Berry, E.A. / Kim, S.-H.
CitationJournal: Nature / Year: 1998
Title: Electron transfer by domain movement in cytochrome bc1.
Authors: Zhang, Z. / Huang, L. / Shulmeister, V.M. / Chi, Y.I. / Kim, K.K. / Hung, L.W. / Crofts, A.R. / Berry, E.A. / Kim, S.H.
History
DepositionMar 23, 1998Processing site: BNL
Revision 1.0Aug 19, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Mar 19, 2014Group: Other
Revision 1.4Oct 29, 2014Group: Non-polymer description
Revision 1.5Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
B: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
C: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
D: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
E: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
F: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
G: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
H: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
I: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
J: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)233,61318
Polymers228,93410
Non-polymers4,6798
Water0
1
A: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
B: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
C: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
D: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
E: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
F: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
G: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
H: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
I: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
J: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
hetero molecules

A: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
B: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
C: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
D: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
E: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
F: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
G: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
H: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
I: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
J: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)467,22636
Polymers457,86720
Non-polymers9,35816
Water0
TypeNameSymmetry operationNumber
identity operation1
point symmetry operation1
Unit cell
Length a, b, c (Å)169.590, 182.518, 240.573
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(-0.835029, -0.550204, -0.001423), (-0.550192, 0.834987, 0.009204), (-0.003876, 0.008468, -0.999957)128.9528, 37.82, 171.594

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Components

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UBIQUINOL CYTOCHROME C ... , 10 types, 10 molecules ABCDEFGHIJ

#1: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 49795.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle
References: UniProt: P13272, UniProt: P31800*PLUS, quinol-cytochrome-c reductase
#2: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 45077.699 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P23004, quinol-cytochrome-c reductase
#3: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 42622.977 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P18946, quinol-cytochrome-c reductase
#4: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 27357.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P00125, quinol-cytochrome-c reductase
#5: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 21739.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P13272, quinol-cytochrome-c reductase
#6: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 13400.142 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P00129, quinol-cytochrome-c reductase
#7: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 9715.241 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P13271, quinol-cytochrome-c reductase
#8: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 9223.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P00126, quinol-cytochrome-c reductase
#9: Protein/peptide UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 2826.475 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: quinol-cytochrome-c reductase
#10: Protein UBIQUINOL CYTOCHROME C OXIDOREDUCTASE / CYTOCHROME BC1 COMPLEX / COMPLEX III


Mass: 7175.295 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ISOLATED FROM NATURAL HEART MUSCLE TISSUE / Source: (natural) Gallus gallus (chicken)
Cellular location: MITOCHONDRIAL INNER MEMBRANEInner mitochondrial membrane
Organ: HEART / Organelle: MITOCHONDRIAMitochondrion / Tissue: MUSCLESkeletal muscle / References: UniProt: P00130, quinol-cytochrome-c reductase

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Sugars , 1 types, 1 molecules

#14: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 4 types, 7 molecules

#11: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#12: Chemical ChemComp-U10 / UBIQUINONE-10 / Coenzyme Q10 / Coenzyme Q10


Mass: 863.343 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C59H90O4
#13: Chemical ChemComp-PEE / 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE / Discrete optimized protein energy


Mass: 749.073 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H83NO8P / Comment: DOPE, phospholipid*YM
#15: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 1 / 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: 3.83 Å3/Da / Density % sol: 67.9 %
Crystal growpH: 6.7
Details: 20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000
Crystal
*PLUS
Crystal grow
*PLUS
Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
160 mMKMES1droppH6.7
28 %PEG40001drop
320 mMK-MOPS 7.51drop
420 g/ln-octyl-beta-D-glucopyranoside1drop
587.5 mM1dropNaCl
610 %glycerol1drop
730 %glycerol1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 20, 1995 / Details: CYL.-BENT MIRRORS
RadiationMonochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.08 Å / Relative weight: 1
ReflectionHighest resolution: 3.16 Å / Num. obs: 123869 / % possible obs: 91.6 % / Observed criterion σ(I): -2 / Redundancy: 4.5 % / Biso Wilson estimate: 64.6 Å2 / Rmerge(I) obs: 0.095 / Rsym value: 0.102 / Net I/σ(I): 12.5
Reflection shellResolution: 3.16→3.27 Å / Redundancy: 3.32 % / Rmerge(I) obs: 0.324 / Mean I/σ(I) obs: 2.7 / Rsym value: 0.4 / % possible all: 84.5
Reflection
*PLUS
Num. measured all: 556456

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
MLPHAREphasing
RAVEmodel building
CNS0.1refinement
RAVEphasing
RefinementMethod to determine structure: MIR, NCS AVERAGING / Resolution: 3.16→12 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 16310580.72 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.31 5446 5.1 %RANDOM
Rwork0.27 ---
obs0.27 107167 85.5 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 44.84 Å2 / ksol: 0.257 e/Å3
Displacement parametersBiso mean: 78.4 Å2
Baniso -1Baniso -2Baniso -3
1--48.37 Å20 Å20 Å2
2--23.87 Å20 Å2
3---24.5 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.66 Å0.55 Å
Luzzati d res low-12 Å
Luzzati sigma a0.56 Å0.46 Å
Refinement stepCycle: LAST / Resolution: 3.16→12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15439 0 280 0 15719
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.009
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.613
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d20.8
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.89
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
Refine LS restraints NCSNCS model details: RESTRAINS
LS refinement shellResolution: 3.16→3.35 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.43 694 5 %
Rwork0.407 13256 -
obs--67.3 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMTOPHCSDX.PRO
X-RAY DIFFRACTION2PROTEIN_REP.PARAMTOPH19.RCV
X-RAY DIFFRACTION3PARAM19.RCVFES.TOP
X-RAY DIFFRACTION4PARAM19X.HEMEHETERO.TOP
Software
*PLUS
Name: CNS / Version: 0.1 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.009935
X-RAY DIFFRACTIONc_angle_deg1.61327
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg20.8
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.89
LS refinement shell
*PLUS
Rfactor Rfree: 0.43

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