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- PDB-1zrt: Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound -

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Basic information

Entry
Database: PDB / ID: 1zrt
TitleRhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound
Components
  • Cytochrome b
  • Cytochrome c1
  • Ubiquinol-cytochrome c reductase iron-sulfur subunit
KeywordsELECTRON TRANSPORT / CYTOCHROME BC1 / MEMBRANE PROTEIN / HEME PROTEIN / RIESKE IRON SULFUR PROTEIN / CYTOCHROME B / CYTOCHROME C1 / COMPLEX III / OXIDOREDUCTASE / REDOX ENZYME / RESPIRATORY CHAIN / STIGMATELLIN
Function / homology
Function and homology information


respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / : / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / membrane => GO:0016020 / electron transfer activity / heme binding / metal ion binding / plasma membrane
Similarity search - Function
Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Single helix bin / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 3-layer Sandwich / Cytochrome b ...Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Single helix bin / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 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. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / 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 / 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 / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-PG6 / STIGMATELLIN A / Unknown ligand / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Cytochrome b / Cytochrome c1 / Cytochrome b ...FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-PG6 / STIGMATELLIN A / Unknown ligand / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Cytochrome b / Cytochrome c1 / Cytochrome b / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Cytochrome c1
Similarity search - Component
Biological speciesRhodobacter capsulatus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.51 Å
AuthorsBerry, E.A. / Huang, L.S. / Saechao, L.K. / Pon, N.G. / Valkova-Valchanov, M. / Daldal, F.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)DK44842 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM38237 United States
CitationJournal: Photosynth.Res. / Year: 2004
Title: X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts.
Authors: Berry, E.A. / Huang, L.S. / Saechao, L.K. / Pon, N.G. / Valkova-Valchanova, M. / Daldal, F.
History
DepositionMay 22, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 7, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Aug 17, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Database references / Derived calculations / Experimental preparation / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_sites ...atom_site / atom_sites / cell / chem_comp / database_2 / diffrn / diffrn_detector / diffrn_radiation / diffrn_radiation_wavelength / entity / entity_name_com / entity_src_gen / exptl_crystal_grow / pdbx_audit_support / pdbx_contact_author / pdbx_database_related / pdbx_database_status / pdbx_entity_instance_feature / pdbx_entity_nonpoly / pdbx_entry_details / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_torsion / refine / refine_analyze / refine_hist / refine_ls_restr / refine_ls_restr_ncs / refine_ls_shell / reflns / reflns_shell / software / struct / struct_asym / struct_biol / struct_conf / struct_conn / struct_conn_type / struct_keywords / struct_mon_prot_cis / struct_ncs_dom / struct_ncs_dom_lim / struct_ncs_ens / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_sheet / struct_sheet_order / struct_sheet_range / struct_site / struct_site_gen / symmetry
Item: _atom_sites.fract_transf_matrix[1][3] / _atom_sites.fract_transf_matrix[3][3] ..._atom_sites.fract_transf_matrix[1][3] / _atom_sites.fract_transf_matrix[3][3] / _cell.volume / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn.pdbx_serial_crystal_experiment / _diffrn_detector.pdbx_collection_date / _diffrn_detector.type / _diffrn_radiation.wavelength_id / _entity_name_com.name / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_seq_type / _exptl_crystal_grow.pdbx_details / _pdbx_database_status.SG_entry / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.value / _refine.B_iso_mean / _refine.aniso_B[1][1] / _refine.aniso_B[1][2] / _refine.aniso_B[1][3] / _refine.aniso_B[2][2] / _refine.aniso_B[2][3] / _refine.aniso_B[3][3] / _refine.details / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_free_error / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine.ls_d_res_low / _refine.ls_number_reflns_R_free / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_all / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_R_free / _refine.ls_percent_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_data_cutoff_high_absF / _refine.pdbx_data_cutoff_low_absF / _refine.pdbx_diffrn_id / _refine.pdbx_isotropic_thermal_model / _refine.pdbx_ls_cross_valid_method / _refine.pdbx_ls_sigma_F / _refine.pdbx_overall_phase_error / _refine.pdbx_solvent_shrinkage_radii / _refine.pdbx_solvent_vdw_probe_radii / _refine.pdbx_starting_model / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine.solvent_model_param_bsol / _refine.solvent_model_param_ksol / _refine_hist.d_res_high / _refine_hist.d_res_low / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_ligand / _refine_hist.pdbx_number_atoms_protein / _reflns.B_iso_Wilson_estimate / _reflns.number_all / _reflns.pdbx_diffrn_id / _reflns_shell.number_unique_obs / _struct.pdbx_CASP_flag / _struct_conn_type.id / _struct_keywords.pdbx_keywords / _struct_keywords.text / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq.pdbx_strand_id / _struct_ref_seq.ref_id / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end / _symmetry.space_group_name_Hall
Description: Model completeness
Details: Regions that were unclear in the original maps have been built/corrected with help from subsequently deposited structures of related proteins and with the help of modern software for rebuilding and refinement.
Provider: author / Type: Coordinate replacement
Revision 2.1Aug 23, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Cytochrome b
D: Cytochrome c1
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit
P: Cytochrome b
Q: Cytochrome c1
R: Ubiquinol-cytochrome c reductase iron-sulfur subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)202,10821
Polymers196,3456
Non-polymers5,76315
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33200 Å2
ΔGint-327 kcal/mol
Surface area70860 Å2
MethodPISA
Unit cell
Length a, b, c (Å)95.633, 154.360, 103.057
Angle α, β, γ (deg.)90.000, 113.570, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "C" and resid 7 through 40)
d_2ens_1(chain "P" and resid 7 through 40)
d_1ens_2(chain "C" and (resid 41 through 230 or resid 501 through 502))
d_2ens_2(chain "P" and (resid 41 through 230 or resid 501 through 502))
d_1ens_3(chain "C" and (resid 231 through 294 or resid 296...
d_2ens_3(chain "P" and (resid 231 through 294 or resid 296...
d_1ens_4(chain "D" and (resid 8 through 97 or resid 501))
d_2ens_4(chain "Q" and (resid 8 through 97 or resid 501))
d_1ens_5(chain "D" and resid 98 through 110)
d_2ens_5(chain "Q" and resid 98 through 110)
d_1ens_6(chain "D" and (resid 120 through 122 or (resid 123...
d_2ens_6(chain "Q" and resid 120 through 140)
d_1ens_7(chain "D" and resid 143 through 145)
d_2ens_7(chain "Q" and resid 143 through 145)
d_1ens_8(chain "D" and resid 149 through 162)
d_2ens_8(chain "Q" and resid 149 through 162)
d_1ens_9(chain "D" and resid 165 through 170)
d_2ens_9(chain "Q" and resid 165 through 170)
d_1ens_10(chain "D" and resid 178 through 254)
d_2ens_10(chain "Q" and resid 178 through 254)
d_1ens_11(chain "E" and resid 16 through 45)
d_2ens_11(chain "R" and resid 16 through 45)
d_1ens_12(chain "E" and (resid 49 through 55 or resid 178 through 191))
d_2ens_12(chain "R" and (resid 49 through 55 or resid 178 through 191))
d_1ens_13(chain "E" and resid 56 through 113)
d_2ens_13(chain "R" and (resid 56 through 82 or (resid 83...
d_1ens_14(chain "E" and (resid 119 through 172 or resid 174 through 177))
d_2ens_14(chain "R" and (resid 119 through 172 or resid 174 through 177))

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg label comp-IDEnd label comp-IDLabel asym-IDLabel seq-ID
d_11ens_1ASPASNA6 - 39
d_21ens_1ASPASNK6 - 39
d_11ens_2LEUARGA40 - 229
d_12ens_2HEMHEMB
d_13ens_2HEMHEMC
d_21ens_2LEUARGK40 - 229
d_22ens_2HEMHEML
d_23ens_2HEMHEMM
d_11ens_3ARGPROA230 - 293
d_12ens_3TRPTHRA296 - 385
d_13ens_3TYRPROA387 - 417
d_14ens_3PROSERA419 - 430
d_21ens_3ARGPROK230 - 293
d_22ens_3TRPTHRK296 - 385
d_23ens_3TYRPROK387 - 417
d_24ens_3PROSERK419 - 430
d_11ens_4ALAGLYG2 - 91
d_12ens_4HECHECH
d_21ens_4ALAGLYQ2 - 91
d_22ens_4HECHECR
d_11ens_5PROPHEG92 - 104
d_21ens_5PROPHEQ92 - 104
d_11ens_6GLNGLUG114 - 134
d_21ens_6GLNGLUQ114 - 134
d_11ens_7GLUALAG137 - 139
d_21ens_7GLUALAQ137 - 139
d_11ens_8ILEGLYG143 - 156
d_21ens_8ILEGLYQ143 - 156
d_11ens_9ASPALAG159 - 164
d_21ens_9ASPALAQ159 - 164
d_11ens_10GLYLYSG172 - 248
d_21ens_10GLYLYSQ172 - 248
d_11ens_11TYRLYSI8 - 37
d_21ens_11TYRLYST8 - 37
d_11ens_12SERSERI41 - 47
d_12ens_12PROGLYI170 - 183
d_21ens_12SERSERT41 - 47
d_22ens_12PROGLYT170 - 183
d_11ens_13ALAARGI48 - 105
d_21ens_13ALAARGT48 - 105
d_11ens_14ASPPROI111 - 164
d_12ens_14ASNILEI166 - 169
d_21ens_14ASPPROT111 - 164
d_22ens_14ASNILET166 - 169

NCS ensembles :
ID
ens_1
ens_2
ens_3
ens_4
ens_5
ens_6
ens_7
ens_8
ens_9
ens_10
ens_11
ens_12
ens_13
ens_14

NCS oper: (Code: given
Matrix: (0.625867, 0.319623, 0.711429), (0.319623, -0.937167, 0.139857), (0.711429, 0.139857, -0.6887)
Vector: -18.1065, -2.2872, 42.40731)

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Components

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Protein , 3 types, 6 molecules CPDQER

#1: Protein Cytochrome b


Mass: 49386.469 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter capsulatus (bacteria)
Description: The strain pMTS1/MT-RBC1 corresponds to a deletion strain MT-RBC1 complemented in trans with the plasmid pMTS1 bearing a wild-type copy of the petABC operon encoding the bc1 complex
Gene: petB, cytB, RCAP_rcc02769 / Plasmid: pMTS1 / Production host: Rhodobacter capsulatus (bacteria) / Strain (production host): pMTS1/MT-RBC1 / References: UniProt: D5ANZ3, UniProt: P0CY47*PLUS
#2: Protein Cytochrome c1


Mass: 28321.121 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter capsulatus (bacteria)
Description: The strain pMTS1/MT-RBC1 corresponds to a deletion strain MT-RBC1 complemented in trans with the plasmid pMTS1 bearing a wild-type copy of the petABC operon encoding the bc1 complex
Gene: petC, RCAP_rcc02770 / Plasmid: pMTS1 / Production host: Rhodobacter capsulatus (bacteria) / Strain (production host): pMTS1/MT-RBC1 / References: UniProt: D5ANZ4, UniProt: P0CY49*PLUS
#3: Protein Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP


Mass: 20465.109 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter capsulatus (bacteria)
Description: The strain pMTS1/MT-RBC1 corresponds to a deletion strain MT-RBC1 complemented in trans with the plasmid pMTS1 bearing a wild-type copy of the petABC operon encoding the bc1 complex
Gene: petA, fbcF, RCAP_rcc02768 / Plasmid: pMTS1 / Production host: Rhodobacter capsulatus (bacteria) / Strain (production host): pMTS1/MT-RBC1
References: UniProt: D5ANZ2, UniProt: P0CY48*PLUS, quinol-cytochrome-c reductase

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Non-polymers , 6 types, 15 molecules

#4: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C34H32FeN4O4
#5: Chemical ChemComp-SMA / STIGMATELLIN A


Mass: 514.650 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C30H42O7 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical
ChemComp-UNL / UNKNOWN LIGAND


Mass: 103.120 Da / Num. of mol.: 4 / Source method: obtained synthetically
#7: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#8: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#9: Chemical ChemComp-PG6 / 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE


Mass: 266.331 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H26O6

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Details

Has ligand of interestY

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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: 3.56 Å3/Da / Density % sol: 65.16 % / Description: IRON-SULFUR PROTEINS, HEME PROTEINS
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.2
Details: PEG-400, 0.1 M MgCl2, Heptanetriol, Cacodylate, Undecylmaltoside

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Data collection

Diffraction
IDMean temperature (K)Crystal-IDSerial crystal experiment
11001N
21001N
31001N
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONSSRL BL7-111.08
SYNCHROTRONALS 5.0.221.1
SYNCHROTRONALS 5.0.231.1
Detector
TypeIDDetectorDate
MAR scanner 345 mm plate1IMAGE PLATEMar 14, 2001
ADSC QUANTUM 42CCDMar 20, 2001
ADSC QUANTUM 43CCDMar 21, 2001
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray2
3SINGLE WAVELENGTHMx-ray3
Radiation wavelength
IDWavelength (Å)Relative weight
11.081
21.11
31
ReflectionResolution: 3.5→60 Å / Num. obs: 33596 / % possible obs: 97.6 % / Observed criterion σ(F): -999.9 / Observed criterion σ(I): -3 / Redundancy: 2.68 % / Biso Wilson estimate: 100.43 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 8.5
Reflection shellResolution: 3.5→3.63 Å / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 3.9 / Num. unique obs: 3197 / % possible all: 94

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Processing

Software
NameVersionClassification
PHENIXdev_3885refinement
CNS1.1refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BCC

2bcc


Resolution: 3.51→59.77 Å / SU ML: 0.4762 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 36.1787 / Stereochemistry target values: GeoStd + Monomer Library
RfactorNum. reflection% reflectionSelection details
Rfree0.2887 1656 4.99 %RANDOM
Rwork0.2207 31549 --
obs0.224 33205 96.46 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 119.7 Å2
Refinement stepCycle: LAST / Resolution: 3.51→59.77 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13482 0 419 0 13901
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.018714392
X-RAY DIFFRACTIONf_angle_d2.18719719
X-RAY DIFFRACTIONf_chiral_restr0.08522066
X-RAY DIFFRACTIONf_plane_restr0.01182473
X-RAY DIFFRACTIONf_dihedral_angle_d21.53624968
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2PX-RAY DIFFRACTIONcartesian NCS0.0653330298357
ens_2d_2PX-RAY DIFFRACTIONcartesian NCS0.0885304613588
ens_3d_2PX-RAY DIFFRACTIONcartesian NCS0.0805749409682
ens_4d_2QX-RAY DIFFRACTIONcartesian NCS0.0682611329592
ens_5d_2QX-RAY DIFFRACTIONcartesian NCS0.079575772411
ens_6d_2QX-RAY DIFFRACTIONcartesian NCS0.066797928901
ens_7d_2QX-RAY DIFFRACTIONcartesian NCS0.1496511568
ens_8d_2QX-RAY DIFFRACTIONcartesian NCS0.0756510398254
ens_9d_2QX-RAY DIFFRACTIONcartesian NCS0.07510838443
ens_10d_2QX-RAY DIFFRACTIONcartesian NCS0.0693718727455
ens_11d_2RX-RAY DIFFRACTIONcartesian NCS0.0624369614808
ens_12d_2RX-RAY DIFFRACTIONcartesian NCS0.0595744219526
ens_13d_2RX-RAY DIFFRACTIONcartesian NCS0.0728131768225
ens_14d_2RX-RAY DIFFRACTIONcartesian NCS0.0825896710096
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.51-3.610.38021120.25972199X-RAY DIFFRACTION81.6
3.61-3.730.37991370.27392535X-RAY DIFFRACTION93.3
3.73-3.860.29291260.25222578X-RAY DIFFRACTION93.6
3.86-4.010.33981270.23862558X-RAY DIFFRACTION95.11
4.01-4.20.29981380.22322631X-RAY DIFFRACTION96.48
4.2-4.420.29641480.2122665X-RAY DIFFRACTION98.6
4.42-4.690.3041560.19762699X-RAY DIFFRACTION99.48
4.69-5.060.26491440.19512713X-RAY DIFFRACTION99.9
5.06-5.570.25341190.18532756X-RAY DIFFRACTION99.97
5.57-6.370.30541460.20362725X-RAY DIFFRACTION99.93
6.37-8.020.25591460.22282730X-RAY DIFFRACTION100
8.02-59.770.26841570.23142760X-RAY DIFFRACTION99.39

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