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- PDB-1efr: BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIO... -

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Basic information

Entry
Database: PDB / ID: 1efr
TitleBOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
Components
  • (BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ...) x 3
  • EFRAPEPTIN C
KeywordsHYDROLASE/ANTIBIOTIC / ANTIBIOTIC / ATP PHOSPHORYLASE / HYDROGEN ION TRANSPORT / ATP SYNTHASE / F1-ATPASE / IONOPHORE / HYDROLASE-ANTIBIOTIC COMPLEX / EFRAPEPTIN / F1-ATPASE-ANTIBIOTIC COMPLEX
Function / homology
Function and homology information


Formation of ATP by chemiosmotic coupling / Cristae formation / : / : / Mitochondrial protein degradation / : / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase ...Formation of ATP by chemiosmotic coupling / Cristae formation / : / : / Mitochondrial protein degradation / : / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, gamma subunit, helix hairpin domain / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit ...ATP synthase alpha/beta chain, C-terminal domain / Lysin / Thrombin, subunit H - #170 / Elongation Factor Tu (Ef-tu); domain 3 - #20 / Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3 / Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3 / ATP synthase, gamma subunit, helix hairpin domain / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / Elongation Factor Tu (Ef-tu); domain 3 / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Helix Hairpins / Thrombin, subunit H / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Up-down Bundle / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
EFRAPEPTIN C / ADENOSINE-5'-DIPHOSPHATE / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / ATP synthase subunit beta, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit alpha, mitochondrial
Similarity search - Component
Biological speciesTOLYPOCLADIUM INFLATUM (fungus)
BOS TAURUS (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsAbrahams, J.P. / Buchanan, S.K. / Van Raaij, M.J. / Fearnley, I.M. / Leslie, A.G.W. / Walker, J.E.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: The Structure of Bovine F1-ATPase Complexed with the Peptide Antibiotic Efrapeptin.
Authors: Abrahams, J.P. / Buchanan, S.K. / Van Raaij, M.J. / Fearnley, I.M. / Leslie, A.G. / Walker, J.E.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: The Structure of Bovine F1-ATPase Complexed with the Antibiotic Inhibitor Aurovertin B
Authors: Van Raaij, M.J. / Abrahams, J.P. / Leslie, A.G. / Walker, J.E.
#2: Journal: Nature / Year: 1994
Title: Structure at 2.8 A Resolution of F1-ATPase from Bovine Heart Mitochondria
Authors: Abrahams, J.P. / Leslie, A.G. / Lutter, R. / Walker, J.E.
#3: Journal: J.Mol.Biol. / Year: 1993
Title: Crystallization of F1-ATPase from Bovine Heart Mitochondria
Authors: Lutter, R. / Abrahams, J.P. / Van Raaij, M.J. / Todd, R.J. / Lundqvist, T. / Buchanan, S.K. / Leslie, A.G. / Walker, J.E.
#4: Journal: Embo J. / Year: 1993
Title: Inherent Asymmetry of the Structure of F1-ATPase from Bovine Heart Mitochondria at 6.5 A Resolution
Authors: Abrahams, J.P. / Lutter, R. / Todd, R.J. / Van Raaij, M.J. / Leslie, A.G. / Walker, J.E.
History
DepositionMay 24, 1996Processing site: BNL
Revision 1.0Feb 12, 1997Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 27, 2011Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary
Revision 1.4Dec 12, 2012Group: Other
Revision 1.5Nov 1, 2017Group: Advisory / Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly / pdbx_unobs_or_zero_occ_residues
Item: _pdbx_database_status.process_site / _pdbx_struct_assembly.method_details
Revision 1.6Aug 9, 2023Group: Advisory / Database references ...Advisory / Database references / Derived calculations / Refinement description
Category: database_2 / pdbx_initial_refinement_model ...database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues / struct_conn / struct_conn_type / struct_ref_seq / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.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.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
B: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
C: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
D: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT BETA
E: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT BETA
F: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT BETA
G: BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT GAMMA
Q: EFRAPEPTIN C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)355,53118
Polymers352,9588
Non-polymers2,57410
Water9,638535
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area39290 Å2
ΔGint-198.6 kcal/mol
Surface area101930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)285.700, 107.400, 139.500
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ... , 3 types, 7 molecules ABCDEFG

#1: Protein BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA / F1-ATPASE


Mass: 55302.191 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Organelle: MITOCHONDRION / Tissue: MUSCLE / References: UniProt: P19483, EC: 3.6.1.34
#2: Protein BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT BETA / F1-ATPASE


Mass: 51757.836 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Organelle: MITOCHONDRION / Tissue: MUSCLE / References: UniProt: P00829, EC: 3.6.1.34
#3: Protein BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT GAMMA / F1-ATPASE


Mass: 30185.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: HEART / Organelle: MITOCHONDRION / Tissue: MUSCLE / References: UniProt: P05631, EC: 3.6.1.34

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Protein/peptide , 1 types, 1 molecules Q

#4: Protein/peptide EFRAPEPTIN C


Type: Polypeptide / Class: Antimicrobial / Mass: 1592.068 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: EFRAPEPTIN C IS A LINEAR PEPTIDE, WITH ACETYLATED (ACE) PIPECOLIC ACID (YCP) AT THE N-TERMINUS AND A MODIFIED LEUCINE AT THE C-TERM (TLX)
Source: (gene. exp.) TOLYPOCLADIUM INFLATUM (fungus) / References: EFRAPEPTIN C, UniProt: P05631*PLUS

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Non-polymers , 4 types, 545 molecules

#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#7: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 535 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsTHE F1-ATPASE MOLECULE HAS THREE COPIES OF THE NON-CATALYTIC ALPHA SUBUNIT AND THREE COPIES OF THE ...THE F1-ATPASE MOLECULE HAS THREE COPIES OF THE NON-CATALYTIC ALPHA SUBUNIT AND THREE COPIES OF THE CATALYTIC BETA SUBUNIT. IN THE FIRST REFERENCE (ABRAHAMS ET AL., 1994), THE BETA SUBUNITS WERE LABELLED ACCORDING TO THE BOUND NUCLEOTIDE, AS BETA(DP) (BINDS ADP), BETA(E) (NO BOUND NUCLEOTIDE) AND BETA(TP) (AMPPNP BOUND). THE ALPHA SUBUNITS (WHICH ALL BIND AMPPNP) CONTRIBUTE TO THE CATALYTIC SITES OF THE BETA SUBUNITS, AND HAVE BEEN LABELLED ACCORDINGLY. THUS ALPHA (DP) CONTRIBUTES TO THE CATALYTIC SITE ON BETA(DP), ALPHA (TP) TO THE SITE ON BETA(TP) AND ALPHA(E) TO THE SITE ON BETA(E). ATP SYNTHASE IS AN MULTI-SUBUNIT PROTEIN WHICH CAN BE READILY DISSOCIATED INTO A SOLUBLE FRAGMENT WITH ATPASE ACTIVITY (F1-ATPASE) AND A MEMBRANE BOUND FRAGMENT (FO) WHICH CONTAINS A PROTON CHANNEL. EFRAPEPTIN C IS A MEMBER OF CLOSELY RELATED LINEAR AMPHIPHILIC PEPTIDE ANTIBIOTICS. MEMBERS OF THIS FAMILY HAVE AN ACETYLATED PIPECOLIC AT THE N-TERM AND AT THE C-TERM A MODIFIED LEUCINE WITH AN ATTACHED HETEROCYCLIC RING STRUCTURE. HERE, EFRAPEPTIN C IS REPRESENTED BY THE SEQUENCE (SEQRES)

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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: 3.03 Å3/Da / Density % sol: 54 % / Description: THE CRYOPROTECTANT WAS 20% (W/V) GLYCEROL.
Crystal growpH: 8.2 / Details: PH 8.2
Crystal grow
*PLUS
Temperature: 22-24 ℃ / pH: 7.2 / Method: microdialysis / Details: Lutter, R., (1993) J.Mol.Biol., 229, 787.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
199.9 %deuterium oxide11
2100 mMTris-HCl11*
314 %(w/v)PEG600011
4400 mMsodium chloride11*
52 mMEDTA11*
60.04 %(w/v)sodium azide11*
70.02 %(w/v)PMSF11*
810 mMdithiothreitol11*
920 mMmagnesium sulphate12
108 mMmagnesium chloride11
110.500 mMAMP-PNP11*
120.010 mMADP11*
139 %(w/v)PEG600012
145 mM2-mercaptoethanol12
15* solutions12half of concentration * solutions

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: May 4, 1995
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.87 Å / Relative weight: 1
ReflectionNum. obs: 68961 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 2.6 % / Rmerge(I) obs: 0.079
Reflection shellResolution: 3.1→3.35 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.152 / % possible all: 83
Reflection
*PLUS
Highest resolution: 3.1 Å / Lowest resolution: 5.5 Å
Reflection shell
*PLUS
% possible obs: 83 %

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Processing

Software
NameVersionClassification
CCP4model building
TNTrefinement
MOSFLMdata reduction
CCP4(SCALA)data scaling
CCP4phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1BMF

1bmf


Resolution: 3.1→5.5 Å / Isotropic thermal model: TNT / σ(F): 0 / Stereochemistry target values: STANDARD TNT
Details: FOR THE PURPOSES OF REFINEMENT, AMPPNP WAS MODELED AS ATP THE POSITIONS OF SIDE CHAIN ATOMS WITH TEMPERATURE FACTORS GREATER THAN 75 IS UNCERTAIN. THE MAIN CHAIN CONFORMATION IS ALSO ...Details: FOR THE PURPOSES OF REFINEMENT, AMPPNP WAS MODELED AS ATP THE POSITIONS OF SIDE CHAIN ATOMS WITH TEMPERATURE FACTORS GREATER THAN 75 IS UNCERTAIN. THE MAIN CHAIN CONFORMATION IS ALSO UNCERTAIN FOR REGIONS WITH TEMPERATURE FACTORS ABOVE 60. RESIDUES A 407-408 AND B 402-409 INCLUSIVE HAVE BEEN GIVEN ZERO OCCUPANCY AS THERE WAS NO INTERPRETABLE ELECTRON DENSITY IN THIS REGION. SOLVENT MOLECULES HAVE BEEN USED TO MODEL SOME FEATURES IN THE ELECTRON DENSITY THAT ARE PROBABLY DUE TO THE "MISSING" REGIONS OF THE GAMMA SUBUNIT (CHAIN G). OTHER SOLVENT MOLECULES (SOME WITH UNUSUALLY LOW B VALUES) MODEL OTHER FEATURES IN THE ELECTRON DENSITY WHICH PROBABLY REPRESENT LARGER MOLECULES (EG GLYCEROL) THAT COULD NOT BE IDENTIFIED UNAMBIGUOUSLY AT THE RESOLUTION OF THE ELECTRON DENSITY MAPS. ASP A, B, AND C 270: THE PEPTIDE BOND BETWEEN ASP 269 AND ASP 270 HAS BEEN MODELED IN A CIS CONFORMATION. RESIDUAL FEATURES IN THE ELECTRON DENSITY AND THE STRAINED STEREOCHEMISTRY OF THIS RESIDUE SUGGESTS THAT THERE IS SOME CONFORMATIONAL DISORDER IN THIS RESIDUE. ASN D, E, AND F 257: THE PEPTIDE BOND BETWEEN ASP 256 AND ASN 257 HAS BEEN MODELED IN A CIS CONFORMATION. THE POSITIONS OF SIDE CHAIN ATOMS WITH TEMPERATURE FACTORS GREATER THAN 75 IS UNCERTAIN. THE MAIN CHAIN CONFORMATION IS ALSO UNCERTAIN FOR REGIONS WITH TEMPERATURE FACTORS ABOVE 60. RESIDUES A 407-408 AND B 402
RfactorNum. reflection% reflection
Rfree0.22 692 1.26 %
Rwork0.177 --
obs-54888 -
Refinement stepCycle: LAST / Resolution: 3.1→5.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22836 0 156 535 23527
Refine LS restraints
Refine-IDTypeDev idealNumberWeight
X-RAY DIFFRACTIONt_bond_d0.006233330.8
X-RAY DIFFRACTIONt_angle_deg1.75314481.6
X-RAY DIFFRACTIONt_dihedral_angle_d16.2142671
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes0.0065762
X-RAY DIFFRACTIONt_gen_planes0.00833795
X-RAY DIFFRACTIONt_it3.6231100.3
X-RAY DIFFRACTIONt_nbd0.01652515
X-RAY DIFFRACTIONt_omega_torsion
X-RAY DIFFRACTIONt_other_torsion
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact
Software
*PLUS
Name: TNT / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.177 / Rfactor Rfree: 0.225
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev idealWeight
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_dihedral_angle_deg16.21
X-RAY DIFFRACTIONt_plane_restr0.0085
LS refinement shell
*PLUS
Highest resolution: 3.1 Å / Lowest resolution: 3.35 Å / Rfactor Rfree: 0.275 / Rfactor obs: 0.245

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