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- PDB-3zry: Rotor architecture in the F(1)-c(10)-ring complex of the yeast F-... -

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Basic information

Entry
Database: PDB / ID: 3zry
TitleRotor architecture in the F(1)-c(10)-ring complex of the yeast F-ATP synthase
Components
  • (ATP SYNTHASE SUBUNIT ...) x 5
  • ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT
KeywordsHYDROLASE / ATP-BINDING / F(1)-F(O)ATP SYNTHASE / MITOCHONDRIA / MOLECULAR MOTOR / CENTRAL STALK / MEMBRANE PROTEIN / C-RING
Function / homology
Function and homology information


mitochondrial proton-transporting ATP synthase, central stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) ...mitochondrial proton-transporting ATP synthase, central stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / 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 / mitochondrial intermembrane space / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / cytosol
Similarity search - Function
: / Fungal epsilon subunit of F1F0-ATP synthase C-terminal domain / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C ...: / Fungal epsilon subunit of F1F0-ATP synthase C-terminal domain / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / 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 / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / 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. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / ATP synthase catalytic sector F1 epsilon subunit / ATP synthase subunit beta, mitochondrial / ATP synthase subunit alpha, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit 9, mitochondrial / ATP synthase subunit delta, mitochondrial
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 6.5 Å
AuthorsGiraud, M.-F. / Dautant, A.
Citation
Journal: J.Struct.Biol. / Year: 2012
Title: Rotor Architecture in the Yeast and Bovine F(1)-C-Ring Complexes of F-ATP Synthase.
Authors: Giraud, M.-F. / Paumard, P. / Sanchez, C. / Brethes, D. / Velours, J. / Dautant, A.
#1: Journal: J.Biol.Chem. / Year: 2010
Title: Crystal Structure of the Mgadp-Inhibited State of the Yeast F1C10-ATP Synthase.
Authors: Dautant, A. / Velours, J. / Giraud, M.
#2: Journal: J.Bioenerg.Biomembr. / Year: 2009
Title: Hydrogenated and Fluorinated Surfactants Derived from Tris(Hydroxymethyl)-Acrylamidomethane Allow the Purification of a Highly Active Yeast F1-F0 ATP-Synthase with an Enhanced Stability.
Authors: Talbot, J.-C. / Dautant, A. / Polidori, A. / Pucci, B. / Cohen-Bouhacina, T. / Maali, A. / Salin, B. / Brethes, D. / Velours, J. / Giraud, M.-F.
#3: Journal: Science / Year: 1999
Title: Molecular Architecture of the Rotary Motor in ATP Synthase
Authors: Stock, D. / Leslie, A.G.W. / Walker, J.E.
#4: Journal: Embo J. / Year: 2006
Title: Novel Features of the Rotary Catalytic Mechanism Revealed in the Structure of Yeast F1 ATPase
Authors: Kabaleeswaran, V. / Puri, N. / Walker, J.E. / Leslie, A.G. / Mueller, D.M.
History
DepositionJun 21, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 18, 2012Provider: repository / Type: Initial release
Revision 1.1Feb 29, 2012Group: Other
Revision 2.0Jan 23, 2019Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Other
Category: atom_site / database_PDB_caveat ...atom_site / database_PDB_caveat / pdbx_database_proc / pdbx_database_status / pdbx_validate_chiral
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.pdbx_auth_atom_name / _pdbx_database_status.recvd_author_approval
Revision 2.1Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_sheet / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.pdbx_dist_value / _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_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_sheet.number_strands / _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 0-STRANDED BARREL THIS IS REPRESENTED BY A 1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-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: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
B: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
D: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
E: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
F: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
G: ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
H: ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
I: ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT
J: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
K: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
L: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
M: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
N: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
O: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
P: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
Q: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
R: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
S: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)450,70729
Polymers448,05419
Non-polymers2,65310
Water0
1
A: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
B: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
D: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
E: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
F: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
G: ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
H: ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
I: ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)373,08319
Polymers370,4309
Non-polymers2,65310
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area39660 Å2
ΔGint-196.6 kcal/mol
Surface area118770 Å2
MethodPISA
2
J: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
K: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
L: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
M: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
N: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
O: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
P: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
Q: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
R: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
S: ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL


Theoretical massNumber of molelcules
Total (without water)77,62410
Polymers77,62410
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30090 Å2
ΔGint-370.8 kcal/mol
Surface area25440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.690, 174.910, 164.260
Angle α, β, γ (deg.)90.00, 93.92, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN J AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
211CHAIN K AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
311CHAIN L AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
411CHAIN M AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
511CHAIN N AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
611CHAIN O AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
711CHAIN P AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
811CHAIN Q AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
911CHAIN R AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
1011CHAIN S AND (RESID 1:34 OR RESID 44:76) AND (NAME C OR NAME CA OR NAME CB OR NAME C OR NAME O)
DetailsBIOMOLECULE 1 IS THE CATALYTIC SECTOR F1, BIOMOLECULE 2 IS THE MEMBRANE ROTOR C(10)-RING.

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Components

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ATP SYNTHASE SUBUNIT ... , 5 types, 18 molecules ABCDEFGHJKLMNOPQRS

#1: Protein ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL /


Mass: 55007.402 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P07251
#2: Protein ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL /


Mass: 51181.082 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A
References: UniProt: P00830, H+-transporting two-sector ATPase
#3: Protein ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL / / F-ATPASE GAMMA SUBUNIT


Mass: 30657.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P38077
#4: Protein ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL / / F-ATPASE DELTA SUBUNIT


Mass: 14565.385 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A
References: UniProt: Q12165, H+-transporting two-sector ATPase
#6: Protein
ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL / / LIPID-BINDING PROTEIN / OLIGOMYCIN RESISTANCE PROTEIN 1


Mass: 7762.375 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: P61829

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Protein , 1 types, 1 molecules I

#5: Protein ATP SYNTHASE CATALYTIC SECTOR F1 EPSILON SUBUNIT / ATP SYNTHASE SUBUNIT EPSILON / MITOCHONDRIAL


Mass: 6642.381 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain: D273-10B/A / References: UniProt: E9P9X4

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Non-polymers , 2 types, 10 molecules

#7: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg

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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: 3.5 Å3/Da / Density % sol: 65 % / Description: NONE
Crystal growpH: 6.5
Details: 10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 ...Details: 10% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM HEPES PH 6.5 MIXED 1:1 WITH PROTEIN SOLUTION (10 MG/ML) CONTAINING 0.64 MM DDM, 25 MM TRIS PH 8.0, 100 MM SODIUM CHLORIDE, 25 MM TREHALOSE, 0.5 MM EDTA, 3 MM SODIUM AZIDE, 2 MM MAGNESIUM CHLORIDE, 0.04 MM ADP, 1 MM AMP-PNP, 0.1 MM DCCD, 2.5 MM DTT, 0.5 MM PMSF.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726
DetectorType: MARRESEARCH / Detector: CCD / Date: Feb 7, 2010 / Details: MIRRORS
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 6.5→54.62 Å / Num. obs: 11687 / % possible obs: 96.6 % / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Biso Wilson estimate: 274.5 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 8.9
Reflection shellResolution: 6.5→6.85 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.92 / Mean I/σ(I) obs: 1.8 / % possible all: 97.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2XOK

2xok


Resolution: 6.5→54.625 Å / SU ML: 1.32 / σ(F): 1.37 / Phase error: 34.96 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3387 559 4.8 %
Rwork0.3168 --
obs0.3178 11669 96.59 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 209.6 Å2 / ksol: 0.276 e/Å3
Displacement parametersBiso mean: 309.874 Å2
Baniso -1Baniso -2Baniso -3
1--15.0914 Å20 Å237.0521 Å2
2---56.6941 Å20 Å2
3---71.7855 Å2
Refinement stepCycle: LAST / Resolution: 6.5→54.625 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29940 0 160 0 30100
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00330542
X-RAY DIFFRACTIONf_angle_d0.94441417
X-RAY DIFFRACTIONf_dihedral_angle_d17.56411256
X-RAY DIFFRACTIONf_chiral_restr0.0754960
X-RAY DIFFRACTIONf_plane_restr0.0025312
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11J240X-RAY DIFFRACTIONPOSITIONAL
12K240X-RAY DIFFRACTIONPOSITIONAL0.064
13L240X-RAY DIFFRACTIONPOSITIONAL0.001
14M240X-RAY DIFFRACTIONPOSITIONAL0.001
15N240X-RAY DIFFRACTIONPOSITIONAL0.001
16O244X-RAY DIFFRACTIONPOSITIONAL0.037
17P244X-RAY DIFFRACTIONPOSITIONAL0.001
18Q244X-RAY DIFFRACTIONPOSITIONAL0.067
19R244X-RAY DIFFRACTIONPOSITIONAL0.001
110S244X-RAY DIFFRACTIONPOSITIONAL0.001
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
6.5005-7.15330.34161370.33262783X-RAY DIFFRACTION97
7.1533-8.18550.34641560.29772749X-RAY DIFFRACTION97
8.1855-10.30150.26681260.2362788X-RAY DIFFRACTION97
10.3015-54.62710.37621400.37232790X-RAY DIFFRACTION96

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