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- PDB-5bw9: Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form -

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Basic information

Entry
Database: PDB / ID: 5bw9
TitleCrystal Structure of Yeast V1-ATPase in the Autoinhibited Form
Components
  • (V-type proton ATPase subunit ...) x 5
  • V-type proton ATPase catalytic subunit A
KeywordsHYDROLASE / Autoinhibition
Function / homology
Function and homology information


vacuole-mitochondrion membrane contact site / Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proteasome storage granule assembly / pexophagy / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain ...vacuole-mitochondrion membrane contact site / Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / proteasome storage granule assembly / pexophagy / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase complex / intron homing / protein metabolic process / intein-mediated protein splicing / fungal-type vacuole membrane / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification / ATP metabolic process / H+-transporting two-sector ATPase / proton transmembrane transport / Neutrophil degranulation / phagocytic vesicle / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / transmembrane transport / cytoplasmic stress granule / intracellular calcium ion homeostasis / endonuclease activity / Hydrolases; Acting on ester bonds / Golgi membrane / mRNA binding / ATP hydrolysis activity / DNA binding / ATP binding / cytoplasm
Similarity search - Function
Homing endonuclease PI-Sce / Homing endonuclease / Hom-end-associated Hint / Hom_end-associated Hint / ATPase, V1 complex, subunit H / ATPase, V1 complex, subunit H, C-terminal / ATPase, V1 complex, subunit H, C-terminal domain superfamily / V-ATPase subunit H / V-ATPase subunit H / Vacuolar (H+)-ATPase G subunit ...Homing endonuclease PI-Sce / Homing endonuclease / Hom-end-associated Hint / Hom_end-associated Hint / ATPase, V1 complex, subunit H / ATPase, V1 complex, subunit H, C-terminal / ATPase, V1 complex, subunit H, C-terminal domain superfamily / V-ATPase subunit H / V-ATPase subunit H / Vacuolar (H+)-ATPase G subunit / Vacuolar (H+)-ATPase G subunit / ATPase, V1 complex, subunit B / Intein / Intein DOD homing endonuclease / Intein DOD-type homing endonuclease domain profile. / Intein C-terminal splicing region / Intein C-terminal splicing motif profile. / Hint domain C-terminal / Hint (Hedgehog/Intein) domain C-terminal region / V-type ATPase subunit E / V-type ATPase subunit E, C-terminal domain superfamily / ATP synthase (E/31 kDa) subunit / ATPase, V1 complex, subunit D / Intein N-terminal splicing region / ATP synthase subunit D / Intein N-terminal splicing motif profile. / Hint domain N-terminal / Hint (Hedgehog/Intein) domain N-terminal region / Homing endonuclease / Hint domain superfamily / V-type ATP synthase regulatory subunit B/beta / V-type ATP synthase catalytic alpha chain / ATPsynthase alpha/beta subunit, N-terminal extension / ATPsynthase alpha/beta subunit N-term extension / 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 / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
V-type proton ATPase subunit B / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit E / V-type proton ATPase subunit D / V-type proton ATPase subunit H / V-type proton ATPase subunit G
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 7 Å
AuthorsOot, R.A. / Kane, P.M. / Berry, E.A. / Wilkens, S.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM058600 United States
CitationJournal: Embo J. / Year: 2016
Title: Crystal structure of yeast V1-ATPase in the autoinhibited state.
Authors: Oot, R.A. / Kane, P.M. / Berry, E.A. / Wilkens, S.
History
DepositionJun 6, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 8, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2016Group: Database references
Revision 1.2Aug 17, 2016Group: Database references
Revision 1.3Sep 20, 2017Group: Author supporting evidence / Database references / Derived calculations
Category: citation / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 27, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: V-type proton ATPase catalytic subunit A
B: V-type proton ATPase catalytic subunit A
C: V-type proton ATPase catalytic subunit A
D: V-type proton ATPase subunit B
E: V-type proton ATPase subunit B
F: V-type proton ATPase subunit B
H: V-type proton ATPase subunit H
G: V-type proton ATPase subunit D
J: V-type proton ATPase subunit G
I: V-type proton ATPase subunit E
K: V-type proton ATPase subunit E
L: V-type proton ATPase subunit G
M: V-type proton ATPase subunit E
N: V-type proton ATPase subunit G
h: V-type proton ATPase subunit H
g: V-type proton ATPase subunit D
i: V-type proton ATPase subunit E
j: V-type proton ATPase subunit G
l: V-type proton ATPase subunit G
k: V-type proton ATPase subunit E
a: V-type proton ATPase catalytic subunit A
b: V-type proton ATPase catalytic subunit A
c: V-type proton ATPase catalytic subunit A
d: V-type proton ATPase subunit B
e: V-type proton ATPase subunit B
f: V-type proton ATPase subunit B
m: V-type proton ATPase subunit E
n: V-type proton ATPase subunit G


Theoretical massNumber of molelcules
Total (without water)1,162,56928
Polymers1,162,56928
Non-polymers00
Water00
1
A: V-type proton ATPase catalytic subunit A
B: V-type proton ATPase catalytic subunit A
C: V-type proton ATPase catalytic subunit A
D: V-type proton ATPase subunit B
E: V-type proton ATPase subunit B
F: V-type proton ATPase subunit B
H: V-type proton ATPase subunit H
G: V-type proton ATPase subunit D
J: V-type proton ATPase subunit G
I: V-type proton ATPase subunit E
K: V-type proton ATPase subunit E
L: V-type proton ATPase subunit G
M: V-type proton ATPase subunit E
N: V-type proton ATPase subunit G


Theoretical massNumber of molelcules
Total (without water)581,28414
Polymers581,28414
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
h: V-type proton ATPase subunit H
g: V-type proton ATPase subunit D
i: V-type proton ATPase subunit E
j: V-type proton ATPase subunit G
l: V-type proton ATPase subunit G
k: V-type proton ATPase subunit E
a: V-type proton ATPase catalytic subunit A
b: V-type proton ATPase catalytic subunit A
c: V-type proton ATPase catalytic subunit A
d: V-type proton ATPase subunit B
e: V-type proton ATPase subunit B
f: V-type proton ATPase subunit B
m: V-type proton ATPase subunit E
n: V-type proton ATPase subunit G


Theoretical massNumber of molelcules
Total (without water)581,28414
Polymers581,28414
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)468.479, 159.740, 245.040
Angle α, β, γ (deg.)90.000, 113.880, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain a
12chain B
22chain b
13chain C
23chain c
14chain D
24chain d
15chain E
25chain e
16chain F
26chain f
17chain G
27chain g
18chain H
28chain h
19chain I
29chain i
110chain J
210chain j
111chain K
211chain k
112chain L
212chain l
113chain M
213chain m
114chain N
214chain n

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUGLUGLUchain AAA24 - 61424 - 614
21GLUGLUGLUGLUchain aaU24 - 61424 - 614
12HISHISALAALAchain BBB20 - 61320 - 613
22TYRTYRALAALAchain bbV25 - 61325 - 613
13ALAALAGLNGLNchain CCC21 - 60921 - 609
23GLUGLUGLNGLNchain ccW24 - 60924 - 609
14ASNASNASPASPchain DDD27 - 48627 - 486
24ASNASNASPASPchain ddX27 - 48627 - 486
15ASNASNASPASPchain EEE27 - 48627 - 486
25ASNASNASPASPchain eeY27 - 48627 - 486
16ASNASNASPASPchain FFF27 - 48627 - 486
26PROPROASPASPchain ffZ24 - 48624 - 486
17PHEPHEALAALAchain GGH9 - 2199 - 219
27PHEPHEASPASPchain ggP9 - 2269 - 226
18GLYGLYTHRTHRchain HHG2 - 4762 - 476
28ALAALATHRTHRchain hhO3 - 4763 - 476
19THRTHRGLYGLYchain IIJ9 - 2249 - 224
29LEULEUGLYGLYchain iiQ8 - 2248 - 224
110GLNGLNSERSERchain JJI3 - 10611 - 114
210SERSERVALVALchain jjR2 - 10210 - 110
111LYSLYSGLYGLYchain KKK47 - 22447 - 224
211ASNASNGLYGLYchain kkT57 - 22457 - 224
112ALAALASERSERchain LLL39 - 10647 - 114
212LYSLYSSERSERchain llS41 - 10649 - 114
113ALAALAGLYGLYchain MMM22 - 22422 - 224
213GLUGLUGLYGLYchain mmAA44 - 22444 - 224
114LYSLYSSERSERchain NNN26 - 10634 - 114
214LYSLYSSERSERchain nnBA26 - 10634 - 114

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

NCS oper:
IDCodeMatrixVector
1given(-0.920058, -0.008979, -0.391679), (0.000982, -0.999787, 0.020612), (-0.39178, 0.018579, 0.919871)-49.003899, 106.900002, -11.05
2given(-0.923744, -0.002815, -0.383001), (-0.000454, -0.999964, 0.008446), (-0.383011, 0.007976, 0.923709)-49.817699, 107.314003, -9.42829
3given(-0.919825, -0.009386, -0.392217), (0.003477, -0.99987, 0.015772), (-0.392313, 0.013144, 0.919738)-48.783001, 107.679001, -10.5694
4given(-0.916825, -0.007656, -0.399216), (0.000496, -0.999837, 0.018035), (-0.399289, 0.016336, 0.916679)-48.371601, 107.064003, -11.3326
5given(-0.919681, -0.005667, -0.392626), (0.001223, -0.999932, 0.011567), (-0.392665, 0.010158, 0.919625)-49.0131, 107.230003, -10.721
6given(-0.919685, -0.006626, -0.392601), (0.001844, -0.999919, 0.012556), (-0.392653, 0.010824, 0.919623)-48.918301, 107.751999, -10.5371
7given(-0.922559, -0.007054, -0.385791), (0.003777, -0.99995, 0.009251), (-0.385837, 0.007078, 0.92254)-49.373501, 108.391998, -9.85751
8given(-0.911701, 0.00554, -0.410817), (-0.004742, -0.999984, -0.00296), (-0.410827, -0.000751, 0.911713)-49.413898, 108.688004, -10.2542
9given(-0.917568, -0.016243, -0.397246), (0.018141, -0.999835, -0.001019), (-0.397164, -0.008141, 0.917712)-47.852798, 109.706001, -9.81481
10given(-0.92344, -0.004877, -0.383711), (0.011033, -0.999843, -0.013846), (-0.383583, -0.017019, 0.923349)-50.598099, 109.813004, -9.07866
11given(-0.924153, 0.001314, -0.382019), (-0.013997, -0.999439, 0.030422), (-0.381765, 0.033462, 0.923654)-50.467499, 104.574997, -10.4568
12given(-0.941863, 1.32915, -0.382019), (-0.002886, -0.999963, 0.008052), (-0.335985, 0.008554, 0.941828)-54.7215, 107.138, -2.15803
13given(-0.918851, -0.00916, -0.394498), (0.00139, -0.999799, 0.019977), (-0.394602, 0.017808, 0.91868)-48.610401, 107.261002, -11.5046
14given(-0.925094, -0.004257, -0.379715), (-0.002651, -0.99984, 0.01767), (-0.37973, 0.017353, 0.924935)-49.318401, 107.300003, -10.2207

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Components

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Protein , 1 types, 6 molecules ABCabc

#1: Protein
V-type proton ATPase catalytic subunit A / V-ATPase subunit A / Vacuolar proton pump subunit A


Mass: 67796.508 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c
References: UniProt: P17255, H+-transporting two-sector ATPase, Hydrolases; Acting on ester bonds

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V-type proton ATPase subunit ... , 5 types, 22 molecules DEFdefHhGgJLNjlnIKMikm

#2: Protein
V-type proton ATPase subunit B / V-ATPase subunit B / V-ATPase 57 kDa subunit / Vacuolar proton pump subunit B


Mass: 57815.023 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c / References: UniProt: P16140
#3: Protein V-type proton ATPase subunit H / V-ATPase subunit H / V-ATPase 54 kDa subunit / Vacuolar proton pump subunit H


Mass: 54482.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c / References: UniProt: P41807
#4: Protein V-type proton ATPase subunit D / V-ATPase subunit D / Vacuolar proton pump subunit D


Mass: 29235.023 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c / References: UniProt: P32610
#5: Protein
V-type proton ATPase subunit G / V-ATPase subunit G / V-ATPase 13 kDa subunit / Vacuolar proton pump subunit G


Mass: 13735.680 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c / References: UniProt: P48836
#6: Protein
V-type proton ATPase subunit E / V-ATPase subunit E / V-ATPase 27 kDa subunit / Vacuolar proton pump subunit E


Mass: 26508.393 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Variant: vma5 delete / Strain: ATCC 204508 / S288c / References: UniProt: P22203

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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: 3.63 Å3/Da / Density % sol: 66.13 %
Crystal growTemperature: 291 K / Method: microfluidic / pH: 7.5
Details: 9.5 % PEG 8k, 150mM Ammonium Sulfate, 100mM HEPES, 12.5mM MgCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.9782 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 22, 2015
RadiationMonochromator: Si (111) crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9782 Å / Relative weight: 1
ReflectionResolution: 7→40.0101 Å / Num. obs: 26115 / % possible obs: 100 % / Redundancy: 8.5 % / Biso Wilson estimate: 402.94 Å2 / Rmerge(I) obs: 0.189 / Rpim(I) all: 0.094 / Rrim(I) all: 0.201 / Χ2: 1.397 / Net I/av σ(I): 9.569 / Net I/σ(I): 4.7 / Num. measured all: 222178
Reflection shell

Diffraction-ID: 1 / Rejects: _ / % possible all: 100

Resolution (Å)Redundancy (%)Num. unique allCC1/2Rpim(I) allΧ2Rmerge(I) obsRrim(I) all
7-7.128.412930.3550.8211.493
7.12-7.258.413120.3480.7171.482
7.25-7.398.612640.4560.6041.461
7.39-7.548.513280.4890.5821.485
7.54-7.78.612940.5780.4721.457
7.7-7.888.512900.6640.3951.497
7.88-8.078.612940.7370.3181.5040.8760.933
8.07-8.298.612870.8480.2291.4820.630.671
8.29-8.538.613020.9120.1831.4520.5020.535
8.53-8.88.613180.9330.1491.4630.4120.438
8.8-9.118.612930.9610.1131.4040.3120.332
9.11-9.488.612790.9840.0871.3780.240.255
9.48-9.98.613170.9790.0781.4090.2160.23
9.9-10.418.613010.9880.0631.3340.1740.186
10.41-11.058.613030.990.0551.3330.1530.162
11.05-11.898.513130.9910.051.2870.1380.147
11.89-13.048.513220.9910.051.2850.1360.145
13.04-14.858.513090.9890.0461.2620.1250.133
14.85-18.48.413310.9930.0441.2650.1210.129
18.4-408.113650.9940.0351.220.0930.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: dev_1957)refinement
HKL-2000data reduction
PHASERphasing
PDB_EXTRACT3.15data extraction
SCALEPACKdata scaling
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3vr5 chains A,B,C,D,E,F

3vr5


Resolution: 7→40.101 Å / SU ML: 1.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.41 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.309 1998 7.66 %Random selection
Rwork0.2604 24089 --
obs0.2642 26087 99.27 %-
Solvent computationShrinkage radii: 2 Å / VDW probe radii: 2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 790.13 Å2 / Biso mean: 290.9011 Å2 / Biso min: 50.74 Å2
Refinement stepCycle: final / Resolution: 7→40.101 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms44760 0 0 0 44760
Num. residues----9074
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00144720
X-RAY DIFFRACTIONf_angle_d0.42362178
X-RAY DIFFRACTIONf_chiral_restr0.0288464
X-RAY DIFFRACTIONf_plane_restr0.0019034
X-RAY DIFFRACTIONf_dihedral_angle_d2.5049034
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2905X-RAY DIFFRACTIONPOSITIONAL0.007
12a2905X-RAY DIFFRACTIONPOSITIONAL0.007
21B2895X-RAY DIFFRACTIONPOSITIONAL0.002
22b2895X-RAY DIFFRACTIONPOSITIONAL0.002
31C2880X-RAY DIFFRACTIONPOSITIONAL0.01
32c2880X-RAY DIFFRACTIONPOSITIONAL0.01
41D2250X-RAY DIFFRACTIONPOSITIONAL0.004
42d2250X-RAY DIFFRACTIONPOSITIONAL0.004
51E2231X-RAY DIFFRACTIONPOSITIONAL0.001
52e2231X-RAY DIFFRACTIONPOSITIONAL0.001
61F2197X-RAY DIFFRACTIONPOSITIONAL0.003
62f2197X-RAY DIFFRACTIONPOSITIONAL0.003
71G666X-RAY DIFFRACTIONPOSITIONAL0.002
72g666X-RAY DIFFRACTIONPOSITIONAL0.002
81H2208X-RAY DIFFRACTIONPOSITIONAL0.007
82h2208X-RAY DIFFRACTIONPOSITIONAL0.007
91I1073X-RAY DIFFRACTIONPOSITIONAL0.002
92i1073X-RAY DIFFRACTIONPOSITIONAL0.002
101J494X-RAY DIFFRACTIONPOSITIONAL0.001
102j494X-RAY DIFFRACTIONPOSITIONAL0.001
111K833X-RAY DIFFRACTIONPOSITIONAL0.001
112k833X-RAY DIFFRACTIONPOSITIONAL0.001
121L325X-RAY DIFFRACTIONPOSITIONAL0.002
122l325X-RAY DIFFRACTIONPOSITIONAL0.002
131M898X-RAY DIFFRACTIONPOSITIONAL0.001
132m898X-RAY DIFFRACTIONPOSITIONAL0.001
141N288X-RAY DIFFRACTIONPOSITIONAL0.002
142n288X-RAY DIFFRACTIONPOSITIONAL0.002
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
7-7.17410.38261280.33441555168391
7.1741-7.3670.38891430.312317181861100
7.367-7.58230.4071430.308817301873100
7.5823-7.82530.37441410.291916941835100
7.8253-8.10280.32731430.277417231866100
8.1028-8.42440.3011440.252317341878100
8.4244-8.80390.28561430.227217331876100
8.8039-9.26270.26291420.218417081850100
9.2627-9.8350.26041450.194117491894100
9.835-10.58140.27861440.198117301874100
10.5814-11.62270.25411430.195717281871100
11.6227-13.25110.26741450.220417471892100
13.2511-16.49920.28861460.286417461892100
16.4992-40.10120.42011480.404317941942100

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