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- PDB-5d80: Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form -

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Basic information

Entry
Database: PDB / ID: 5d80
TitleCrystal Structure of Yeast V1-ATPase in the Autoinhibited Form
Components
  • (V-type proton ATPase subunit ...) x 6
  • 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 / protein metabolic process / intein-mediated protein splicing / intron homing / 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 / intracellular calcium ion homeostasis / cytoplasmic stress granule / endonuclease activity / Hydrolases; Acting on ester bonds / Golgi membrane / mRNA binding / ATP hydrolysis activity / DNA binding / ATP binding / membrane / 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 / ATPase, V1 complex, subunit F, eukaryotic / 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 / ATPase, V1 complex, subunit F / ATPase, V1 complex, subunit F superfamily / ATP synthase subunit D / ATP synthase (F/14-kDa) subunit / 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 F / 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: 6.202 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
DepositionAug 14, 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 ...Author supporting evidence / Database references / Derived calculations / Refinement description
Category: citation / pdbx_audit_support ...citation / pdbx_audit_support / pdbx_struct_oper_list / software
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization ..._citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation / _software.classification
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 / software / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _software.name / _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

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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
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
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
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
G: V-type proton ATPase subunit D
g: V-type proton ATPase subunit D
o: V-type proton ATPase subunit F
O: V-type proton ATPase subunit F


Theoretical massNumber of molelcules
Total (without water)1,189,52730
Polymers1,189,52730
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
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
G: V-type proton ATPase subunit D
O: V-type proton ATPase subunit F


Theoretical massNumber of molelcules
Total (without water)594,76415
Polymers594,76415
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
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
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
g: V-type proton ATPase subunit D
o: V-type proton ATPase subunit F


Theoretical massNumber of molelcules
Total (without water)594,76415
Polymers594,76415
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)468.020, 159.650, 248.270
Angle α, β, γ (deg.)90.000, 113.750, 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
115chain O
215chain o

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 aaN24 - 61424 - 614
12HISHISASPASPchain BBB20 - 61720 - 617
22HISHISASPASPchain bbO20 - 61720 - 617
13ALAALAGLNGLNchain CCC21 - 60921 - 609
23ALAALAGLNGLNchain ccP21 - 60921 - 609
14ASNASNASPASPchain DDD27 - 48627 - 486
24ASNASNASPASPchain ddQ27 - 48627 - 486
15ASNASNASPASPchain EEE27 - 48627 - 486
25ASNASNASPASPchain eeR27 - 48627 - 486
16ASNASNASPASPchain FFF27 - 48627 - 486
26ASNASNASPASPchain ffS27 - 48627 - 486
17ASNASNASPASPchain GGAA4 - 2264 - 226
27GLNGLNALAALAchain ggBA7 - 2287 - 228
18GLYGLYTHRTHRchain HHG2 - 4762 - 476
28GLYGLYTHRTHRchain hhT2 - 4762 - 476
19THRTHRGLYGLYchain III9 - 2249 - 224
29THRTHRGLYGLYchain iiV9 - 2249 - 224
110GLNGLNSERSERchain JJH3 - 10611 - 114
210GLNGLNSERSERchain jjU3 - 10611 - 114
111ALAALAGLYGLYchain KKJ22 - 22422 - 224
211LYSLYSGLYGLYchain kkW47 - 22447 - 224
112GLUGLUSERSERchain LLK19 - 10627 - 114
212ALAALASERSERchain llX39 - 10647 - 114
113ALAALAGLYGLYchain MML22 - 22422 - 224
213LEULEUGLYGLYchain mmY17 - 22417 - 224
114LYSLYSSERSERchain NNM26 - 10634 - 114
214SERSERSERSERchain nnZ2 - 10610 - 114
115ALAALAPHEPHEchain OODA2 - 1162 - 116
215ALAALAPHEPHEchain ooCA2 - 1162 - 116

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15

NCS oper:
IDCodeMatrixVector
1given(-0.91267, -0.01111, -0.408546), (0.007704, -0.999921, 0.009981), (-0.408624, 0.005962, 0.912683)-47.189999, 114.261002, -10.6839
2given(-0.921603, -0.004488, -0.388107), (0.003868, -0.99999, 0.002379), (-0.388114, 0.000691, 0.921611)-49.397598, 114.106003, -8.54885
3given(-0.914714, -0.00708, -0.404041), (0.006617, -0.999975, 0.002543), (-0.404048, -0.000347, 0.914738)-47.992599, 114.702003, -9.65686
4given(-0.913586, -0.009464, -0.406536), (0.008348, -0.999955, 0.004518), (-0.40656, 0.000734, 0.913624)-47.597801, 114.580002, -10.0481
5given(-0.920169, -0.007903, -0.391441), (0.00971, -0.999949, -0.002636), (-0.391401, -0.006227, 0.920199)-48.9958, 114.828003, -8.14611
6given(-0.918932, -0.008163, -0.394331), (0.008963, -0.99996, -0.000186), (-0.394314, -0.003705, 0.918968)-48.523399, 114.761002, -8.94947
7given(-0.909713, -0.00368, -0.415222), (-0.002365, -0.999899, 0.014042), (-0.415232, 0.013756, 0.909612)-47.317902, 113.230003, -12.006
8given(-0.908482, 0.001984, -0.417918), (-0.0004, -0.999992, -0.003878), (-0.417923, -0.003356, 0.908476)-48.165901, 114.917999, -10.0169
9given(-0.904204, -0.011051, -0.426957), (0.008363, -0.999932, 0.008169), (-0.427018, 0.003816, 0.904235)-45.123798, 114.546997, -10.722
10given(-0.919872, -0.005516, -0.392179), (0.012353, -0.999812, -0.014913), (-0.392023, -0.018562, 0.919768)-49.6007, 116.330002, -8.91132
11given(-0.91363, 0.006832, -0.40649), (-0.016449, -0.999661, 0.02017), (-0.406214, 0.025114, 0.913433)-48.603401, 110.677002, -11.9032
12given(-0.937143, -0.022018, -0.348249), (0.015417, -0.999645, 0.021715), (-0.348604, 0.014981, 0.937151)-52.281799, 114.762001, -3.22771
13given(-0.911824, -0.013957, -0.410343), (0.010166, -0.999883, 0.011421), (-0.410455, 0.006242, 0.91186)-47.694599, 114.594002, -10.9953
14given(-0.902933, -0.006021, -0.429739), (0.0077, -0.999968, -0.002167), (-0.429712, -0.005266, 0.902951)-48.006199, 114.704002, -11.5759
15given(-0.909024, 0.002156, -0.416738), (-0.011493, -0.999736, 0.019898), (-0.416585, 0.022877, 0.908809)-47.964298, 112.116997, -12.7962

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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 ... , 6 types, 24 molecules DEFdefHhJLNjlnIKMikmGgoO

#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, H+-transporting two-sector ATPase
#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, H+-transporting two-sector ATPase
#4: 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, H+-transporting two-sector ATPase
#5: 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, H+-transporting two-sector ATPase
#6: 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, H+-transporting two-sector ATPase
#7: Protein V-type proton ATPase subunit F / V-ATPase subunit F / V-ATPase 14 kDa subunit / Vacuolar proton pump subunit F


Mass: 13479.170 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: P39111, H+-transporting two-sector ATPase

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 3.64 Å3/Da / Density % sol: 66.25 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 8.25% PEG 8000, 0.25 M Ammonium Sulfate, 0.1 M HEPES pH 7.5, 0.05 M Strontium Chloride

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.6279 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 10, 2015
RadiationMonochromator: Diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.6279 Å / Relative weight: 1
ReflectionResolution: 6.01→39.72 Å / Num. obs: 41729 / % possible obs: 99.3 % / Redundancy: 11.1 % / Biso Wilson estimate: 422.24 Å2 / CC1/2: 0.981 / Rmerge(I) obs: 0.258 / Rpim(I) all: 0.083 / Net I/σ(I): 11 / Num. measured all: 463370 / Scaling rejects: 282
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) all% possible all
6.01-6.34114.3490.66548659590.2321.36797.5
19.02-39.728.90.22537.51103612440.9280.08589.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIXdev-1957refinement
Aimless0.2.17data scaling
PHASERphasing
PDB_EXTRACT3.15data extraction
Cootmodel building
XDSdata scaling
autoPROCdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5BW9

5bw9


Resolution: 6.202→39.72 Å / SU ML: 0.97 / Cross valid method: FREE R-VALUE / σ(F): 1.89 / Phase error: 34.7 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.3018 1997 5.97 %Random selection
Rwork0.2545 31468 --
obs0.2573 33465 87.62 %-
Solvent computationShrinkage radii: 2.5 Å / VDW probe radii: 2.5 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 719.28 Å2 / Biso mean: 320.3381 Å2 / Biso min: 38.8 Å2
Refinement stepCycle: final / Resolution: 6.202→39.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms47363 0 0 0 47363
Num. residues----9600
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00247322
X-RAY DIFFRACTIONf_angle_d0.62365803
X-RAY DIFFRACTIONf_chiral_restr0.038963
X-RAY DIFFRACTIONf_plane_restr0.0029559
X-RAY DIFFRACTIONf_dihedral_angle_d2.8079559
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2905X-RAY DIFFRACTIONPOSITIONAL0.006
12a2905X-RAY DIFFRACTIONPOSITIONAL0.006
21B2940X-RAY DIFFRACTIONPOSITIONAL0.007
22b2940X-RAY DIFFRACTIONPOSITIONAL0.007
31C2895X-RAY DIFFRACTIONPOSITIONAL0.006
32c2895X-RAY DIFFRACTIONPOSITIONAL0.006
41D2245X-RAY DIFFRACTIONPOSITIONAL0.007
42d2245X-RAY DIFFRACTIONPOSITIONAL0.007
51E2231X-RAY DIFFRACTIONPOSITIONAL0.008
52e2231X-RAY DIFFRACTIONPOSITIONAL0.008
61F2201X-RAY DIFFRACTIONPOSITIONAL0.007
62f2201X-RAY DIFFRACTIONPOSITIONAL0.007
71G1039X-RAY DIFFRACTIONPOSITIONAL0.011
72g1039X-RAY DIFFRACTIONPOSITIONAL0.011
81H2212X-RAY DIFFRACTIONPOSITIONAL0.009
82h2212X-RAY DIFFRACTIONPOSITIONAL0.009
91I1073X-RAY DIFFRACTIONPOSITIONAL0.006
92i1073X-RAY DIFFRACTIONPOSITIONAL0.006
101J514X-RAY DIFFRACTIONPOSITIONAL0.007
102j514X-RAY DIFFRACTIONPOSITIONAL0.007
111K883X-RAY DIFFRACTIONPOSITIONAL0.006
112k883X-RAY DIFFRACTIONPOSITIONAL0.006
121L335X-RAY DIFFRACTIONPOSITIONAL0.005
122l335X-RAY DIFFRACTIONPOSITIONAL0.005
131M1008X-RAY DIFFRACTIONPOSITIONAL0.005
132m1008X-RAY DIFFRACTIONPOSITIONAL0.005
141N400X-RAY DIFFRACTIONPOSITIONAL0.006
142n400X-RAY DIFFRACTIONPOSITIONAL0.006
151O571X-RAY DIFFRACTIONPOSITIONAL0.005
152o571X-RAY DIFFRACTIONPOSITIONAL0.005
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 (%)
6.2018-6.35630.4009190.349630031912
6.3563-6.52750.3945600.331948100837
6.5275-6.71870.40811290.30382029215880
6.7187-6.93440.34681600.281725252685100
6.9344-7.18090.31571600.263425232683100
7.1809-7.46660.35321640.247625802744100
7.4666-7.8040.29911620.24525412703100
7.804-8.2120.3171620.232725572719100
8.212-8.72140.31610.224525522713100
8.7214-9.38660.25861630.202625712734100
9.3866-10.31620.25081640.192925642728100
10.3162-11.77480.20241620.200325652727100
11.7748-14.70870.2921650.25782584274999
14.7087-39.72570.4291660.37872629279599

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