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- PDB-5c90: Staphylococcus aureus ClpP mutant - Y63A -

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Basic information

Entry
Database: PDB / ID: 5c90
TitleStaphylococcus aureus ClpP mutant - Y63A
ComponentsATP-dependent Clp protease proteolytic subunit
KeywordsHYDROLASE / Clp protease / proteolysis
Function / homology
Function and homology information


endopeptidase Clp / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / ATPase binding / serine-type endopeptidase activity / cytoplasm
Similarity search - Function
ClpP, Ser active site / Endopeptidase Clp serine active site. / ClpP, histidine active site / Endopeptidase Clp histidine active site. / ATP-dependent Clp protease proteolytic subunit / Clp protease proteolytic subunit /Translocation-enhancing protein TepA / Clp protease / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily ...ClpP, Ser active site / Endopeptidase Clp serine active site. / ClpP, histidine active site / Endopeptidase Clp histidine active site. / ATP-dependent Clp protease proteolytic subunit / Clp protease proteolytic subunit /Translocation-enhancing protein TepA / Clp protease / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ATP-dependent Clp protease proteolytic subunit
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsYe, F. / Liu, H. / Zhang, J. / Gan, J. / Yang, C.-G.
CitationJournal: Acs Chem.Biol. / Year: 2016
Title: Characterization of Gain-of-Function Mutant Provides New Insights into ClpP Structure
Authors: Ni, T. / Ye, F. / Liu, X. / Zhang, J. / Liu, H. / Li, J. / Zhang, Y. / Sun, Y. / Wang, M. / Luo, C. / Jiang, H. / Lan, L. / Gan, J. / Zhang, A. / Zhou, H. / Yang, C.-G.
History
DepositionJun 26, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 25, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2016Group: Database references
Revision 1.2Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _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: ATP-dependent Clp protease proteolytic subunit
B: ATP-dependent Clp protease proteolytic subunit
C: ATP-dependent Clp protease proteolytic subunit
D: ATP-dependent Clp protease proteolytic subunit
E: ATP-dependent Clp protease proteolytic subunit
F: ATP-dependent Clp protease proteolytic subunit
G: ATP-dependent Clp protease proteolytic subunit
H: ATP-dependent Clp protease proteolytic subunit
I: ATP-dependent Clp protease proteolytic subunit
J: ATP-dependent Clp protease proteolytic subunit
K: ATP-dependent Clp protease proteolytic subunit
L: ATP-dependent Clp protease proteolytic subunit
M: ATP-dependent Clp protease proteolytic subunit
N: ATP-dependent Clp protease proteolytic subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)301,87728
Polymers300,22214
Non-polymers1,65414
Water31,8141766
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area55340 Å2
ΔGint-403 kcal/mol
Surface area91230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)94.359, 126.237, 145.647
Angle α, β, γ (deg.)90.00, 93.74, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28I
19A
29J
110A
210K
111A
211L
112A
212M
113A
213N
114B
214C
115B
215D
116B
216E
117B
217F
118B
218G
119B
219H
120B
220I
121B
221J
122B
222K
123B
223L
124B
224M
125B
225N
126C
226D
127C
227E
128C
228F
129C
229G
130C
230H
131C
231I
132C
232J
133C
233K
134C
234L
135C
235M
136C
236N
137D
237E
138D
238F
139D
239G
140D
240H
141D
241I
142D
242J
143D
243K
144D
244L
145D
245M
146D
246N
147E
247F
148E
248G
149E
249H
150E
250I
151E
251J
152E
252K
153E
253L
154E
254M
155E
255N
156F
256G
157F
257H
158F
258I
159F
259J
160F
260K
161F
261L
162F
262M
163F
263N
164G
264H
165G
265I
166G
266J
167G
267K
168G
268L
169G
269M
170G
270N
171H
271I
172H
272J
173H
273K
174H
274L
175H
275M
176H
276N
177I
277J
178I
278K
179I
279L
180I
280M
181I
281N
182J
282K
183J
283L
184J
284M
185J
285N
186K
286L
187K
287M
188K
288N
189L
289M
190L
290N
191M
291N

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PROPROPROPROAA5 - 1925 - 192
21PROPROPROPROBB5 - 1925 - 192
12PROPROVALVALAA5 - 1915 - 191
22PROPROVALVALCC5 - 1915 - 191
13ILEILEVALVALAA8 - 1918 - 191
23ALAALAVALVALDD17 - 19117 - 191
14PROPROVALVALAA5 - 1915 - 191
24PROPROVALVALEE5 - 1915 - 191
15PROPROPROPROAA5 - 1925 - 192
25PROPROPROPROFF5 - 1925 - 192
16PROPROVALVALAA5 - 1915 - 191
26PROPROVALVALGG5 - 1915 - 191
17PROPROPROPROAA5 - 1925 - 192
27PROPROPROPROHH5 - 1925 - 192
18PROPROPROPROAA5 - 1925 - 192
28PROPROPROPROII5 - 1925 - 192
19PROPROVALVALAA5 - 1915 - 191
29PROPROVALVALJJ5 - 1915 - 191
110PROPROPROPROAA5 - 1925 - 192
210PROPROPROPROKK5 - 1925 - 192
111PROPROVALVALAA5 - 1915 - 191
211PROPROVALVALLL5 - 1915 - 191
112PROPROVALVALAA5 - 1915 - 191
212PROPROVALVALMM5 - 1915 - 191
113PROPROVALVALAA5 - 1915 - 191
213PROPROVALVALNN5 - 1915 - 191
114LEULEUPROPROBB3 - 1923 - 192
214LEULEUPROPROCC3 - 1923 - 192
115LEULEUVALVALBB3 - 1913 - 191
215LEULEUVALVALDD3 - 1913 - 191
116LEULEUGLUGLUBB3 - 1933 - 193
216LEULEUGLUGLUEE3 - 1933 - 193
117LEULEUGLUGLUBB3 - 1933 - 193
217LEULEUGLUGLUFF3 - 1933 - 193
118ILEILEVALVALBB4 - 1914 - 191
218ILEILEVALVALGG4 - 1914 - 191
119ILEILEVALVALBB8 - 1918 - 191
219ILEILEVALVALHH4 - 1914 - 191
120ILEILEVALVALBB8 - 1918 - 191
220ILEILEVALVALII4 - 1914 - 191
121ILEILEVALVALBB4 - 1914 - 191
221ILEILEVALVALJJ4 - 1914 - 191
122LEULEUGLUGLUBB3 - 1933 - 193
222LEULEUGLUGLUKK3 - 1933 - 193
123LEULEUPROPROBB3 - 1923 - 192
223LEULEUPROPROLL3 - 1923 - 192
124ILEILEPROPROBB8 - 1928 - 192
224ILEILEPROPROMM4 - 1924 - 192
125ILEILEGLUGLUBB4 - 1934 - 193
225ILEILEGLUGLUNN4 - 1934 - 193
126LEULEUPROPROCC3 - 1923 - 192
226LEULEUPROPRODD3 - 1923 - 192
127LEULEUPROPROCC3 - 1923 - 192
227LEULEUPROPROEE3 - 1923 - 192
128LEULEUPROPROCC3 - 1923 - 192
228LEULEUPROPROFF3 - 1923 - 192
129ILEILEVALVALCC4 - 1914 - 191
229ILEILEVALVALGG4 - 1914 - 191
130ILEILEPROPROCC4 - 1924 - 192
230ILEILEPROPROHH4 - 1924 - 192
131ILEILEPROPROCC4 - 1924 - 192
231ILEILEPROPROII4 - 1924 - 192
132ILEILEPROPROCC4 - 1924 - 192
232ILEILEPROPROJJ4 - 1924 - 192
133LEULEUPROPROCC3 - 1923 - 192
233LEULEUPROPROKK3 - 1923 - 192
134LEULEUPROPROCC3 - 1923 - 192
234LEULEUPROPROLL3 - 1923 - 192
135ILEILEPROPROCC4 - 1924 - 192
235ILEILEPROPROMM4 - 1924 - 192
136ILEILEVALVALCC4 - 1914 - 191
236ILEILEVALVALNN4 - 1914 - 191
137LEULEUPROPRODD3 - 1923 - 192
237LEULEUPROPROEE3 - 1923 - 192
138LEULEUVALVALDD3 - 1913 - 191
238LEULEUVALVALFF3 - 1913 - 191
139PROPROPROPRODD5 - 1925 - 192
239THRTHRPROPROGG10 - 19210 - 192
140ILEILEVALVALDD4 - 1914 - 191
240ILEILEVALVALHH4 - 1914 - 191
141ILEILEVALVALDD4 - 1914 - 191
241ILEILEVALVALII4 - 1914 - 191
142LEULEUVALVALDD3 - 1913 - 191
242VALVALVALVALJJ7 - 1917 - 191
143LEULEUVALVALDD3 - 1913 - 191
243LEULEUVALVALKK3 - 1913 - 191
144LEULEUPROPRODD3 - 1923 - 192
244LEULEUPROPROLL3 - 1923 - 192
145ILEILEVALVALDD4 - 1914 - 191
245ILEILEVALVALMM4 - 1914 - 191
146ILEILEVALVALDD4 - 1914 - 191
246ILEILEVALVALNN4 - 1914 - 191
147LEULEUGLUGLUEE3 - 1933 - 193
247LEULEUGLUGLUFF3 - 1933 - 193
148ILEILEPROPROEE4 - 1924 - 192
248ILEILEPROPROGG4 - 1924 - 192
149ILEILEPROPROEE4 - 1924 - 192
249ILEILEPROPROHH4 - 1924 - 192
150ILEILEPROPROEE4 - 1924 - 192
250ILEILEPROPROII4 - 1924 - 192
151ILEILEVALVALEE4 - 1914 - 191
251ILEILEVALVALJJ4 - 1914 - 191
152LEULEUGLUGLUEE3 - 1933 - 193
252LEULEUGLUGLUKK3 - 1933 - 193
153LEULEUGLUGLUEE3 - 1933 - 193
253LEULEUGLUGLULL3 - 1933 - 193
154ILEILEGLUGLUEE4 - 1934 - 193
254ILEILEGLUGLUMM4 - 1934 - 193
155ILEILEGLUGLUEE4 - 1934 - 193
255ILEILEGLUGLUNN4 - 1934 - 193
156ILEILEPROPROFF4 - 1924 - 192
256ILEILEPROPROGG4 - 1924 - 192
157ILEILEPROPROFF4 - 1924 - 192
257ILEILEPROPROHH4 - 1924 - 192
158ILEILEPROPROFF4 - 1924 - 192
258ILEILEPROPROII4 - 1924 - 192
159ILEILEVALVALFF4 - 1914 - 191
259ILEILEVALVALJJ4 - 1914 - 191
160LEULEUGLUGLUFF3 - 1933 - 193
260LEULEUGLUGLUKK3 - 1933 - 193
161LEULEUGLUGLUFF3 - 1933 - 193
261LEULEUGLUGLULL3 - 1933 - 193
162ILEILEPROPROFF4 - 1924 - 192
262ILEILEPROPROMM4 - 1924 - 192
163ILEILEGLUGLUFF4 - 1934 - 193
263ILEILEGLUGLUNN4 - 1934 - 193
164THRTHRVALVALGG10 - 19110 - 191
264PROPROVALVALHH5 - 1915 - 191
165THRTHRVALVALGG10 - 19110 - 191
265PROPROVALVALII5 - 1915 - 191
166ILEILEPROPROGG4 - 1924 - 192
266ILEILEPROPROJJ4 - 1924 - 192
167ILEILEPROPROGG4 - 1924 - 192
267ILEILEPROPROKK4 - 1924 - 192
168ILEILEVALVALGG4 - 1914 - 191
268ILEILEVALVALLL4 - 1914 - 191
169THRTHRVALVALGG10 - 19110 - 191
269PROPROVALVALMM5 - 1915 - 191
170ILEILEVALVALGG4 - 1914 - 191
270ILEILEVALVALNN4 - 1914 - 191
171ILEILEPROPROHH4 - 1924 - 192
271ILEILEPROPROII4 - 1924 - 192
172ILEILEVALVALHH4 - 1914 - 191
272ILEILEVALVALJJ8 - 1918 - 191
173ILEILEPROPROHH4 - 1924 - 192
273ILEILEPROPROKK4 - 1924 - 192
174ILEILEVALVALHH4 - 1914 - 191
274ILEILEVALVALLL4 - 1914 - 191
175ILEILEVALVALHH4 - 1914 - 191
275ILEILEVALVALMM4 - 1914 - 191
176ILEILEPROPROHH4 - 1924 - 192
276ILEILEPROPRONN4 - 1924 - 192
177ILEILEVALVALII4 - 1914 - 191
277ILEILEVALVALJJ8 - 1918 - 191
178ILEILEPROPROII4 - 1924 - 192
278ILEILEPROPROKK4 - 1924 - 192
179ILEILEVALVALII4 - 1914 - 191
279ILEILEVALVALLL4 - 1914 - 191
180ILEILEVALVALII4 - 1914 - 191
280ILEILEVALVALMM4 - 1914 - 191
181ILEILEPROPROII4 - 1924 - 192
281ILEILEPROPRONN4 - 1924 - 192
182ILEILEVALVALJJ4 - 1914 - 191
282ILEILEVALVALKK4 - 1914 - 191
183ILEILEPROPROJJ4 - 1924 - 192
283ILEILEPROPROLL4 - 1924 - 192
184ILEILEVALVALJJ8 - 1918 - 191
284ILEILEVALVALMM4 - 1914 - 191
185ILEILEPROPROJJ4 - 1924 - 192
285ILEILEPROPRONN4 - 1924 - 192
186LEULEUGLUGLUKK3 - 1933 - 193
286LEULEUGLUGLULL3 - 1933 - 193
187ILEILEPROPROKK4 - 1924 - 192
287ILEILEPROPROMM4 - 1924 - 192
188ILEILEGLUGLUKK4 - 1934 - 193
288ILEILEGLUGLUNN4 - 1934 - 193
189ILEILEGLUGLULL4 - 1934 - 193
289ILEILEGLUGLUMM4 - 1934 - 193
190ILEILEPROPROLL4 - 1924 - 192
290ILEILEPROPRONN4 - 1924 - 192
191ILEILEGLUGLUMM4 - 1934 - 193
291ILEILEGLUGLUNN4 - 1934 - 193

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91

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Components

#1: Protein
ATP-dependent Clp protease proteolytic subunit / Endopeptidase Clp


Mass: 21444.434 Da / Num. of mol.: 14 / Mutation: Y63A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Strain: NCTC 8325 / Gene: clpP, SAOUHSC_00790
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
Strain (production host): BL21-Gold(DE3)pLysS AG / References: UniProt: Q2G036, endopeptidase Clp
#2: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1766 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.09 Å3/Da / Density % sol: 60.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 30% MPD, 100mM sodium acetate (pH 5.5), 20mM calcium chloride

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9735 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 1, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9735 Å / Relative weight: 1
ReflectionResolution: 1.75→50 Å / Num. obs: 340047 / % possible obs: 99.6 % / Redundancy: 3.4 % / Net I/σ(I): 16.6
Reflection shellResolution: 1.75→1.81 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 3.8 / Num. measured obs: 112177 / Num. unique all: 33993 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.7.0029refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3STA

3sta


Resolution: 1.75→30 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.952 / SU B: 1.929 / SU ML: 0.062 / Cross valid method: THROUGHOUT / ESU R: 0.101 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20164 17178 5.1 %RANDOM
Rwork0.18229 ---
obs0.18312 322791 99.43 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 27.289 Å2
Baniso -1Baniso -2Baniso -3
1-1.23 Å2-0 Å2-0.16 Å2
2--0.07 Å2-0 Å2
3----1.28 Å2
Refinement stepCycle: LAST / Resolution: 1.75→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19646 0 112 1766 21524
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01920307
X-RAY DIFFRACTIONr_bond_other_d0.0090.0220192
X-RAY DIFFRACTIONr_angle_refined_deg1.4661.98127499
X-RAY DIFFRACTIONr_angle_other_deg1.618346500
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.40752641
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.62725.598895
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.456153757
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.96415106
X-RAY DIFFRACTIONr_chiral_restr0.0860.23246
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0222998
X-RAY DIFFRACTIONr_gen_planes_other0.0060.024260
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A110560.07
12B110560.07
21A109130.07
22C109130.07
31A108120.06
32D108120.06
41A110720.06
42E110720.06
51A109500.07
52F109500.07
61A108860.08
62G108860.08
71A110210.07
72H110210.07
81A110910.06
82I110910.06
91A108760.08
92J108760.08
101A109690.07
102K109690.07
111A109250.07
112L109250.07
121A109220.07
122M109220.07
131A109650.08
132N109650.08
141B114360.07
142C114360.07
151B112400.06
152D112400.06
161B114700.07
162E114700.07
171B115760.07
172F115760.07
181B115270.07
182G115270.07
191B112290.05
192H112290.05
201B111630.05
202I111630.05
211B113950.08
212J113950.08
221B116790.06
222K116790.06
231B111860.09
232L111860.09
241B112030.06
242M112030.06
251B113210.07
252N113210.07
261C112030.08
262D112030.08
271C113040.08
272E113040.08
281C112830.08
282F112830.08
291C111790.08
292G111790.08
301C113270.06
302H113270.06
311C113120.06
312I113120.06
321C113300.07
322J113300.07
331C113310.08
332K113310.08
341C112800.08
342L112800.08
351C112490.07
352M112490.07
361C112160.07
362N112160.07
371D111830.07
372E111830.07
381D112780.05
382F112780.05
391D109590.07
392G109590.07
401D111480.06
402H111480.06
411D110820.07
412I110820.07
421D110780.07
422J110780.07
431D112030.07
432K112030.07
441D111550.08
442L111550.08
451D111440.06
452M111440.06
461D109530.08
462N109530.08
471E114240.08
472F114240.08
481E113100.08
482G113100.08
491E111830.07
492H111830.07
501E112600.06
502I112600.06
511E112770.08
512J112770.08
521E114290.08
522K114290.08
531E113340.08
532L113340.08
541E111490.08
542M111490.08
551E111890.08
552N111890.08
561F113440.08
562G113440.08
571F111630.06
572H111630.06
581F110920.06
582I110920.06
591F113150.07
592J113150.07
601F115450.07
602K115450.07
611F110610.08
612L110610.08
621F111790.06
622M111790.06
631F111270.07
632N111270.07
641G109860.07
642H109860.07
651G109810.06
652I109810.06
661G114050.08
662J114050.08
671G114750.08
672K114750.08
681G110020.09
682L110020.09
691G109390.08
692M109390.08
701G111410.08
702N111410.08
711H112710.05
712I112710.05
721H108870.07
722J108870.07
731H111770.06
732K111770.06
741H109080.08
742L109080.08
751H112480.05
752M112480.05
761H111410.07
762N111410.07
771I108580.07
772J108580.07
781I110610.06
782K110610.06
791I108970.08
792L108970.08
801I111300.06
802M111300.06
811I112030.06
812N112030.06
821J113180.08
822K113180.08
831J110050.09
832L110050.09
841J109170.07
842M109170.07
851J111120.07
852N111120.07
861K110550.09
862L110550.09
871K111340.07
872M111340.07
881K110750.08
882N110750.08
891L109770.09
892M109770.09
901L109470.09
902N109470.09
911M112370.08
912N112370.08
LS refinement shellResolution: 1.75→1.795 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.273 1210 -
Rwork0.252 23471 -
obs--98.34 %

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