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- PDB-5dsv: Crystal structure of human proteasome alpha7 tetradecamer -

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Basic information

Entry
Database: PDB / ID: 5dsv
TitleCrystal structure of human proteasome alpha7 tetradecamer
ComponentsProteasome subunit alpha type-3
KeywordsHYDROLASE / Proteasome
Function / homology
Function and homology information


regulation of endopeptidase activity / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / proteasome core complex, alpha-subunit complex / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin ...regulation of endopeptidase activity / Regulation of ornithine decarboxylase (ODC) / proteasome core complex / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / proteasome core complex, alpha-subunit complex / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Degradation of DVL / proteasomal protein catabolic process / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of AXIN / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Negative regulation of NOTCH4 signaling / G2/M Checkpoints / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / ABC-family proteins mediated transport / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / UCH proteinases / The role of GTSE1 in G2/M progression after G2 checkpoint / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / Neddylation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / ER-Phagosome pathway / proteasome-mediated ubiquitin-dependent protein catabolic process / Ub-specific processing proteases / synapse / ubiquitin protein ligase binding / extracellular exosome / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Proteasome subunit alpha type-3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.75 Å
AuthorsSatoh, T. / Thammaporn, R. / Seetaha, S. / Kato, K.
Funding support Japan, 1items
OrganizationGrant numberCountry
JSPS, MEXT, Japan25102001, 25102008, and 15H02491 to K.K. and 25121722 and 26102530 to S.U. Japan
CitationJournal: Sci Rep / Year: 2015
Title: Disassembly of the self-assembled, double-ring structure of proteasome alpha 7 homo-tetradecamer by alpha 6
Authors: Ishii, K. / Noda, M. / Yagi, H. / Thammaporn, R. / Seetaha, S. / Satoh, T. / Kato, K. / Uchiyama, S.
History
DepositionSep 17, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Dec 2, 2015Provider: repository / Type: Initial release
Revision 1.1Dec 30, 2015Group: 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: Proteasome subunit alpha type-3
B: Proteasome subunit alpha type-3
C: Proteasome subunit alpha type-3
D: Proteasome subunit alpha type-3
E: Proteasome subunit alpha type-3
F: Proteasome subunit alpha type-3
G: Proteasome subunit alpha type-3
H: Proteasome subunit alpha type-3
I: Proteasome subunit alpha type-3
J: Proteasome subunit alpha type-3
K: Proteasome subunit alpha type-3
L: Proteasome subunit alpha type-3
M: Proteasome subunit alpha type-3
N: Proteasome subunit alpha type-3


Theoretical massNumber of molelcules
Total (without water)398,57014
Polymers398,57014
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area46970 Å2
ΔGint-202 kcal/mol
Surface area125400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)132.481, 132.481, 444.563
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
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: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11SERSERLYSLYSAA2 - 2443 - 245
21SERSERLYSLYSBB2 - 2443 - 245
12SERSERGLUGLUAA2 - 2453 - 246
22SERSERGLUGLUCC2 - 2453 - 246
13SERSERGLUGLUAA2 - 2453 - 246
23SERSERGLUGLUDD2 - 2453 - 246
14SERSERLYSLYSAA2 - 2443 - 245
24SERSERLYSLYSEE2 - 2443 - 245
15SERSERGLUGLUAA2 - 2453 - 246
25SERSERGLUGLUFF2 - 2453 - 246
16GLYGLYLYSLYSAA4 - 2445 - 245
26GLYGLYLYSLYSGG4 - 2445 - 245
17SERSERLYSLYSAA2 - 2443 - 245
27SERSERLYSLYSHH2 - 2443 - 245
18SERSERLEULEUAA2 - 2433 - 244
28SERSERLEULEUII2 - 2433 - 244
19SERSERGLUGLUAA2 - 2453 - 246
29SERSERGLUGLUJJ2 - 2453 - 246
110SERSERLEULEUAA2 - 2433 - 244
210SERSERLEULEUKK2 - 2433 - 244
111SERSERLYSLYSAA2 - 2443 - 245
211SERSERLYSLYSLL2 - 2443 - 245
112SERSERLEULEUAA2 - 2433 - 244
212SERSERLEULEUMM2 - 2433 - 244
113SERSERGLUGLUAA2 - 2453 - 246
213SERSERGLUGLUNN2 - 2453 - 246
114SERSERGLUGLUBB1 - 2452 - 246
214SERSERGLUGLUCC1 - 2452 - 246
115SERSERLYSLYSBB2 - 2443 - 245
215SERSERLYSLYSDD2 - 2443 - 245
116SERSERGLUGLUBB1 - 2452 - 246
216SERSERGLUGLUEE1 - 2452 - 246
117SERSERLYSLYSBB2 - 2443 - 245
217SERSERLYSLYSFF2 - 2443 - 245
118GLYGLYLYSLYSBB4 - 2445 - 245
218GLYGLYLYSLYSGG4 - 2445 - 245
119SERSERLYSLYSBB1 - 2442 - 245
219SERSERLYSLYSHH1 - 2442 - 245
120SERSERLEULEUBB1 - 2432 - 244
220SERSERLEULEUII1 - 2432 - 244
121SERSERGLUGLUBB1 - 2452 - 246
221SERSERGLUGLUJJ1 - 2452 - 246
122SERSERLEULEUBB1 - 2432 - 244
222SERSERLEULEUKK1 - 2432 - 244
123SERSERGLUGLUBB1 - 2452 - 246
223SERSERGLUGLULL1 - 2452 - 246
124SERSERLEULEUBB1 - 2432 - 244
224SERSERLEULEUMM1 - 2432 - 244
125SERSERLYSLYSBB2 - 2443 - 245
225SERSERLYSLYSNN2 - 2443 - 245
126SERSERGLUGLUCC2 - 2453 - 246
226SERSERGLUGLUDD2 - 2453 - 246
127SERSERGLUGLUCC1 - 2452 - 246
227SERSERGLUGLUEE1 - 2452 - 246
128SERSERGLUGLUCC2 - 2453 - 246
228SERSERGLUGLUFF2 - 2453 - 246
129GLYGLYGLUGLUCC4 - 2455 - 246
229GLYGLYGLUGLUGG4 - 2455 - 246
130SERSERLYSLYSCC1 - 2442 - 245
230SERSERLYSLYSHH1 - 2442 - 245
131SERSERLYSLYSCC1 - 2442 - 245
231SERSERLYSLYSII1 - 2442 - 245
132SERSERGLUGLUCC1 - 2452 - 246
232SERSERGLUGLUJJ1 - 2452 - 246
133SERSERLYSLYSCC1 - 2442 - 245
233SERSERLYSLYSKK1 - 2442 - 245
134SERSERGLUGLUCC1 - 2452 - 246
234SERSERGLUGLULL1 - 2452 - 246
135SERSERLEULEUCC1 - 2432 - 244
235SERSERLEULEUMM1 - 2432 - 244
136SERSERGLUGLUCC2 - 2453 - 246
236SERSERGLUGLUNN2 - 2453 - 246
137SERSERLYSLYSDD2 - 2443 - 245
237SERSERLYSLYSEE2 - 2443 - 245
138SERSERGLUGLUDD2 - 2453 - 246
238SERSERGLUGLUFF2 - 2453 - 246
139GLYGLYLYSLYSDD4 - 2445 - 245
239GLYGLYLYSLYSGG4 - 2445 - 245
140SERSERLYSLYSDD2 - 2443 - 245
240SERSERLYSLYSHH2 - 2443 - 245
141SERSERLEULEUDD2 - 2433 - 244
241SERSERLEULEUII2 - 2433 - 244
142SERSERGLUGLUDD2 - 2453 - 246
242SERSERGLUGLUJJ2 - 2453 - 246
143SERSERLEULEUDD2 - 2433 - 244
243SERSERLEULEUKK2 - 2433 - 244
144SERSERLYSLYSDD2 - 2443 - 245
244SERSERLYSLYSLL2 - 2443 - 245
145SERSERLEULEUDD2 - 2433 - 244
245SERSERLEULEUMM2 - 2433 - 244
146SERSERGLUGLUDD2 - 2453 - 246
246SERSERGLUGLUNN2 - 2453 - 246
147SERSERLYSLYSEE2 - 2443 - 245
247SERSERLYSLYSFF2 - 2443 - 245
148GLYGLYLYSLYSEE4 - 2445 - 245
248GLYGLYLYSLYSGG4 - 2445 - 245
149SERSERLYSLYSEE1 - 2442 - 245
249SERSERLYSLYSHH1 - 2442 - 245
150SERSERLEULEUEE1 - 2432 - 244
250SERSERLEULEUII1 - 2432 - 244
151SERSERGLUGLUEE1 - 2452 - 246
251SERSERGLUGLUJJ1 - 2452 - 246
152SERSERLEULEUEE1 - 2432 - 244
252SERSERLEULEUKK1 - 2432 - 244
153SERSERGLUGLUEE1 - 2452 - 246
253SERSERGLUGLULL1 - 2452 - 246
154SERSERLEULEUEE1 - 2432 - 244
254SERSERLEULEUMM1 - 2432 - 244
155SERSERLYSLYSEE2 - 2443 - 245
255SERSERLYSLYSNN2 - 2443 - 245
156GLYGLYLYSLYSFF4 - 2445 - 245
256GLYGLYLYSLYSGG4 - 2445 - 245
157SERSERLYSLYSFF2 - 2443 - 245
257SERSERLYSLYSHH2 - 2443 - 245
158SERSERLEULEUFF2 - 2433 - 244
258SERSERLEULEUII2 - 2433 - 244
159SERSERGLUGLUFF2 - 2453 - 246
259SERSERGLUGLUJJ2 - 2453 - 246
160SERSERLEULEUFF2 - 2433 - 244
260SERSERLEULEUKK2 - 2433 - 244
161SERSERLYSLYSFF2 - 2443 - 245
261SERSERLYSLYSLL2 - 2443 - 245
162SERSERLEULEUFF2 - 2433 - 244
262SERSERLEULEUMM2 - 2433 - 244
163SERSERGLUGLUFF2 - 2453 - 246
263SERSERGLUGLUNN2 - 2453 - 246
164GLYGLYLYSLYSGG4 - 2445 - 245
264GLYGLYLYSLYSHH4 - 2445 - 245
165GLYGLYLEULEUGG4 - 2435 - 244
265GLYGLYLEULEUII4 - 2435 - 244
166GLYGLYGLUGLUGG4 - 2455 - 246
266GLYGLYGLUGLUJJ4 - 2455 - 246
167GLYGLYLEULEUGG4 - 2435 - 244
267GLYGLYLEULEUKK4 - 2435 - 244
168GLYGLYLYSLYSGG4 - 2445 - 245
268GLYGLYLYSLYSLL4 - 2445 - 245
169GLYGLYSERSERGG4 - 2425 - 243
269GLYGLYSERSERMM4 - 2425 - 243
170GLYGLYLYSLYSGG4 - 2445 - 245
270GLYGLYLYSLYSNN4 - 2445 - 245
171SERSERLYSLYSHH1 - 2442 - 245
271SERSERLYSLYSII1 - 2442 - 245
172SERSERLYSLYSHH1 - 2442 - 245
272SERSERLYSLYSJJ1 - 2442 - 245
173SERSERLYSLYSHH1 - 2442 - 245
273SERSERLYSLYSKK1 - 2442 - 245
174SERSERLYSLYSHH1 - 2442 - 245
274SERSERLYSLYSLL1 - 2442 - 245
175SERSERLEULEUHH1 - 2432 - 244
275SERSERLEULEUMM1 - 2432 - 244
176SERSERLYSLYSHH2 - 2443 - 245
276SERSERLYSLYSNN2 - 2443 - 245
177SERSERLYSLYSII1 - 2442 - 245
277SERSERLYSLYSJJ1 - 2442 - 245
178SERSERLYSLYSII1 - 2442 - 245
278SERSERLYSLYSKK1 - 2442 - 245
179SERSERLEULEUII1 - 2432 - 244
279SERSERLEULEULL1 - 2432 - 244
180SERSERLEULEUII1 - 2432 - 244
280SERSERLEULEUMM1 - 2432 - 244
181SERSERLEULEUII2 - 2433 - 244
281SERSERLEULEUNN2 - 2433 - 244
182SERSERLYSLYSJJ1 - 2442 - 245
282SERSERLYSLYSKK1 - 2442 - 245
183SERSERGLUGLUJJ1 - 2452 - 246
283SERSERGLUGLULL1 - 2452 - 246
184SERSERLEULEUJJ1 - 2432 - 244
284SERSERLEULEUMM1 - 2432 - 244
185SERSERGLUGLUJJ2 - 2453 - 246
285SERSERGLUGLUNN2 - 2453 - 246
186SERSERLEULEUKK1 - 2432 - 244
286SERSERLEULEULL1 - 2432 - 244
187SERSERLEULEUKK1 - 2432 - 244
287SERSERLEULEUMM1 - 2432 - 244
188SERSERLEULEUKK2 - 2433 - 244
288SERSERLEULEUNN2 - 2433 - 244
189SERSERLEULEULL1 - 2432 - 244
289SERSERLEULEUMM1 - 2432 - 244
190SERSERLYSLYSLL2 - 2443 - 245
290SERSERLYSLYSNN2 - 2443 - 245
191SERSERLEULEUMM2 - 2433 - 244
291SERSERLEULEUNN2 - 2433 - 244

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
Proteasome subunit alpha type-3 / / proteasome alpha7 subunit / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 ...proteasome alpha7 subunit / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8


Mass: 28469.252 Da / Num. of mol.: 14
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMA3, HC8, PSC8 / Plasmid: pRSF-Duet1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: P25788, proteasome endopeptidase complex

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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: 2.45 Å3/Da / Density % sol: 49.74 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 24% PEG400, 100 mM Tris-HCl (pH 7.5), 0.2 M magnesium chloride

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Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 10, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.75→50 Å / Num. all: 41746 / Num. obs: 40504 / % possible obs: 97.1 % / Observed criterion σ(I): -3 / Redundancy: 4.9 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 16.3
Reflection shellResolution: 3.75→3.81 Å / Redundancy: 5 % / Rmerge(I) obs: 0.497 / Mean I/σ(I) obs: 2.5 / % possible all: 98.5

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Processing

Software
NameVersionClassification
REFMAC5.8.0069refinement
SCALEPACKdata reduction
DENZOdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1J2P
Resolution: 3.75→20 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.903 / SU B: 52.338 / SU ML: 0.719 / Cross valid method: THROUGHOUT / ESU R Free: 0.935 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.29107 2039 5.1 %RANDOM
Rwork0.20945 ---
obs0.21349 38252 96.53 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 152.993 Å2
Baniso -1Baniso -2Baniso -3
1-4.99 Å20 Å20 Å2
2--4.99 Å20 Å2
3----9.99 Å2
Refinement stepCycle: 1 / Resolution: 3.75→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms26493 0 0 0 26493
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01926988
X-RAY DIFFRACTIONr_bond_other_d0.0060.0225767
X-RAY DIFFRACTIONr_angle_refined_deg1.2251.95836343
X-RAY DIFFRACTIONr_angle_other_deg0.935359301
X-RAY DIFFRACTIONr_dihedral_angle_1_deg
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0550.23960
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0230480
X-RAY DIFFRACTIONr_gen_planes_other0.0060.026158
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_it13.59414.68713549
X-RAY DIFFRACTIONr_mcbond_other13.59214.68713548
X-RAY DIFFRACTIONr_mcangle_it20.89121.98116903
X-RAY DIFFRACTIONr_mcangle_other20.89221.98116904
X-RAY DIFFRACTIONr_scbond_it13.74615.83213438
X-RAY DIFFRACTIONr_scbond_other13.74615.83213436
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other21.48523.32519439
X-RAY DIFFRACTIONr_long_range_B_refined28.35521569
X-RAY DIFFRACTIONr_long_range_B_other28.35621570
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)
11A150540.02
12B150540.02
21A141310.03
22C141310.03
31A150730.02
32D150730.02
41A150310.02
42E150310.02
51A151280.01
52F151280.01
61A148710.02
62G148710.02
71A146780.03
72H146780.03
81A149340.02
82I149340.02
91A146740.02
92J146740.02
101A149530.03
102K149530.03
111A150180.02
112L150180.02
121A144770.02
122M144770.02
131A151200.02
132N151200.02
141B142050.03
142C142050.03
151B150130.02
152D150130.02
161B151360.02
162E151360.02
171B150710.02
172F150710.02
181B148770.02
182G148770.02
191B147500.02
192H147500.02
201B149980.02
202I149980.02
211B147450
212J147450
221B150250.03
222K150250.03
231B151290.02
232L151290.02
241B145420.02
242M145420.02
251B150660.02
252N150660.02
261C141850.02
262D141850.02
271C141850.03
272E141850.03
281C141480.03
282F141480.03
291C140650.02
292G140650.02
301C141860.02
302H141860.02
311C142140.02
312I142140.02
321C142420.03
322J142420.03
331C141740.02
332K141740.02
341C142530.02
342L142530.02
351C137520.02
352M137520.02
361C141480.03
362N141480.03
371D149960.02
372E149960.02
381D150860.01
382F150860.01
391D149190.01
392G149190.01
401D146430.03
402H146430.03
411D149830.01
412I149830.01
421D146380.01
422J146380.01
431D149210.03
432K149210.03
441D150610.01
442L150610.01
451D145240.01
452M145240.01
461D150860.02
462N150860.02
471E150450.02
472F150450.02
481E148710.02
482G148710.02
491E147310.03
492H147310.03
501E149890.02
502I149890.02
511E147250.02
512J147250.02
521E150060.03
522K150060.03
531E151110.02
532L151110.02
541E145290.03
542M145290.03
551E150480.02
552N150480.02
561F148870.01
562G148870.01
571F146930.02
572H146930.02
581F149480.01
582I149480.01
591F146890
592J146890
601F149720.02
602K149720.02
611F150370.01
612L150370.01
621F144940.02
622M144940.02
631F151360.01
632N151360.01
641G145360.03
642H145360.03
651G148480.01
652I148480.01
661G145270.01
662J145270.01
671G147880.02
672K147880.02
681G149310.01
682L149310.01
691G143120.02
692M143120.02
701G148890.01
702N148890.01
711H147150.03
712I147150.03
721H146870.02
722J146870.02
731H147750.01
732K147750.01
741H147180.03
742L147180.03
751H142250.03
752M142250.03
761H146920.02
762N146920.02
771I146700.01
772J146700.01
781I150750.02
782K150750.02
791I150540
792L150540
801I146000.01
802M146000.01
811I149510.01
812N149510.01
821J146900.02
822K146900.02
831J147100.01
832L147100.01
841J142060.02
842M142060.02
851J146870.01
852N146870.01
861K149940.02
862L149940.02
871K145370.03
872M145370.03
881K149730.02
882N149730.02
891L146030.01
892M146030.01
901L150320.01
902N150320.01
911M144940.02
912N144940.02
LS refinement shellResolution: 3.75→3.844 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.405 127 -
Rwork0.332 2737 -
obs--98.59 %

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