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- PDB-5xgo: The Ferritin E-Domain: Toward Understanding Its Role in Protein C... -

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Basic information

Entry
Database: PDB / ID: 5xgo
TitleThe Ferritin E-Domain: Toward Understanding Its Role in Protein Cage Assembly Through the Crystal Structure of a Maxi-/Mini-Ferritin Chimera
ComponentsDNA protection during starvation protein,Bacterioferritin
KeywordsOXIDOREDUCTASE / Ferritin / Protein engineering / protein cage
Function / homology
Function and homology information


DnaA-Dps complex / Oxidoreductases; Oxidizing metal ions / oxidoreductase activity, acting on metal ions / iron ion sequestering activity / nucleoid / chromosome condensation / response to stress / response to starvation / ferroxidase / ferroxidase activity ...DnaA-Dps complex / Oxidoreductases; Oxidizing metal ions / oxidoreductase activity, acting on metal ions / iron ion sequestering activity / nucleoid / chromosome condensation / response to stress / response to starvation / ferroxidase / ferroxidase activity / intracellular sequestering of iron ion / negative regulation of DNA-templated DNA replication initiation / ferric iron binding / iron ion transport / intracellular iron ion homeostasis / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity / DNA binding / identical protein binding / membrane / cytosol / cytoplasm
Similarity search - Function
DNA protection during starvation protein, gammaproteobacteria / Dps protein family signature 2. / Dps protein family signature 1. / Bacterioferritin signature. / Bacterioferritin / DNA-binding protein Dps, conserved site / DNA-binding protein Dps / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin-like diiron domain ...DNA protection during starvation protein, gammaproteobacteria / Dps protein family signature 2. / Dps protein family signature 1. / Bacterioferritin signature. / Bacterioferritin / DNA-binding protein Dps, conserved site / DNA-binding protein Dps / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Bacterioferritin / DNA protection during starvation protein
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.99 Å
AuthorsCornell, T.A. / Srivastava, Y. / Jauch, R. / Fan, R. / Orner, B.P.
Funding support Singapore, 1items
OrganizationGrant numberCountry
A*STAR Singapore
CitationJournal: Biochemistry / Year: 2017
Title: The Crystal Structure of a Maxi/Mini-Ferritin Chimera Reveals Guiding Principles for the Assembly of Protein Cages.
Authors: Cornell, T.A. / Srivastava, Y. / Jauch, R. / Fan, R. / Orner, B.P.
History
DepositionApr 14, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 28, 2018Provider: repository / Type: Initial release
Revision 1.1Mar 27, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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: DNA protection during starvation protein,Bacterioferritin
B: DNA protection during starvation protein,Bacterioferritin
C: DNA protection during starvation protein,Bacterioferritin
D: DNA protection during starvation protein,Bacterioferritin
E: DNA protection during starvation protein,Bacterioferritin
F: DNA protection during starvation protein,Bacterioferritin
G: DNA protection during starvation protein,Bacterioferritin
H: DNA protection during starvation protein,Bacterioferritin
I: DNA protection during starvation protein,Bacterioferritin
J: DNA protection during starvation protein,Bacterioferritin
K: DNA protection during starvation protein,Bacterioferritin
L: DNA protection during starvation protein,Bacterioferritin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)271,97614
Polymers271,90512
Non-polymers712
Water32,0851781
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area46280 Å2
ΔGint-148 kcal/mol
Surface area57190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.139, 104.723, 207.756
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
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
112B
212C
113B
213D
114B
214E
115B
215F
116B
216G
117B
217H
118B
218I
119B
219J
120B
220K
121B
221L
122C
222D
123C
223E
124C
224F
125C
225G
126C
226H
127C
227I
128C
228J
129C
229K
130C
230L
131D
231E
132D
232F
133D
233G
134D
234H
135D
235I
136D
236J
137D
237K
138D
238L
139E
239F
140E
240G
141E
241H
142E
242I
143E
243J
144E
244K
145E
245L
146F
246G
147F
247H
148F
248I
149F
249J
150F
250K
151F
251L
152G
252H
153G
253I
154G
254J
155G
255K
156G
256L
157H
257I
158H
258J
159H
259K
160H
260L
161I
261J
162I
262K
163I
263L
164J
264K
165J
265L
166K
266L

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
11LEULEUASPASPAA14 - 16728 - 181
21LEULEUASPASPBB14 - 16728 - 181
12LEULEULEULEUAA14 - 16828 - 182
22LEULEULEULEUCC14 - 16828 - 182
13LEULEUASPASPAA14 - 16728 - 181
23LEULEUASPASPDD14 - 16728 - 181
14LEULEULEULEUAA14 - 16828 - 182
24LEULEULEULEUEE14 - 16828 - 182
15LEULEUASPASPAA14 - 16728 - 181
25LEULEUASPASPFF14 - 16728 - 181
16LEULEUASPASPAA14 - 16728 - 181
26LEULEUASPASPGG14 - 16728 - 181
17LEULEUASPASPAA14 - 16728 - 181
27LEULEUASPASPHH14 - 16728 - 181
18LEULEUASPASPAA14 - 16728 - 181
28LEULEUASPASPII14 - 16728 - 181
19LEULEULEULEUAA14 - 16828 - 182
29LEULEULEULEUJJ14 - 16828 - 182
110LEULEUASPASPAA14 - 16728 - 181
210LEULEUASPASPKK14 - 16728 - 181
111LEULEULEULEUAA14 - 16828 - 182
211LEULEULEULEULL14 - 16828 - 182
112LEULEUASPASPBB14 - 16728 - 181
212LEULEUASPASPCC14 - 16728 - 181
113ASNASNLEULEUBB13 - 16827 - 182
213ASNASNLEULEUDD13 - 16827 - 182
114LEULEUASPASPBB14 - 16728 - 181
214LEULEUASPASPEE14 - 16728 - 181
115ASNASNLEULEUBB13 - 16827 - 182
215ASNASNLEULEUFF13 - 16827 - 182
116ASNASNLEULEUBB13 - 16827 - 182
216ASNASNLEULEUGG13 - 16827 - 182
117ASNASNLEULEUBB13 - 16827 - 182
217ASNASNLEULEUHH13 - 16827 - 182
118ASNASNLEULEUBB13 - 16827 - 182
218ASNASNLEULEUII13 - 16827 - 182
119LEULEUASPASPBB14 - 16728 - 181
219LEULEUASPASPJJ14 - 16728 - 181
120ASNASNLEULEUBB13 - 16827 - 182
220ASNASNLEULEUKK13 - 16827 - 182
121LEULEUASPASPBB14 - 16728 - 181
221LEULEUASPASPLL14 - 16728 - 181
122LEULEUASPASPCC14 - 16728 - 181
222LEULEUASPASPDD14 - 16728 - 181
123LEULEULEULEUCC14 - 16828 - 182
223LEULEULEULEUEE14 - 16828 - 182
124LEULEUASPASPCC14 - 16728 - 181
224LEULEUASPASPFF14 - 16728 - 181
125LEULEUASPASPCC14 - 16728 - 181
225LEULEUASPASPGG14 - 16728 - 181
126LEULEUASPASPCC14 - 16728 - 181
226LEULEUASPASPHH14 - 16728 - 181
127LEULEUASPASPCC14 - 16728 - 181
227LEULEUASPASPII14 - 16728 - 181
128LEULEULEULEUCC14 - 16828 - 182
228LEULEULEULEUJJ14 - 16828 - 182
129LEULEUASPASPCC14 - 16728 - 181
229LEULEUASPASPKK14 - 16728 - 181
130LEULEULEULEUCC14 - 16828 - 182
230LEULEULEULEULL14 - 16828 - 182
131LEULEUASPASPDD14 - 16728 - 181
231LEULEUASPASPEE14 - 16728 - 181
132ASNASNLEULEUDD13 - 16827 - 182
232ASNASNLEULEUFF13 - 16827 - 182
133ASNASNLEULEUDD13 - 16827 - 182
233ASNASNLEULEUGG13 - 16827 - 182
134ASNASNLEULEUDD13 - 16827 - 182
234ASNASNLEULEUHH13 - 16827 - 182
135ASNASNLEULEUDD13 - 16827 - 182
235ASNASNLEULEUII13 - 16827 - 182
136LEULEUASPASPDD14 - 16728 - 181
236LEULEUASPASPJJ14 - 16728 - 181
137ASNASNLEULEUDD13 - 16827 - 182
237ASNASNLEULEUKK13 - 16827 - 182
138LEULEUASPASPDD14 - 16728 - 181
238LEULEUASPASPLL14 - 16728 - 181
139LEULEUASPASPEE14 - 16728 - 181
239LEULEUASPASPFF14 - 16728 - 181
140LEULEUASPASPEE14 - 16728 - 181
240LEULEUASPASPGG14 - 16728 - 181
141LEULEUASPASPEE14 - 16728 - 181
241LEULEUASPASPHH14 - 16728 - 181
142LEULEUASPASPEE14 - 16728 - 181
242LEULEUASPASPII14 - 16728 - 181
143LEULEULEULEUEE14 - 16828 - 182
243LEULEULEULEUJJ14 - 16828 - 182
144LEULEUASPASPEE14 - 16728 - 181
244LEULEUASPASPKK14 - 16728 - 181
145LEULEULEULEUEE14 - 16828 - 182
245LEULEULEULEULL14 - 16828 - 182
146ASNASNLEULEUFF13 - 16827 - 182
246ASNASNLEULEUGG13 - 16827 - 182
147ASNASNLEULEUFF13 - 16827 - 182
247ASNASNLEULEUHH13 - 16827 - 182
148ASNASNLEULEUFF13 - 16827 - 182
248ASNASNLEULEUII13 - 16827 - 182
149LEULEUASPASPFF14 - 16728 - 181
249LEULEUASPASPJJ14 - 16728 - 181
150ASNASNLEULEUFF13 - 16827 - 182
250ASNASNLEULEUKK13 - 16827 - 182
151LEULEUASPASPFF14 - 16728 - 181
251LEULEUASPASPLL14 - 16728 - 181
152ASNASNLEULEUGG13 - 16827 - 182
252ASNASNLEULEUHH13 - 16827 - 182
153ASNASNLEULEUGG13 - 16827 - 182
253ASNASNLEULEUII13 - 16827 - 182
154LEULEUASPASPGG14 - 16728 - 181
254LEULEUASPASPJJ14 - 16728 - 181
155ASNASNLEULEUGG13 - 16827 - 182
255ASNASNLEULEUKK13 - 16827 - 182
156LEULEUASPASPGG14 - 16728 - 181
256LEULEUASPASPLL14 - 16728 - 181
157ASNASNLEULEUHH13 - 16827 - 182
257ASNASNLEULEUII13 - 16827 - 182
158LEULEUASPASPHH14 - 16728 - 181
258LEULEUASPASPJJ14 - 16728 - 181
159ASNASNLEULEUHH13 - 16827 - 182
259ASNASNLEULEUKK13 - 16827 - 182
160LEULEUASPASPHH14 - 16728 - 181
260LEULEUASPASPLL14 - 16728 - 181
161LEULEUASPASPII14 - 16728 - 181
261LEULEUASPASPJJ14 - 16728 - 181
162ASNASNLEULEUII13 - 16827 - 182
262ASNASNLEULEUKK13 - 16827 - 182
163LEULEUASPASPII14 - 16728 - 181
263LEULEUASPASPLL14 - 16728 - 181
164LEULEUASPASPJJ14 - 16728 - 181
264LEULEUASPASPKK14 - 16728 - 181
165LEULEULEULEUJJ14 - 16828 - 182
265LEULEULEULEULL14 - 16828 - 182
166LEULEUASPASPKK14 - 16728 - 181
266LEULEUASPASPLL14 - 16728 - 181

NCS ensembles :
ID
1
3
4
5
6
7
8
9
10
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
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
41
42
11
12
2

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Components

#1: Protein
DNA protection during starvation protein,Bacterioferritin / BFR / Cytochrome b-1 / Cytochrome b-557


Mass: 22658.719 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Details: Chimera protein of residues 1-163 from DNA protection during starvation protein (P0ABT2) and residues 138-158 from Bacterioferritin (P0ABD3).
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: dps, pexB, vtm, b0812, JW0797, bfr, b3336, JW3298 / Plasmid: pET-46 / Production host: Escherichia coli (E. coli)
References: UniProt: P0ABT2, UniProt: P0ABD3, Oxidoreductases; Oxidizing metal ions, ferroxidase
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1781 / Source method: isolated from a natural source / Formula: H2O

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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: 2.06 Å3/Da / Density % sol: 40.38 %
Crystal growTemperature: 292.15 K / Method: vapor diffusion / pH: 4.2 / Details: 0.2M lithium sulphate, 18% PEG 1000, pH 4.2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 27, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.075 Å / Relative weight: 1
ReflectionResolution: 1.99→50 Å / Num. obs: 135428 / % possible obs: 92.3 % / Redundancy: 12.8 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 320.3
Reflection shellHighest resolution: 2 Å / Rmerge(I) obs: 0.517

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Processing

Software
NameVersionClassification
REFMAC5.8.0135refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementResolution: 1.99→46.76 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.946 / SU B: 7.259 / SU ML: 0.103 / Cross valid method: THROUGHOUT / ESU R: 0.182 / ESU R Free: 0.151 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20721 7156 5 %RANDOM
Rwork0.17929 ---
obs0.18069 135428 92.33 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 33.276 Å2
Baniso -1Baniso -2Baniso -3
1--0.67 Å2-0 Å20 Å2
2--0.57 Å2-0 Å2
3---0.1 Å2
Refinement stepCycle: 1 / Resolution: 1.99→46.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14780 0 2 1781 16563
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.01914996
X-RAY DIFFRACTIONr_bond_other_d0.0130.0214634
X-RAY DIFFRACTIONr_angle_refined_deg1.881.95120321
X-RAY DIFFRACTIONr_angle_other_deg1.921333499
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.02151855
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.54724.966739
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.874152695
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.3591596
X-RAY DIFFRACTIONr_chiral_restr0.1830.22407
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.0216999
X-RAY DIFFRACTIONr_gen_planes_other0.0090.023393
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_it1.4872.1317456
X-RAY DIFFRACTIONr_mcbond_other1.4852.1317455
X-RAY DIFFRACTIONr_mcangle_it2.0623.1819299
X-RAY DIFFRACTIONr_mcangle_other2.0633.1819300
X-RAY DIFFRACTIONr_scbond_it2.6682.4617540
X-RAY DIFFRACTIONr_scbond_other2.6682.4617541
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.1823.56311023
X-RAY DIFFRACTIONr_long_range_B_refined18.35520.18919564
X-RAY DIFFRACTIONr_long_range_B_other18.35520.1919565
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)
11A193040.04
12B193040.04
21A196120.04
22C196120.04
31A194680.04
32D194680.04
41A193800.04
42E193800.04
51A194940.04
52F194940.04
61A194100.03
62G194100.03
71A193820.04
72H193820.04
81A192120.05
82I192120.05
91A195400.04
92J195400.04
101A193260.04
102K193260.04
111A193920.04
112L193920.04
121B192180.04
122C192180.04
131B194860.04
132D194860.04
141B193460.04
142E193460.04
151B194580.05
152F194580.05
161B193780.05
162G193780.05
171B193540.05
172H193540.05
181B192440.05
182I192440.05
191B192100.04
192J192100.04
201B193100.05
202K193100.05
211B193640.04
212L193640.04
221C195240.03
222D195240.03
231C193020.05
232E193020.05
241C194000.05
242F194000.05
251C193520.04
252G193520.04
261C193600.03
262H193600.03
271C192640.04
272I192640.04
281C195900.04
282J195900.04
291C193460.05
292K193460.05
301C193260.05
302L193260.05
311D191900.04
312E191900.04
321D196240.04
322F196240.04
331D195900.04
332G195900.04
341D195760.04
342H195760.04
351D195220.04
352I195220.04
361D194880.02
362J194880.02
371D195660.04
372K195660.04
381D192180.04
382L192180.04
391E192580.04
392F192580.04
401E191660.05
402G191660.05
411E190800.05
412H190800.05
421E189880.05
422I189880.05
431E193200.04
432J193200.04
441E190760.04
442K190760.04
451E195160.04
452L195160.04
461F196000.04
462G196000.04
471F195240.05
472H195240.05
481F194040.05
482I194040.05
491F193960.04
492J193960.04
501F195260.04
502K195260.04
511F192720.04
512L192720.04
521G195080.04
522H195080.04
531G193780.05
532I193780.05
541G193140.04
542J193140.04
551G194000.05
552K194000.05
561G192380.04
562L192380.04
571H196120.05
572I196120.05
581H192540.05
582J192540.05
591H193740.05
592K193740.05
601H191040.05
602L191040.05
611I193640.03
612J193640.03
621I193300.05
622K193300.05
631I190820.05
632L190820.05
641J193160.04
642K193160.04
651J194140.04
652L194140.04
661K190900.04
662L190900.04
LS refinement shellResolution: 1.99→2.042 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.261 559 -
Rwork0.228 10162 -
obs--95 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.14420.0869-0.19540.28370.03910.4194-0.01810.02840.058-0.02770.03940.092-0.01980.0025-0.02130.10460.02450.0050.05280.02550.09662.20617.27611.583
20.39620.07270.11930.21250.07330.16220.0502-0.01560.06530.00850.0007-0.0047-0.06970.0347-0.05090.1173-0.02760.02020.0431-0.00190.101728.97430.67222.467
30.37750.3183-0.10340.3834-0.12540.29240.03690.00390.06520.12230.00440.0649-0.015-0.0029-0.04140.1774-0.00470.05820.0163-0.02460.06757.55418.84342.949
40.3764-0.06850.02320.2369-0.10280.1297-0.0820.0032-0.0206-0.02190.013-0.02720.1328-0.01790.06910.2264-0.01330.06160.0063-0.01580.07112.639-28.76223.295
50.18310.0795-0.17020.25910.01750.2571-0.0380.04910.0239-0.00360.03390.08780.0458-0.01930.00410.1114-0.01640.0020.0597-0.00290.0735-3.048-3.99610.772
60.12050.069-0.10550.4234-0.16290.2993-0.05830.0671-0.0083-0.08910.0437-0.05880.0919-0.02120.01460.1586-0.01380.06220.055-0.01740.066423.916-14.284-2.792
70.13570.02060.07080.2687-0.07580.13190.01240.0075-0.0046-0.0552-0.012-0.0837-0.01920.0094-0.00040.0655-0.01420.03820.06170.0160.124842.98419.7569.528
80.38860.0348-0.04140.24340.02470.0592-0.00850.0191-0.00250.176-0.03780.01340.09610.00850.04630.2786-0.01010.04330.01390.00920.044812.918-21.63344.008
90.07940.0677-0.00280.66460.0050.1728-0.03220.0385-0.0511-0.05290.0334-0.19040.06570.0415-0.00120.10840.02850.10140.04020.0010.155844.553-11.6764.211
100.2170.183-0.17550.4337-0.00890.2150.0313-0.1077-0.18810.1599-0.1501-0.24160.02050.04690.11880.18680.0152-0.10830.09580.09020.202543.78-13.58545.05
110.25820.21370.04230.44460.08990.15920.0389-0.0540.04790.2256-0.0245-0.02190.04420.0371-0.01450.2446-0.0234-0.02090.0342-0.02220.026121.5566.99355.003
120.02490.0859-0.0560.52660.06110.41880.0195-0.0311-0.05970.0936-0.091-0.2564-0.03620.0820.07140.0570.014-0.07240.08620.03990.184154.6840.30331.959
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A14 - 168
2X-RAY DIFFRACTION2B13 - 168
3X-RAY DIFFRACTION3C14 - 168
4X-RAY DIFFRACTION4D13 - 168
5X-RAY DIFFRACTION5E14 - 168
6X-RAY DIFFRACTION6F13 - 168
7X-RAY DIFFRACTION7G13 - 168
8X-RAY DIFFRACTION8H13 - 168
9X-RAY DIFFRACTION9I13 - 168
10X-RAY DIFFRACTION10J14 - 168
11X-RAY DIFFRACTION11K13 - 168
12X-RAY DIFFRACTION12L14 - 168

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