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- PDB-2jd8: Crystal Structure of the Zn-soaked Ferritin from the Hyperthermop... -

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Basic information

Entry
Database: PDB / ID: 2jd8
TitleCrystal Structure of the Zn-soaked Ferritin from the Hyperthermophilic Archaeal Anaerobe Pyrococcus furiosus
ComponentsFERRITIN HOMOLOG
KeywordsMETAL TRANSPORT / FERRITIN / IRON / ARCHAEON / HYPERTHERMOPHILE / FERROXIDASE CENTER / THERMOSTABILITY / ENTRY CHANNELS / PORES METAL TRANSPORT
Function / homology
Function and homology information


intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / ferrous iron binding / iron ion transport / cytosol
Similarity search - Function
Ferritin, prokaryotic-type / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily ...Ferritin, prokaryotic-type / Ferritin, core subunit, four-helix bundle / Ferritin / 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
: / Ferritin homolog
Similarity search - Component
Biological speciesPYROCOCCUS FURIOSUS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsTatur, J. / Hagen, W.R. / Matias, P.M.
Citation
Journal: J.Biol.Inorg.Chem. / Year: 2007
Title: Crystal Structure of the Ferritin from the Hyperthermophilic Archaeal Anaerobe Pyrococcus Furiosus
Authors: Tatur, J. / Hagen, W.R. / Matias, P.M.
#1: Journal: Acta Crystallogr.,Sect.F / Year: 2005
Title: Crystallization and Preliminary X-Ray Characterization of a Ferritin from the Hyperthermophilic Archaeon and Anaerobe Pyrococcus Furiosus
Authors: Matias, P.M. / Tatur, J. / Carrondo, M.A. / Hagen, W.R.
History
DepositionJan 5, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 27, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: FERRITIN HOMOLOG
1: FERRITIN HOMOLOG
2: FERRITIN HOMOLOG
3: FERRITIN HOMOLOG
4: FERRITIN HOMOLOG
5: FERRITIN HOMOLOG
6: FERRITIN HOMOLOG
7: FERRITIN HOMOLOG
8: FERRITIN HOMOLOG
9: FERRITIN HOMOLOG
A: FERRITIN HOMOLOG
B: FERRITIN HOMOLOG
C: FERRITIN HOMOLOG
D: FERRITIN HOMOLOG
E: FERRITIN HOMOLOG
F: FERRITIN HOMOLOG
G: FERRITIN HOMOLOG
H: FERRITIN HOMOLOG
I: FERRITIN HOMOLOG
J: FERRITIN HOMOLOG
K: FERRITIN HOMOLOG
L: FERRITIN HOMOLOG
M: FERRITIN HOMOLOG
N: FERRITIN HOMOLOG
O: FERRITIN HOMOLOG
P: FERRITIN HOMOLOG
Q: FERRITIN HOMOLOG
R: FERRITIN HOMOLOG
S: FERRITIN HOMOLOG
T: FERRITIN HOMOLOG
U: FERRITIN HOMOLOG
V: FERRITIN HOMOLOG
W: FERRITIN HOMOLOG
X: FERRITIN HOMOLOG
Y: FERRITIN HOMOLOG
Z: FERRITIN HOMOLOG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)742,939188
Polymers731,99236
Non-polymers10,947152
Water2,918162
1
0: FERRITIN HOMOLOG
1: FERRITIN HOMOLOG
2: FERRITIN HOMOLOG
3: FERRITIN HOMOLOG
4: FERRITIN HOMOLOG
5: FERRITIN HOMOLOG
6: FERRITIN HOMOLOG
7: FERRITIN HOMOLOG
8: FERRITIN HOMOLOG
9: FERRITIN HOMOLOG
G: FERRITIN HOMOLOG
H: FERRITIN HOMOLOG
I: FERRITIN HOMOLOG
J: FERRITIN HOMOLOG
K: FERRITIN HOMOLOG
L: FERRITIN HOMOLOG
M: FERRITIN HOMOLOG
N: FERRITIN HOMOLOG
O: FERRITIN HOMOLOG
P: FERRITIN HOMOLOG
Q: FERRITIN HOMOLOG
R: FERRITIN HOMOLOG
Y: FERRITIN HOMOLOG
Z: FERRITIN HOMOLOG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)494,973122
Polymers487,99524
Non-polymers6,97898
Water37821
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
A: FERRITIN HOMOLOG
B: FERRITIN HOMOLOG
C: FERRITIN HOMOLOG
D: FERRITIN HOMOLOG
E: FERRITIN HOMOLOG
F: FERRITIN HOMOLOG
S: FERRITIN HOMOLOG
T: FERRITIN HOMOLOG
U: FERRITIN HOMOLOG
V: FERRITIN HOMOLOG
W: FERRITIN HOMOLOG
X: FERRITIN HOMOLOG
hetero molecules

A: FERRITIN HOMOLOG
B: FERRITIN HOMOLOG
C: FERRITIN HOMOLOG
D: FERRITIN HOMOLOG
E: FERRITIN HOMOLOG
F: FERRITIN HOMOLOG
S: FERRITIN HOMOLOG
T: FERRITIN HOMOLOG
U: FERRITIN HOMOLOG
V: FERRITIN HOMOLOG
W: FERRITIN HOMOLOG
X: FERRITIN HOMOLOG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)495,933132
Polymers487,99524
Non-polymers7,938108
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
MethodPQS
Unit cell
Length a, b, c (Å)255.371, 342.055, 265.986
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L
131M
141N
151O
161P
171Q
181R
191S
201T
211U
221V
231W
241X
251Y
261Z
2710
2811
2912
3013
3114
3215
3316
3417
3518
3619

NCS domain segments:

Ens-ID: 1 / Beg auth comp-ID: GLU / Beg label comp-ID: GLU / Refine code: 1

Dom-IDComponent-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUAK1717
21GLUGLUBL1717
31GLUGLUCM1717
41GLUGLUDN1717
51GLUGLUEO1717
61GLUGLUFP1717
71GLUGLUGQ1717
81GLUGLUHR1717
91GLUGLUIS1717
101GLUGLUJT1717
111GLUGLUKU1717
121GLUGLULV1717
131GLUGLUMW1717
141GLUGLUNX1717
151GLUGLUOY1717
161GLUGLUPZ1717
171GLUGLUQAA1717
181GLUGLURBA1717
194GLUGLUSCA1717
204GLUGLUTDA1717
214GLUGLUUEA1717
224GLUGLUVFA1717
234GLUGLUWGA1717
244GLUGLUXHA1717
254GLUGLUYIA1717
264GLUGLUZJA1717
274GLUGLU0A1717
284GLUGLU1B1717
294GLUGLU2C1717
304GLUGLU3D1717
314GLUGLU4E1717
324GLUGLU5F1717
334GLUGLU6G1717
344GLUGLU7H1717
354GLUGLU8I1717
364GLUGLU9J1717
12HISHISAK49 - 5349 - 53
22HISHISBL49 - 5349 - 53
32HISHISCM49 - 5349 - 53
42HISHISDN49 - 5349 - 53
52HISHISEO49 - 5349 - 53
62HISHISFP49 - 5349 - 53
72HISHISGQ49 - 5349 - 53
82HISHISHR49 - 5349 - 53
92HISHISIS49 - 5349 - 53
102HISHISJT49 - 5349 - 53
112HISHISKU49 - 5349 - 53
122HISHISLV49 - 5349 - 53
132HISHISMW49 - 5349 - 53
142HISHISNX49 - 5349 - 53
152HISHISOY49 - 5349 - 53
162HISHISPZ49 - 5349 - 53
172HISHISQAA49 - 5349 - 53
182HISHISRBA49 - 5349 - 53
195HISHISSCA49 - 5349 - 53
205HISHISTDA49 - 5349 - 53
215HISHISUEA49 - 5349 - 53
225HISHISVFA49 - 5349 - 53
235HISHISWGA49 - 5349 - 53
245HISHISXHA49 - 5349 - 53
255HISHISYIA49 - 5349 - 53
265HISHISZJA49 - 5349 - 53
275HISHIS0A49 - 5349 - 53
285HISHIS1B49 - 5349 - 53
295HISHIS2C49 - 5349 - 53
305HISHIS3D49 - 5349 - 53
315HISHIS4E49 - 5349 - 53
325HISHIS5F49 - 5349 - 53
335HISHIS6G49 - 5349 - 53
345HISHIS7H49 - 5349 - 53
355HISHIS8I49 - 5349 - 53
365HISHIS9J49 - 5349 - 53
13GLUGLUAK126 - 130126 - 130
23GLUGLUBL126 - 130126 - 130
33GLUGLUCM126 - 130126 - 130
43GLUGLUDN126 - 130126 - 130
53GLUGLUEO126 - 130126 - 130
63GLUGLUFP126 - 130126 - 130
73GLUGLUGQ126 - 130126 - 130
83GLUGLUHR126 - 130126 - 130
93GLUGLUIS126 - 130126 - 130
103GLUGLUJT126 - 130126 - 130
113GLUGLUKU126 - 130126 - 130
123GLUGLULV126 - 130126 - 130
133GLUGLUMW126 - 130126 - 130
143GLUGLUNX126 - 130126 - 130
153GLUGLUOY126 - 130126 - 130
163GLUGLUPZ126 - 130126 - 130
173GLUGLUQAA126 - 130126 - 130
183GLUGLURBA126 - 130126 - 130
196GLUGLUSCA126 - 130126 - 130
206GLUGLUTDA126 - 130126 - 130
216GLUGLUUEA126 - 130126 - 130
226GLUGLUVFA126 - 130126 - 130
236GLUGLUWGA126 - 130126 - 130
246GLUGLUXHA126 - 130126 - 130
256GLUGLUYIA126 - 130126 - 130
266GLUGLUZJA126 - 130126 - 130
276GLUGLU0A126 - 130126 - 130
286GLUGLU1B126 - 130126 - 130
296GLUGLU2C126 - 130126 - 130
306GLUGLU3D126 - 130126 - 130
316GLUGLU4E126 - 130126 - 130
326GLUGLU5F126 - 130126 - 130
336GLUGLU6G126 - 130126 - 130
346GLUGLU7H126 - 130126 - 130
356GLUGLU8I126 - 130126 - 130
366GLUGLU9J126 - 130126 - 130
17GLUGLUAK9494
27GLUGLUBL9494
37GLUGLUCM9494
47GLUGLUDN9494
57GLUGLUEO9494
67GLUGLUFP9494
77GLUGLUGQ9494
87GLUGLUHR9494
97GLUGLUIS9494
107GLUGLUJT9494
117GLUGLUKU9494
127GLUGLULV9494
137GLUGLUMW9494
147GLUGLUNX9494
157GLUGLUOY9494
167GLUGLUPZ9494
177GLUGLUQAA9494
187GLUGLURBA9494
198GLUGLUSCA9494
208GLUGLUTDA9494
218GLUGLUUEA9494
228GLUGLUVFA9494
238GLUGLUWGA9494
248GLUGLUXHA9494
258GLUGLUYIA9494
268GLUGLUZJA9494
278GLUGLU0A9494
288GLUGLU1B9494
298GLUGLU2C9494
308GLUGLU3D9494
318GLUGLU4E9494
328GLUGLU5F9494
338GLUGLU6G9494
348GLUGLU7H9494
358GLUGLU8I9494
368GLUGLU9J9494

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Components

#1: Protein ...
FERRITIN HOMOLOG / FERRITIN


Mass: 20333.123 Da / Num. of mol.: 36
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PYROCOCCUS FURIOSUS (archaea) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q8U2T8
#2: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 72 / Source method: obtained synthetically / Formula: Zn
#3: Chemical...
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: Fe
#4: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 44 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 162 / 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: 4 Å3/Da / Density % sol: 69.2 %
Crystal growDetails: THE CRYSTALS USED FOR DATA COLLECTION WERE GROWN AGAINST 0.5 ML OF 2 M AMMONIUM SULPHATE RESERVOIR SOLUTION, WITH DROPS CONTAINING 2 MICROL ITERS OF 5 MG/ML PROTEIN SOLUTION IN 50 MM HEPES, ...Details: THE CRYSTALS USED FOR DATA COLLECTION WERE GROWN AGAINST 0.5 ML OF 2 M AMMONIUM SULPHATE RESERVOIR SOLUTION, WITH DROPS CONTAINING 2 MICROL ITERS OF 5 MG/ML PROTEIN SOLUTION IN 50 MM HEPES, PH 7 AND EQUAL AMOUNT OF THE RESERVOIR SOLUTION. ZINC SOAKING OF FERRITIN CRYSTALS WAS PERFORMED BY TRANSFERRING THEM TO A 10-20 MICROLITER DROP OF A SOLUTION WITH COMPOSITION 20 MM ZNCL2, 25 % GLYCEROL AND 2 M AMMONIUM SULFATE, FOR 15 MINUTES.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1.281
DetectorType: MARRESEARCH / Detector: CCD / Date: Jun 25, 2006 / Details: COLLIMATING AND FOCUSSING MIRRORS
RadiationMonochromator: CHANNEL-CUT SI(III) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.281 Å / Relative weight: 1
ReflectionResolution: 2.8→42.9 Å / Num. obs: 279537 / % possible obs: 98.7 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 58.5 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 8.8
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 3 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 2.5 / % possible all: 91.6

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Processing

Software
NameVersionClassification
REFMAC5.3.0021refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2JD6

2jd6


Resolution: 2.8→204.12 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.878 / SU B: 11.078 / SU ML: 0.22 / Cross valid method: THROUGHOUT / ESU R: 0.509 / ESU R Free: 0.312 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: ELECTRON DENSITY FOR C-TERMINAL RESIDUES BEYOND 167 (667) WAS NOT VISIBLE.
RfactorNum. reflection% reflectionSelection details
Rfree0.251 14134 5.1 %RANDOM
Rwork0.2 ---
obs0.203 265356 98.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 32.53 Å2
Baniso -1Baniso -2Baniso -3
1-1.31 Å20 Å20 Å2
2---0.65 Å20 Å2
3----0.67 Å2
Refinement stepCycle: LAST / Resolution: 2.8→204.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49788 0 328 162 50278
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02251310
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.4791.9869165
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.60356004
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.10124.752678
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.198159376
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.515253
X-RAY DIFFRACTIONr_chiral_restr0.1020.26998
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0239385
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2330.225276
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3220.235079
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.130.21681
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2090.2166
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2080.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.03330943
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.324.548070
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.705623671
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it6.988921081
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

Ens-ID: 1 / Number: 202 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDTypeRms dev position (Å)Weight position
1Atight positional0.10.1
2Btight positional0.10.1
3Ctight positional0.10.1
4Dtight positional0.10.1
5Etight positional0.10.1
6Ftight positional0.10.1
7Gtight positional0.10.1
8Htight positional0.10.1
9Itight positional0.10.1
10Jtight positional0.10.1
11Ktight positional0.10.1
12Ltight positional0.10.1
13Mtight positional0.10.1
14Ntight positional0.10.1
15Otight positional0.10.1
16Ptight positional0.10.1
17Qtight positional0.10.1
18Rtight positional0.10.1
19Stight positional0.10.1
20Ttight positional0.10.1
21Utight positional0.10.1
22Vtight positional0.10.1
23Wtight positional0.10.1
24Xtight positional0.10.1
25Ytight positional0.10.1
26Ztight positional0.10.1
270tight positional0.10.1
281tight positional0.10.1
292tight positional0.10.1
303tight positional0.10.1
314tight positional0.10.1
325tight positional0.10.1
336tight positional0.10.1
347tight positional0.10.1
358tight positional0.10.1
369tight positional0.10.1
1Atight thermal0.541
2Btight thermal0.510
3Ctight thermal0.550
4Dtight thermal0.50
5Etight thermal0.70
6Ftight thermal0.510
7Gtight thermal0.560
8Htight thermal0.740
9Itight thermal0.410
10Jtight thermal0.380
11Ktight thermal0.470
12Ltight thermal0.360
13Mtight thermal0.570
14Ntight thermal0.490
15Otight thermal0.680
16Ptight thermal0.520
17Qtight thermal0.450
18Rtight thermal0.440
19Stight thermal0.541
20Ttight thermal0.510
21Utight thermal0.550
22Vtight thermal0.50
23Wtight thermal0.70
24Xtight thermal0.510
25Ytight thermal0.560
26Ztight thermal0.740
270tight thermal0.410
281tight thermal0.380
292tight thermal0.470
303tight thermal0.360
314tight thermal0.570
325tight thermal0.490
336tight thermal0.680
347tight thermal0.520
358tight thermal0.450
369tight thermal0.440
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.373 964
Rwork0.304 17471

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