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- PDB-2xka: Crystal structure of a GTPyS-form protofilament of Bacillus thuri... -

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Basic information

Entry
Database: PDB / ID: 2xka
TitleCrystal structure of a GTPyS-form protofilament of Bacillus thuringiensis serovar israelensis TubZ
ComponentsFTSZ/TUBULIN-RELATED PROTEIN
KeywordsSTRUCTURAL PROTEIN / MOTOR PROTEIN / CYTOSKELETON / CYTOMOTIVE / DNA SEGREGATION / MICROTUBULE / PBTOXIS / PBT156 / REPX / TUBR
Function / homology
Function and homology information


plasmid partitioning / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / GTPase activity / GTP binding / metal ion binding / identical protein binding / cytoplasm
Similarity search - Function
: / Tubulin/FtsZ-like protein TubZ-like, C-terminal domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE / Tubulin-like protein TubZ
Similarity search - Component
Biological speciesBACILLUS THURINGIENSIS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3 Å
AuthorsAylett, C.H.S. / Lowe, J.
CitationJournal: Proc Natl Acad Sci U S A / Year: 2010
Title: Filament structure of bacterial tubulin homologue TubZ.
Authors: Christopher H S Aylett / Qing Wang / Katharine A Michie / Linda A Amos / Jan Löwe /
Abstract: Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a ...Low copy number plasmids often depend on accurate partitioning systems for their continued survival. Generally, such systems consist of a centromere-like region of DNA, a DNA-binding adaptor, and a polymerizing cytomotive filament. Together these components drive newly replicated plasmids to opposite ends of the dividing cell. The Bacillus thuringiensis plasmid pBToxis relies on a filament of the tubulin/FtsZ-like protein TubZ for its segregation. By combining crystallography and electron microscopy, we have determined the structure of this filament. We explain how GTP hydrolysis weakens the subunit-subunit contact and also shed light on the partitioning of the plasmid-adaptor complex. The double helical superstructure of TubZ filaments is unusual for tubulin-like proteins. Filaments of ParM, the actin-like partitioning protein, are also double helical. We suggest that convergent evolution shapes these different types of cytomotive filaments toward a general mechanism for plasmid separation.
History
DepositionJul 7, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 10, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 24, 2018Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name ..._entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.4May 8, 2024Group: 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_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.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
A: FTSZ/TUBULIN-RELATED PROTEIN
B: FTSZ/TUBULIN-RELATED PROTEIN
C: FTSZ/TUBULIN-RELATED PROTEIN
D: FTSZ/TUBULIN-RELATED PROTEIN
E: FTSZ/TUBULIN-RELATED PROTEIN
F: FTSZ/TUBULIN-RELATED PROTEIN
G: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)335,25521
Polymers331,3107
Non-polymers3,94514
Water00
1
A: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
7
G: FTSZ/TUBULIN-RELATED PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8943
Polymers47,3301
Non-polymers5642
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)51.060, 85.150, 632.230
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
31C
41D
51E
61F
71G

NCS domain segments:

Ens-ID: 1 / Refine code: 3

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNASNASNAA4 - 154 - 15
21ASNASNASNASNBB4 - 154 - 15
31ASNASNASNASNCC4 - 154 - 15
41ASNASNASNASNDD4 - 154 - 15
51ASNASNASNASNEE4 - 154 - 15
61ASNASNASNASNFF4 - 154 - 15
71ASNASNASNASNGG4 - 154 - 15
12VALVALGLYGLYAA18 - 3118 - 31
22VALVALGLYGLYBB18 - 3118 - 31
32VALVALGLYGLYCC18 - 3118 - 31
42VALVALGLYGLYDD18 - 3118 - 31
52VALVALGLYGLYEE18 - 3118 - 31
62VALVALGLYGLYFF18 - 3118 - 31
72VALVALGLYGLYGG18 - 3118 - 31
13LYSLYSVALVALAA33 - 5833 - 58
23LYSLYSVALVALBB33 - 5833 - 58
33LYSLYSVALVALCC33 - 5833 - 58
43LYSLYSVALVALDD33 - 5833 - 58
53LYSLYSVALVALEE33 - 5833 - 58
63LYSLYSVALVALFF33 - 5833 - 58
73LYSLYSVALVALGG33 - 5833 - 58
14METMETILEILEAA66 - 7766 - 77
24METMETILEILEBB66 - 7766 - 77
34METMETILEILECC66 - 7766 - 77
44METMETILEILEDD66 - 7766 - 77
54METMETILEILEEE66 - 7766 - 77
64METMETILEILEFF66 - 7766 - 77
74METMETILEILEGG66 - 7766 - 77
15ILEILEGLYGLYAA127 - 144127 - 144
25ILEILEGLYGLYBB127 - 144127 - 144
35ILEILEGLYGLYCC127 - 144127 - 144
45ILEILEGLYGLYDD127 - 144127 - 144
55ILEILEGLYGLYEE127 - 144127 - 144
65ILEILEGLYGLYFF127 - 144127 - 144
75ILEILEGLYGLYGG127 - 144127 - 144
16GLYGLYILEILEAA146 - 153146 - 153
26GLYGLYILEILEBB146 - 153146 - 153
36GLYGLYILEILECC146 - 153146 - 153
46GLYGLYILEILEDD146 - 153146 - 153
56GLYGLYILEILEEE146 - 153146 - 153
66GLYGLYILEILEFF146 - 153146 - 153
76GLYGLYILEILEGG146 - 153146 - 153
17GLNGLNGLUGLUAA156 - 175156 - 175
27GLNGLNGLUGLUBB156 - 175156 - 175
37GLNGLNGLUGLUCC156 - 175156 - 175
47GLNGLNGLUGLUDD156 - 175156 - 175
57GLNGLNGLUGLUEE156 - 175156 - 175
67GLNGLNGLUGLUFF156 - 175156 - 175
77GLNGLNGLUGLUGG156 - 175156 - 175
18ASNASNSERSERAA178 - 222178 - 222
28ASNASNSERSERBB178 - 222178 - 222
38ASNASNSERSERCC178 - 222178 - 222
48ASNASNSERSERDD178 - 222178 - 222
58ASNASNSERSEREE178 - 222178 - 222
68ASNASNSERSERFF178 - 222178 - 222
78ASNASNSERSERGG178 - 222178 - 222
19TRPTRPPROPROAA236 - 255236 - 255
29TRPTRPPROPROBB236 - 255236 - 255
39TRPTRPPROPROCC236 - 255236 - 255
49TRPTRPPROPRODD236 - 255236 - 255
59TRPTRPPROPROEE236 - 255236 - 255
69TRPTRPPROPROFF236 - 255236 - 255
79TRPTRPPROPROGG236 - 255236 - 255
110PROPROILEILEAA267 - 288267 - 288
210PROPROILEILEBB267 - 288267 - 288
310PROPROILEILECC267 - 288267 - 288
410PROPROILEILEDD267 - 288267 - 288
510PROPROILEILEEE267 - 288267 - 288
610PROPROILEILEFF267 - 288267 - 288
710PROPROILEILEGG267 - 288267 - 288
111ILEILESERSERAA300 - 329300 - 329
211ILEILESERSERBB300 - 329300 - 329
311ILEILESERSERCC300 - 329300 - 329
411ILEILESERSERDD300 - 329300 - 329
511ILEILESERSEREE300 - 329300 - 329
611ILEILESERSERFF300 - 329300 - 329
711ILEILESERSERGG300 - 329300 - 329
112ARGARGTYRTYRAA344 - 350344 - 350
212ARGARGTYRTYRBB344 - 350344 - 350
312ARGARGTYRTYRCC344 - 350344 - 350
412ARGARGTYRTYRDD344 - 350344 - 350
512ARGARGTYRTYREE344 - 350344 - 350
612ARGARGTYRTYRFF344 - 350344 - 350
712ARGARGTYRTYRGG344 - 350344 - 350
113LYSLYSPROPROAA359 - 363359 - 363
213LYSLYSPROPROBB359 - 363359 - 363
313LYSLYSPROPROCC359 - 363359 - 363
413LYSLYSPROPRODD359 - 363359 - 363
513LYSLYSPROPROEE359 - 363359 - 363
613LYSLYSPROPROFF359 - 363359 - 363
713LYSLYSPROPROGG359 - 363359 - 363
114VALVALALAALAAA371 - 389371 - 389
214VALVALALAALABB371 - 389371 - 389
314VALVALALAALACC371 - 389371 - 389
414VALVALALAALADD371 - 389371 - 389
514VALVALALAALAEE371 - 389371 - 389
614VALVALALAALAFF371 - 389371 - 389
714VALVALALAALAGG371 - 389371 - 389

NCS oper:
IDCodeMatrixVector
1given(0.26475, 0.95429, -0.13871), (-0.95798, 0.27675, 0.07546), (0.1104, 0.11291, 0.98745)88.2923, -2.9732, -132.61496
2given(0.65757, 0.74534, -0.1099), (-0.75126, 0.65967, -0.02119), (0.0567, 0.0965, 0.99372)54.93379, 20.43809, -87.99482
3given(0.90991, 0.38724, 0.1487), (-0.38073, 0.92194, -0.07118), (-0.16466, 0.00816, 0.98632)-4.94514, 23.07034, -36.36363
4given(0.91676, -0.3935, -0.06865), (0.3923, 0.91932, -0.03076), (0.07521, 0.00127, 0.99717)-5.32271, -15.02204, 42.63932
5given(0.6764, -0.73578, -0.03337), (0.73287, 0.67686, -0.06902), (0.07337, 0.02223, 0.99706)-18.15366, -35.0983, 88.28479
6given(0.2767, -0.95845, 0.06936), (0.95273, 0.28304, 0.11047), (-0.12551, 0.03551, 0.99146)-27.8295, -84.21684, 142.40529

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Components

#1: Protein
FTSZ/TUBULIN-RELATED PROTEIN / TUBZ


Mass: 47330.051 Da / Num. of mol.: 7 / Fragment: RESIDUES 1-421 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: GSP, MG / Source: (gene. exp.) BACILLUS THURINGIENSIS (bacteria) / Strain: SEROVAR ISRAELENSIS / Description: J. POGLIANO LABORATORY UCSD / Plasmid: PET28A / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q8KNP3
#2: Chemical
ChemComp-GSP / 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE


Mass: 539.246 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C10H16N5O13P3S
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
Compound detailsENGINEERED RESIDUE IN CHAIN A, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN B, LEU 2 TO VAL ENGINEERED ...ENGINEERED RESIDUE IN CHAIN A, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN B, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN C, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN D, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN E, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN F, LEU 2 TO VAL ENGINEERED RESIDUE IN CHAIN G, LEU 2 TO VAL
Nonpolymer detailsMG: C999 IS ALSO BOUND TO OD2 ATOM OF ASP C64.
Sequence detailsL2V, DELTA422-484

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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: 2.08 Å3/Da / Density % sol: 40.85 % / Description: 52 SE SITES FOR SE SAD
Crystal growpH: 8.5 / Details: TRISCL PH 8.5 200 MM MGCL2 30% PEG 400 WV

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9395
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 1, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9395 Å / Relative weight: 1
ReflectionResolution: 3→52.69 Å / Num. obs: 52941 / % possible obs: 93.2 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 47.86 Å2 / Rmerge(I) obs: 0.12 / Rsym value: 0.122 / Net I/σ(I): 7.4
Reflection shellResolution: 3→3.16 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 3.6 / Rsym value: 0.339 / % possible all: 71

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
SHELXphasing
SOLVERESOLVEphasing
REFMAC5.5.0109refinement
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 3→50 Å / Cor.coef. Fo:Fc: 0.884 / Cor.coef. Fo:Fc free: 0.834 / SU B: 24.492 / SU ML: 0.45 / Cross valid method: THROUGHOUT / ESU R Free: 0.598 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.28438 2649 5 %RANDOM
Rwork0.23198 ---
obs0.23459 50190 92.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 24.013 Å2
Baniso -1Baniso -2Baniso -3
1-6.12 Å20 Å20 Å2
2---2.64 Å20 Å2
3----3.48 Å2
Refinement stepCycle: LAST / Resolution: 3→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22407 0 231 0 22638
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02223073
X-RAY DIFFRACTIONr_bond_other_d0.0020.0215500
X-RAY DIFFRACTIONr_angle_refined_deg1.3331.96531256
X-RAY DIFFRACTIONr_angle_other_deg0.972337798
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.67752819
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.37525.0721181
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.522153951
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.43315136
X-RAY DIFFRACTIONr_chiral_restr0.0760.23405
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0225817
X-RAY DIFFRACTIONr_gen_planes_other0.0020.024563
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_refined0.1550.2465
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.030.23
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2130.278
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2590.2180
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1940.214
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5683.514044
X-RAY DIFFRACTIONr_mcbond_other0.0593.55772
X-RAY DIFFRACTIONr_mcangle_it1.054422624
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.80159029
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.4526.58632
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 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1513tight positional0.030.05
2B1513tight positional0.030.05
3C1513tight positional0.030.05
4D1513tight positional0.030.05
5E1513tight positional0.030.05
6F1513tight positional0.030.05
7G1513tight positional0.030.05
1A1874loose positional0.035
2B1874loose positional0.035
3C1874loose positional0.035
4D1874loose positional0.035
5E1874loose positional0.035
6F1874loose positional0.035
7G1874loose positional0.035
1A1513tight thermal0.050.5
2B1513tight thermal0.060.5
3C1513tight thermal0.060.5
4D1513tight thermal0.050.5
5E1513tight thermal0.060.5
6F1513tight thermal0.060.5
7G1513tight thermal0.050.5
1A1874loose thermal0.0410
2B1874loose thermal0.0410
3C1874loose thermal0.0510
4D1874loose thermal0.0410
5E1874loose thermal0.0410
6F1874loose thermal0.0510
7G1874loose thermal0.0410
LS refinement shellResolution: 3→3.078 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.378 141 -
Rwork0.321 2602 -
obs--67.66 %

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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