PDB-4ag5: Structure of VirB4 of Thermoanaerobacter pseudethanolicus

ID or keywords:

Entry

Database: PDB / ID: 4ag5

Title

Structure of VirB4 of Thermoanaerobacter pseudethanolicus

Components

TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

Keywords

HYDROLASE /

TYPE IV SECRETION / CONJUGATION

Function / homology

Function and homology information

nucleotide binding /

metal ion binding
Similarity search - Function

Biological species

THERMOANAEROBACTER PSEUDETHANOLICUS (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.45 Å

Authors

Wallden, K. / Williams, R. / Yan, J. / Lian, P.W. / Wang, L. / Thalassinos, K. / Orlova, E.V. / Waksman, G.

Citation

Journal: Proc Natl Acad Sci U S A / Year: 2012
Title: Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.
Authors: Karin Walldén / Robert Williams / Jun Yan / Pei W Lian / Luchun Wang / Konstantinos Thalassinos / Elena V Orlova / Gabriel Waksman /

Abstract: Type IV secretion (T4S) systems mediate the transfer of proteins and DNA across the cell envelope of bacteria. These systems play important roles in bacterial pathogenesis and in horizontal transfer ...

History

Deposition	Jan 24, 2012	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 4, 2012	Provider: repository / Type: Initial release
Revision 1.1	Jul 25, 2012	Group: Database references
Revision 1.2	Dec 20, 2023	Group: 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 / struct_conn / 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 / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4ag5.cif.gz	520.2 KB	Display	PDBx/mmCIF format
PDB format	pdb4ag5.ent.gz	427.6 KB	Display	PDB format
PDBx/mmJSON format	4ag5.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ag/4ag5 ftp://data.pdbj.org/pub/pdb/validation_reports/ag/4ag5	HTTPS FTP

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Related structure data

Related structure data	2136C 2137C 4ag6SC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	3i09-d 4ag6-2 1hjw-d 5gm8-d 1pe9-d 2iry-d 1ce2-d 1pzx-d 2ag2-d 2wt2-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

B: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

C: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

D: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

hetero molecules

178 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

D: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

hetero molecules

defined by author&software
89.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

C: TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN

hetero molecules

defined by author&software
88.9 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	108.080, 110.800, 156.430
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	18
Space group name H-M	P22₁2₁

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Protein , 1 types, 4 molecules ABCD

#1: Protein	TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN / VIRB4 ATPASE Mass: 44165.949 Da / Num. of mol.: 4 / Fragment: ATPASE DOMAIN, RESIDUES 203-594 Source method: isolated from a genetically manipulated source Source: (gene. exp.) THERMOANAEROBACTER PSEUDETHANOLICUS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: B0KAW2

#1: Protein

TYPE IV SECRETORY PATHWAY VIRB4 COMPONENTS-LIKE PROTEIN / VIRB4 ATPASE

Mass: 44165.949 Da / Num. of mol.: 4 / Fragment: ATPASE DOMAIN, RESIDUES 203-594
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

THERMOANAEROBACTER PSEUDETHANOLICUS (bacteria)
Production host:

ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: B0KAW2

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Non-polymers , 5 types, 170 molecules

#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₃H₈O₃
#4: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Comment: ADP, energy-carrying molecule*YM
#5: Chemical	ChemComp-SO4 / SULFATE ION / Sulfate Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO₄
#6: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 161 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.7 Å³/Da / Density % sol: 54 % / Description: NONE

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9173
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 22, 2011
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9173 Å / Relative weight: 1
Reflection	Resolution: 2.45→54.04 Å / Num. obs: 69350 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / B_iso Wilson estimate: 46.15 Å² / R_merge(I) obs: 0.06 / Net I/σ(I): 14.3
Reflection shell	Resolution: 2.45→2.58 Å / Redundancy: 4.8 % / R_merge(I) obs: 0.49 / Mean I/σ(I) obs: 3 / % possible all: 99.5

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
MOSFLM		data reduction
SCALA		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4AG6

4ag6

Resolution: 2.45→54.04 Å / SU ML: 0.38 / σ(F): 0 / Phase error: 30.32 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2877	3374	5.1 %
R_work	0.2334	-	-
obs	0.2362	66795	95.85 %

Solvent computation

Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 58.709 Å² / k_sol: 0.327 e/Å³

Displacement parameters

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-6.8478 Å²	0 Å²	0 Å²
2-	-	16.8289 Å²	0 Å²
3-	-	-	-9.9811 Å²

Refinement step

Cycle: LAST / Resolution: 2.45→54.04 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9842	0	80	161	10083

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.009	10115
X-RAY DIFFRACTION	f_angle_d	1.152	13774
X-RAY DIFFRACTION	f_dihedral_angle_d	16.049	3584
X-RAY DIFFRACTION	f_chiral_restr	0.069	1574
X-RAY DIFFRACTION	f_plane_restr	0.005	1762

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.45-2.5376	0.3266	278	0.2837	5796	X-RAY DIFFRACTION	88
2.5376-2.6392	0.3657	320	0.2878	5764	X-RAY DIFFRACTION	89
2.6392-2.7593	0.3164	348	0.2537	6054	X-RAY DIFFRACTION	93
2.7593-2.9047	0.319	359	0.255	6268	X-RAY DIFFRACTION	96
2.9047-3.0867	0.3354	342	0.2541	6434	X-RAY DIFFRACTION	98
3.0867-3.325	0.2956	352	0.2298	6472	X-RAY DIFFRACTION	99
3.325-3.6596	0.263	338	0.2208	6567	X-RAY DIFFRACTION	99
3.6596-4.1889	0.2655	372	0.21	6502	X-RAY DIFFRACTION	98
4.1889-5.2769	0.2488	329	0.1971	6697	X-RAY DIFFRACTION	100
5.2769-54.0531	0.3008	336	0.2588	6867	X-RAY DIFFRACTION	99

Refinement TLS params.

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

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	0.1427	0.0588	0.1498	0.2938	0.4041	0.3423	0.4892	-0.2968	0.508	-0.0462	-0.1357	0.0242	-0.4942	-0.208	-0.0003	0.3446	0.1044	0.0385	0.2421	-0.0871	0.3407	4.6763	36.2952	70.8798
2	0.2261	0.4566	-0.0526	1.0884	-0.2537	0.0819	0.0707	0.0373	-0.0266	-0.3099	0.0101	-0.1081	0.1676	-0.256	0	0.336	0.0789	0.0131	0.1256	0.0424	0.2503	0.9178	24.9844	67.7692
3	0.3041	0.1323	0.4293	0.534	0.6327	0.6575	-0.1955	-0.8211	0.3039	0.2152	0.8452	-0.3522	0.4164	0.5467	0.0171	0.3769	0.0964	0.0443	0.2743	0.0193	0.2246	-1.8312	15.9866	73.1886
4	-0.0085	0.4389	0.23	0.3975	-0.4851	0.521	0.1596	-0.1852	-0.0894	0.2995	-0.0385	-0.2863	0.4594	0.1073	0.0002	0.309	0.0361	-0.0352	0.2884	-0.0006	0.2299	1.7429	6.1421	75.6988
5	0.0051	-0.0535	-0.0199	0.0353	0.0133	0.1017	-0.2225	-0.3736	-0.0906	-0.1367	0.1787	0.0051	0.2301	-0.3797	0	0.3317	-0.0841	-0.066	0.1765	0.1742	0.3366	-16.4485	2.9238	65.1252
6	0.6298	0.781	0.0447	0.6487	0.2193	0.0575	-0.3695	0.6937	0.8911	0.026	0.4682	0.2838	0.4454	-0.0037	0.0136	0.3797	-0.0151	-0.2069	0.4389	0.1209	0.3403	-14.892	1	53.3138
7	1.0767	1.024	-0.4837	0.9318	0.6378	0.5817	-0.2037	-0.1937	0.3055	0.1053	0.2881	0.5584	0.3796	0.1802	-0.0024	0.2765	-0.094	-0.1047	0.253	0.0323	0.3569	-20.5905	-6.8597	60.61
8	1.107	1.3969	0.1327	1.6225	0.9461	0.9742	-0.043	0.188	-0.0882	-0.0091	0.1342	-0.0804	0.0042	0.0921	-0	0.2932	0.0008	-0.0572	0.2138	0.0132	0.2319	-5.9778	-1.2452	62.1684
9	0.7918	0.5942	0.1747	0.4396	0.1526	0.2202	-0.0443	-1.6103	0.3092	0.3363	-0.446	0.7371	-0.2546	-0.7811	-0.0207	0.2152	0.0475	0.0547	0.2078	0.1231	0.2938	-13.564	17.6848	72.8581
10	2.4041	1.011	-0.7709	3.414	1.2071	1.8843	-0.1449	0.3764	0.0644	-0.6236	0.2481	-0.1744	-0.202	0.001	0.0827	0.2291	0.033	0.0206	0.1031	0.1043	0.0824	2.3489	22.3462	58.2888
11	1.9981	0.0495	0.1649	5.4689	2.5606	1.8199	-0.3013	0.7825	0.1449	-1.4664	1.275	-0.8448	-1.1055	-0.3371	0.462	0.46	0.0699	-0.258	0.2434	0.3268	0.0966	-0.0496	31.8337	13.9511
12	1.6091	-1.3915	0.5979	0.6952	-0.4278	0.3008	0.2542	0.2012	0.0082	0.0348	-0.1178	0.0895	-0.1762	-0.2659	0	0.3634	-0.0461	-0.0765	0.2951	0.0483	0.2058	0.9756	16.7853	14.9171
13	0.242	-0.0491	0.0143	0.2307	0.0843	0	-0.5608	0.9456	-0.3696	-1.4223	0.7981	0.6277	0.7888	-0.7003	0.0002	0.5799	0.0077	-0.3051	0.617	0.0869	0.5939	0.3213	3.6939	6.9013
14	0.3058	-0.329	-0.5	0.296	0.2889	0.5021	0.3907	0.495	0.6706	-0.1672	-0.4848	0.2213	-0.0125	-0.048	0.0002	0.283	0.0326	-0.0887	0.4762	0.092	0.4512	22.0067	0.7576	18.8267
15	0.1647	-0.2496	0.0021	0.5365	-0.1412	0.4022	0.3806	-0.541	-0.1464	-0.0538	-0.0217	-0.003	0.1211	0.0443	0.0001	0.3744	-0.0371	-0.1253	0.0918	0.0196	0.3254	18.9584	-6.1127	31.6591
16	1.7176	0.1318	0.4395	0.6882	0.5084	0.9179	0.4325	0.9229	-0.333	0.0894	-0.5039	-0.3279	0.3745	0.4947	-0.0279	0.3054	0.0528	-0.057	0.3117	-0.0201	0.3375	23.9981	-12.1731	21.9556
17	0.0946	-0.2438	0.3991	1.3363	-0.1879	0.2456	0.4156	-0.1721	-0.0345	-0.9739	-1.1312	0.3609	0.2593	-0.2693	-0.1761	0.3956	-0.1216	-0.1252	0.347	-0.066	0.2685	10.0479	-9.7881	17.2313
18	1.2433	-1.2837	1.1586	1.0404	-0.47	0.5394	-0.0291	0.3749	-0.4158	-0.095	0.032	-0.1679	0.0056	-0.0601	0.0002	0.2971	-0.013	-0.1104	0.3467	0.0374	0.3107	8.0099	2.9901	17.3326
19	1.1625	-0.5529	0.5303	1.9823	0.6231	0.3996	-0.0989	0.0268	-0.0452	0.214	-0.1378	-0.1812	-0.2782	-0.3028	0.0001	0.2733	-0.0897	-0.1067	0.2213	0.0363	0.2773	10.0741	13.1219	25.1928
20	1.0465	-0.3715	0.0047	0.9972	-0.0844	1.001	0.0997	-0.0272	0.0066	0.4168	0.153	0.1512	-0.6649	-1.0322	0.0119	0.3393	0.0495	-0.0534	0.5907	-0.0119	0.2322	-4.6742	24.5944	25.709
21	0.5161	-0.2788	0.9948	0.1274	-0.4651	2.0854	-0.2635	-0.6634	-1.2382	-0.0809	0.5378	-0.2388	2.1163	-1.0101	0.0538	0.541	0.9535	-0.6311	0.9567	-1.1243	0.9934	37.3816	9.6614	66.4677
22	0.989	0.7132	1.481	1.2495	0.7851	2.3284	-3.3172	-0.8643	1.8514	-1.596	0.5034	-0.9979	-0.4295	2.6101	-0.189	0.3239	0.8952	-0.3387	0.7487	-0.7164	1.0318	43.2869	2.2653	64.4306
23	-0.0146	0.0102	0.0224	0.0038	0.0458	0.0153	-0.4083	-0.6999	-0.213	-0.0701	0.4603	-0.2448	-0.4565	0.3297	0	1.1028	0.8431	-0.6008	0.9715	-0.6426	0.7086	51.1534	-0.0888	66.3872
24	0.0847	0.0045	-0.0729	0.1771	-0.1045	0.093	-1.0129	-1.5178	1.127	0.3933	-1.123	0.3457	-0.0041	0.9123	-0	0.4087	0.2102	-0.3225	0.7028	-0.0724	0.6967	51.9058	-2.4722	51.5176
25	1.1332	-0.694	1.3473	1.4234	0.1573	1.5496	-0.3902	0.1249	0.7499	0.2872	-0.0593	0.1831	-0.0458	0.228	-0.2917	0.2286	0.0102	-0.2155	0.2604	-0.0259	0.533	34.8349	-1.8477	38.8641
26	1.7094	-0.8164	1.0131	0.537	-0.0436	2.0401	0.0384	0.9588	0.187	0.1249	0.0732	-0.167	0.7566	0.7171	-0.3116	0.3274	0.083	-0.1299	0.5077	0.1324	0.3878	41.0705	-8.4313	31.6394
27	0.9959	-0.3063	-2.0713	0.7131	1.4201	5.4988	-1.5367	0.0853	0.1408	0.0174	-0.244	-0.8705	0.7766	0.9401	-0.2219	0.1784	-0.3553	-0.5452	1.0459	0.3864	1.2427	52.1216	0.7798	37.3516
28	1.4714	-0.5	-0.3373	0.7331	0.6828	2.1345	-1.195	-0.7717	1.2546	0.8013	0.6649	-0.5346	0.2332	0.3935	-0.2388	0.6423	0.3076	-0.5065	0.5004	-0.2369	0.9412	44.154	0.0022	51.5811
29	1.3893	-0.0063	0.4025	0.3009	0.5081	0.7322	-1.0118	-0.9296	1.4639	0.2218	0.2599	0.3439	0.3217	-0.4898	-0.0276	0.6164	0.2235	-0.4738	0.4494	-0.3578	1.0862	32.8542	3.1991	54.2463
30	0.0575	-0.1588	0.0782	0.1467	0.0202	0.0116	-0.5124	0.3534	0.8124	0.2687	-0.5112	-0.6426	0.2881	-0.7927	-0	0.8703	0.4583	-0.7617	0.6961	-0.3743	1.6948	26.5762	11.5082	56.2402
31	0.1775	0.1065	0.1673	0.0435	-0.0362	0.3112	-0.6771	-0.0892	-0.0448	-0.2448	0.8502	-0.5768	0.5881	-1.1714	0	1.0566	-0.3588	0.259	1.3634	-0.003	0.678	-23.2696	12.9492	13.9961
32	0.4638	0.0575	0.3321	0.0137	0.0596	0.5099	-0.9893	-0.618	0.9824	-0.9228	-1.1793	0.1771	0.3873	-0.4127	-0.0112	0.1984	-0.0057	0.1197	1.4214	0.5465	0.9822	-38.2441	13.3782	11.482
33	0.0877	0.3806	-0.0986	0.377	-0.1979	0.0462	-0.5465	0.0759	0.7201	-0.3193	0.3781	0.3367	0.6325	-0.7544	0	0.7114	0.0803	-0.1432	1.6227	0.0065	0.543	-41.4366	4.4876	14.5562
34	0.8089	-0.7943	0.451	0.3889	-0.1558	0.2059	-0.4885	-0.0161	-0.6606	-0.0231	0.7938	0.6938	-0.0829	-0.1081	-0.1108	0.1205	-0.3334	-0.2179	1.4649	0.4388	0.44	-29.2474	-4.347	36.7806
35	2.7855	-1.5996	-1.7496	1.3536	1.1823	1.2844	0.7103	-0.8834	1.1219	-0.4145	0.2648	-0.3699	-0.556	-0.4073	0.3214	0.2268	-0.3537	-0.5118	1.3737	0.6421	0.6951	-33.3323	7.3845	42.0914
36	2.381	1.0334	0.8473	0.4332	0.2298	1.5876	-0.5671	1.1434	1.0494	-0.0711	0.265	0.6388	0.2642	-0.1302	-0.4717	0.3136	-0.2309	-0.2184	0.8289	0.3028	0.7473	-35.1159	-3.5618	48.6526
37	0.0519	0.0608	-0.0687	0.004	-0.0579	0.0086	-0.0321	0.4519	-0.4248	0.0385	-0.2895	0.053	0.2578	-0.0403	0	0.3966	-0.3815	-0.5121	2.0258	1.297	1.5267	-45.7959	-0.1222	38.3821
38	0.2756	-1.0703	0.1345	1.1206	-1.037	1.2599	0.3101	0.3317	0.7352	0.0473	-0.2616	-0.0894	0.1348	-0.4466	-0.0001	0.4994	-0.1628	-0.1329	1.1654	0.1595	0.5679	-35.1094	7.1513	28.8887
39	0.1387	0.4458	-0.4962	0.1455	-0.3702	0.5172	0.4654	-0.3168	0.5886	-0.0698	0.3304	0.2443	-0.4056	0.4063	-0	0.4077	-0.1814	0.0041	1.3001	-0.199	0.8183	-25.8613	13.1548	26.0773
40	0.0149	0.0824	0.1308	0.0069	0.0653	0.0745	-0.3234	-0.5891	0.1796	0.7809	-0.4246	-0.4207	-1.2871	0.8758	0	0.9407	-0.1982	-0.0093	1.0246	0.1916	0.6503	-26.7058	22.3573	22.0521

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	(CHAIN A AND RESID 205:228)
2	X-RAY DIFFRACTION	2	(CHAIN A AND RESID 229:262)
3	X-RAY DIFFRACTION	3	(CHAIN A AND RESID 263:274)
4	X-RAY DIFFRACTION	4	(CHAIN A AND RESID 275:297)
5	X-RAY DIFFRACTION	5	(CHAIN A AND RESID 298:317)
6	X-RAY DIFFRACTION	6	(CHAIN A AND RESID 318:344)
7	X-RAY DIFFRACTION	7	(CHAIN A AND RESID 345:390)
8	X-RAY DIFFRACTION	8	(CHAIN A AND RESID 391:458)
9	X-RAY DIFFRACTION	9	(CHAIN A AND RESID 459:468)
10	X-RAY DIFFRACTION	10	(CHAIN A AND RESID 469:588)
11	X-RAY DIFFRACTION	11	(CHAIN B AND RESID 205:231)
12	X-RAY DIFFRACTION	12	(CHAIN B AND RESID 232:278)
13	X-RAY DIFFRACTION	13	(CHAIN B AND RESID 279:293)
14	X-RAY DIFFRACTION	14	(CHAIN B AND RESID 294:329)
15	X-RAY DIFFRACTION	15	(CHAIN B AND RESID 330:352)
16	X-RAY DIFFRACTION	16	(CHAIN B AND RESID 353:404)
17	X-RAY DIFFRACTION	17	(CHAIN B AND RESID 405:423)
18	X-RAY DIFFRACTION	18	(CHAIN B AND RESID 424:461)
19	X-RAY DIFFRACTION	19	(CHAIN B AND RESID 462:525)
20	X-RAY DIFFRACTION	20	(CHAIN B AND RESID 526:587)
21	X-RAY DIFFRACTION	21	(CHAIN C AND RESID 238:257)
22	X-RAY DIFFRACTION	22	(CHAIN C AND RESID 258:277)
23	X-RAY DIFFRACTION	23	(CHAIN C AND RESID 278:287)
24	X-RAY DIFFRACTION	24	(CHAIN C AND RESID 288:298)
25	X-RAY DIFFRACTION	25	(CHAIN C AND RESID 299:347)
26	X-RAY DIFFRACTION	26	(CHAIN C AND RESID 348:403)
27	X-RAY DIFFRACTION	27	(CHAIN C AND RESID 404:416)
28	X-RAY DIFFRACTION	28	(CHAIN C AND RESID 417:459)
29	X-RAY DIFFRACTION	29	(CHAIN C AND RESID 460:503)
30	X-RAY DIFFRACTION	30	(CHAIN C AND RESID 504:532)
31	X-RAY DIFFRACTION	31	(CHAIN D AND RESID 228:248)
32	X-RAY DIFFRACTION	32	(CHAIN D AND RESID 249:258)
33	X-RAY DIFFRACTION	33	(CHAIN D AND RESID 259:288)
34	X-RAY DIFFRACTION	34	(CHAIN D AND RESID 289:328)
35	X-RAY DIFFRACTION	35	(CHAIN D AND RESID 329:338)
36	X-RAY DIFFRACTION	36	(CHAIN D AND RESID 339:408)
37	X-RAY DIFFRACTION	37	(CHAIN D AND RESID 409:418)
38	X-RAY DIFFRACTION	38	(CHAIN D AND RESID 419:488)
39	X-RAY DIFFRACTION	39	(CHAIN D AND RESID 489:519)
40	X-RAY DIFFRACTION	40	(CHAIN D AND RESID 520:545)

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