PDB-2y1r: Structure of MecA121 & ClpC N-domain complex

ID or keywords:

Entry

Database: PDB / ID: 2y1r

Title

Structure of MecA121 & ClpC N-domain complex

Components

ADAPTER PROTEIN MECA 1
NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

Keywords

TRANSCRIPTION / PROTEOLYSIS

Function / homology

Function and homology information

negative regulation of establishment of competence for transformation / negative regulation of sporulation resulting in formation of a cellular spore / establishment of competence for transformation / sporulation resulting in formation of a cellular spore / protein-macromolecule adaptor activity / cellular response to heat / ATP hydrolysis activity / ATP binding / cytoplasm
Similarity search - Function

Biological species

BACILLUS SUBTILIS (bacteria)

Method

X-RAY DIFFRACTION /

MOLECULAR REPLACEMENT / Resolution: 2.595 Å

Authors

Wang, F. / Mei, Z.Q. / Wang, J.W. / Shi, Y.G.

Citation

Journal: Nature / Year: 2011
Title: Structure and Mechanism of the Hexameric Meca-Clpc Molecular Machine.
Authors: Wang, F. / Mei, Z. / Qi, Y. / Yan, C. / Hu, Q. / Wang, J. / Shi, Y.

History

Deposition	Dec 10, 2010	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Mar 16, 2011	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Jun 28, 2017	Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type
Revision 1.4	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_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_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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PDBx/mmCIF format	2y1r.cif.gz	706.9 KB	Display	PDBx/mmCIF format
PDB format	pdb2y1r.ent.gz	587.1 KB	Display	PDB format
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Validation report

Summary document	2y1r_validation.pdf.gz	597.7 KB	Display	wwPDB validaton report
Full document	2y1r_full_validation.pdf.gz	697.7 KB	Display
Data in XML	2y1r_validation.xml.gz	75.1 KB	Display
Data in CIF	2y1r_validation.cif.gz	97.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/y1/2y1r ftp://data.pdbj.org/pub/pdb/validation_reports/y1/2y1r	HTTPS FTP

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Related structure data

Related structure data	2y1qSC 3pxgC 3pxiC 3jtpS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6bti-1 7cdb-2 2fal-d 4bob-d 4c79-2 3k2p-2 3k2p-1 5ivu-1 1jfv-d 3i86-2 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) 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

Related structure data

2y1qSC

3pxgC

3pxiC

3jtpS

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#80 - Aug 2006 AAA+ Proteases similarity (4) #176 - Aug 2014 Dynein similarity (4) #150 - Jun 2012 Sliding Clamps similarity (1)

Deposited unit

A: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

B: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

C: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

D: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

E: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

F: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

G: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

H: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

I: ADAPTER PROTEIN MECA 1

J: ADAPTER PROTEIN MECA 1

K: ADAPTER PROTEIN MECA 1

L: ADAPTER PROTEIN MECA 1

M: ADAPTER PROTEIN MECA 1

N: ADAPTER PROTEIN MECA 1

O: ADAPTER PROTEIN MECA 1

P: ADAPTER PROTEIN MECA 1

hetero molecules

225 kDa, 16 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

7

G: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

8

H: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB

hetero molecules

defined by author&software
16.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

9

I: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

10

J: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

11

K: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

12

L: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers

13

M: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

14

N: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

15

O: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

16

P: ADAPTER PROTEIN MECA 1

defined by author&software
11.5 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	110.020, 124.720, 149.830
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details
1	1	1	CHAIN A AND (RESSEQ 3:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
2	1	1	CHAIN B AND (RESSEQ 4:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
3	1	1	CHAIN C AND (RESSEQ 4:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
4	1	1	CHAIN D AND (RESSEQ 3:143 OR RESSEQ 500:500 OR RESSEQ 600:600 )
5	1	1	CHAIN E AND (RESSEQ 4:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
6	1	1	CHAIN F AND (RESSEQ 3:68 OR RESSEQ 76:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
7	1	1	CHAIN G AND (RESSEQ 4:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
8	1	1	CHAIN H AND (RESSEQ 4:73 OR RESSEQ 74:142 OR RESSEQ 500:500 OR RESSEQ 600:600 )
1	1	2	CHAIN I AND (RESSEQ 125:218 )
2	1	2	CHAIN J AND (RESSEQ 124:218 )
3	1	2	CHAIN K AND (RESSEQ 126:217 )
4	1	2	CHAIN L AND (RESSEQ 126:218 )
5	1	2	CHAIN M AND (RESSEQ 126:146 OR RESSEQ 149:217 )
6	1	2	CHAIN N AND (RESSEQ 125:145 OR RESSEQ 150:217 )
7	1	2	CHAIN O AND (RESSEQ 127:147 OR RESSEQ 150:217 )
8	1	2	CHAIN P AND (RESSEQ 125:218 )

NCS ensembles :

ID
1
2

#1: Protein	NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB / CLPC Mass: 16229.666 Da / Num. of mol.: 8 / Fragment: N-DOMAIN, RESIDUES 1-149 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS SUBTILIS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P37571
#2: Protein	ADAPTER PROTEIN MECA 1 / MECA121 Mass: 11533.901 Da / Num. of mol.: 8 / Fragment: RESIDUES 121-218 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS SUBTILIS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P37958
#3: Chemical	ChemComp-SRT / S,R MESO-TARTARIC ACID Mass: 150.087 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C₄H₆O₆
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 120 / 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: 2.31 Å³/Da / Density % sol: 46.85 % / Description: NONE
Crystal grow	Details: 20%(W/V) POLYETHYLENE GLYCOL 3350, 300MM AMMONIUM TARTRATE AND 6MM N-NONYL-BETA-D-MALTOPYRANOSIDE

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418
Detector	Type: RIGAKU HTC / Detector: IMAGE PLATE / Date: Jul 27, 2009 / Details: MIRRORS
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.5418 Å / Relative weight: 1
Reflection	Resolution: 2.59→50 Å / Num. obs: 60699 / % possible obs: 94.1 % / Observed criterion σ(I): 2 / Redundancy: 3.5 % / B_iso Wilson estimate: 56.4 Å² / R_merge(I) obs: 0.1 / Net I/σ(I): 9.17
Reflection shell	Resolution: 2.59→2.75 Å / Redundancy: 2.79 % / R_merge(I) obs: 0.57 / Mean I/σ(I) obs: 1.91 / % possible all: 79.6

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Processing

Software

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

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3JTP, 2Y1Q

3jtp

2y1q

Resolution: 2.595→47.928 Å / SU ML: 0.33 / σ(F): 1.34 / Phase error: 30.8 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2582	2914	4.8 %
R_work	0.2134	-	-
obs	0.2157	60613	94.1 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 25.441 Å² / k_sol: 0.354 e/Å³

Displacement parameters

B_iso mean: 57.12 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-10.0285 Å²	0 Å²	0 Å²
2-	-	1.4364 Å²	0 Å²
3-	-	-	-11.8393 Å²

Refinement step

Cycle: LAST / Resolution: 2.595→47.928 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13833	0	160	120	14113

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.051	15959
X-RAY DIFFRACTION	f_angle_d	1.48	21061
X-RAY DIFFRACTION	f_dihedral_angle_d	18.212	5525
X-RAY DIFFRACTION	f_chiral_restr	0.072	2318
X-RAY DIFFRACTION	f_plane_restr	0.004	2565

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type	Rms dev position (Å)
1	1	A	1085	X-RAY DIFFRACTION	POSITIONAL
1	2	B	1085	X-RAY DIFFRACTION	POSITIONAL	0.062
1	3	C	1085	X-RAY DIFFRACTION	POSITIONAL	0.055
1	4	D	1090	X-RAY DIFFRACTION	POSITIONAL	0.059
1	5	E	1085	X-RAY DIFFRACTION	POSITIONAL	0.045
1	6	F	1039	X-RAY DIFFRACTION	POSITIONAL	0.063
1	7	G	1085	X-RAY DIFFRACTION	POSITIONAL	0.055
1	8	H	1085	X-RAY DIFFRACTION	POSITIONAL	0.059
2	1	I	767	X-RAY DIFFRACTION	POSITIONAL
2	2	J	767	X-RAY DIFFRACTION	POSITIONAL	0.055
2	3	K	752	X-RAY DIFFRACTION	POSITIONAL	0.055
2	4	L	758	X-RAY DIFFRACTION	POSITIONAL	0.061
2	5	M	737	X-RAY DIFFRACTION	POSITIONAL	0.05
2	6	N	728	X-RAY DIFFRACTION	POSITIONAL	0.058
2	7	O	734	X-RAY DIFFRACTION	POSITIONAL	0.056
2	8	P	767	X-RAY DIFFRACTION	POSITIONAL	0.055

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 (%)
2.5947-2.6373	0	0	0.3291	1898	X-RAY DIFFRACTION	63
2.6373-2.6827	0	0	0.2995	2570	X-RAY DIFFRACTION	84
2.6827-2.7315	0	0	0.2839	2658	X-RAY DIFFRACTION	88
2.7315-2.784	0.3292	567	0.2898	2151	X-RAY DIFFRACTION	90
2.784-2.8409	0	0	0.2787	2770	X-RAY DIFFRACTION	91
2.8409-2.9026	0	0	0.2776	2862	X-RAY DIFFRACTION	93
2.9026-2.9701	0	0	0.2617	2853	X-RAY DIFFRACTION	94
2.9701-3.0444	0.3221	524	0.2676	2371	X-RAY DIFFRACTION	96
3.0444-3.1267	0	0	0.2601	2928	X-RAY DIFFRACTION	96
3.1267-3.2187	0	0	0.2314	2915	X-RAY DIFFRACTION	97
3.2187-3.3226	0.3104	218	0.2274	2766	X-RAY DIFFRACTION	97
3.3226-3.4413	0.2794	278	0.2293	2671	X-RAY DIFFRACTION	97
3.4413-3.579	0	0	0.2145	2943	X-RAY DIFFRACTION	96
3.579-3.7418	0	0	0.2023	2991	X-RAY DIFFRACTION	98
3.7418-3.939	0.2527	446	0.1808	2563	X-RAY DIFFRACTION	97
3.939-4.1857	0	0	0.1631	3033	X-RAY DIFFRACTION	99
4.1857-4.5087	0.1982	378	0.154	2695	X-RAY DIFFRACTION	99
4.5087-4.962	0	0	0.1533	3079	X-RAY DIFFRACTION	99
4.962-5.679	0	0	0.1883	3099	X-RAY DIFFRACTION	100
5.679-7.1511	0.2465	314	0.1955	2835	X-RAY DIFFRACTION	100
7.1511-47.9362	0.1859	189	0.1749	3048	X-RAY DIFFRACTION	98

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	1.4516	-0.5597	0.1586	0.6668	-0.2492	1.3412	-0.2406	-0.0503	0.1098	0.184	-0.0365	-0.1055	-0.1403	-0.0035	0.1178	0.09	0.0114	-0.0287	0.0728	-0.0181	0.0653	-27.7279	9.2212	33.9541
2	0.395	-0.0368	-0.2334	0.2279	-0.259	1.2124	-0.1691	-0.0433	-0.218	-0.0243	-0.1195	-0.0987	0.1691	0.3079	0.0723	0.0217	-0.037	0.0447	0.1235	-0.0097	0.1173	-27.1724	-13.4354	2.1408
3	0.6787	-0.312	-0.0995	0.3761	-0.1881	0.7413	-0.1436	0.1158	-0.1233	0.119	0.0564	0.1322	0.0144	-0.4525	0.0494	0.0893	-0.0601	0.1167	0.2066	-0.1139	0.2933	-58.2476	-18.3091	9.0971
4	1.4192	-0.0407	0.1817	0.3708	0.1116	0.5137	-0.4093	-0.4542	-0.1927	-0.1983	0.089	0.1858	0.015	-0.3885	0.0927	0.0124	0.1277	-0.179	0.1817	-0.0999	0.0213	-57.2699	16.5114	24.4915
5	0.8466	-0.0722	-0.2895	0.1071	0.0884	0.4995	-0.1509	-0.1931	-0.3029	-0.0274	-0.1424	0.0807	0.0539	-0.0673	0.1852	0.184	0.0928	0.113	0.2317	-0.055	0.2655	-3.4907	-8.3179	34.3203
6	0.4317	-0.288	-0.5869	1.3718	0.6037	1.0934	-0.2216	0.191	0.1352	0.0906	0.0088	0.5657	0.1154	-0.3827	0.151	0.095	-0.0374	-0.0149	0.3667	0.0007	0.2536	-3.9982	14.5117	3.0399
7	1.4456	-0.3991	-0.0352	0.6083	-0.119	0.1029	-0.2132	0.3217	0.0618	-0.0651	0.1343	-0.0824	-0.0394	0.0297	0.0534	0.1032	-0.0077	-0.0567	0.1508	0.0386	0.1589	26.867	18.1091	8.8907
8	1.1003	-0.301	-0.1893	0.3337	0.1486	0.713	-0.3876	-0.4356	-0.1704	0.1279	0.1029	0.1192	0.2545	0.3581	0.1696	0.1303	0.0956	0.149	0.2025	0.0952	0.339	25.8908	-16.7719	24.6376
9	1.0844	0.3488	0.0179	0.4467	-0.0672	0.0391	-0.0133	-0.5345	0.1779	0.1668	-0.0997	-0.0076	0.1013	-0.1183	0.0578	0.2349	0.0234	0.0504	0.2231	0.0541	0.0557	-43.7808	-6.3946	44.4221
10	0.1614	-0.2695	-0.0294	1.146	0.4955	1.2038	0.1428	0.0231	0.0629	-0.0615	-0.2434	-0.0252	-0.2249	-0.4586	0.0635	0.1937	0.0062	-0.025	0.1485	0.015	0.06	-41.0136	2.9775	-9.8271
11	0.4453	0.3576	-0.2727	0.3313	-0.175	0.7879	-0.082	-0.088	-0.3552	0.0937	-0.1	-0.2288	0.4702	-0.1366	0.278	0.3239	-0.0397	0.1294	0.0819	0.0692	0.2269	-43.9304	-27.3225	27.373
12	1.4912	-0.5087	0.3452	0.1719	-0.0731	1.0682	0.0526	0.0422	0.5796	-0.1044	-0.0656	-0.186	-0.4624	-0.1948	0.0385	0.3045	0.0345	-0.0338	0.0006	0.0806	0.0596	-40.9198	23.9802	7.3526
13	0.8632	0.1	-0.2594	0.3261	0.12	0.46	0.1136	-0.4684	-0.0969	0.1657	-0.0183	-0.1291	-0.2711	0.7495	-0.1048	0.3021	0.0444	-0.0025	0.4052	-0.0222	0.129	13.4132	6.824	44.4861
14	0.537	0.0952	0.0794	0.3934	0.0912	0.0157	-0.0091	0.5317	0.0219	-0.1188	0.0707	0.1285	-0.0868	0.1845	-0.0369	0.1948	-0.0814	-0.0049	0.28	-0.1245	0.0614	9.3412	-2.8524	-9.4871
15	0.6499	-0.0186	-0.451	0.0992	0.2567	0.9229	0.181	-0.286	0.2498	0.2809	-0.1531	0.1655	-0.2024	0.0135	-0.0264	0.3983	0.0385	-0.0172	0.124	-0.0838	0.1651	13.1807	27.3141	27.4239
16	1.564	-0.0554	-0.3652	-0.025	0.0366	0.5215	-0.083	-0.2124	-0.8978	0.0519	-0.1596	0.2341	0.1177	0.2582	0.1577	0.2051	0.0362	0.1451	-0.2402	-0.3122	0.4774	9.1618	-23.9481	7.7566

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN A
2	X-RAY DIFFRACTION	2	CHAIN B
3	X-RAY DIFFRACTION	3	CHAIN C
4	X-RAY DIFFRACTION	4	CHAIN D
5	X-RAY DIFFRACTION	5	CHAIN E
6	X-RAY DIFFRACTION	6	CHAIN F
7	X-RAY DIFFRACTION	7	CHAIN G
8	X-RAY DIFFRACTION	8	CHAIN H
9	X-RAY DIFFRACTION	9	CHAIN I
10	X-RAY DIFFRACTION	10	CHAIN J
11	X-RAY DIFFRACTION	11	CHAIN K
12	X-RAY DIFFRACTION	12	CHAIN L
13	X-RAY DIFFRACTION	13	CHAIN M
14	X-RAY DIFFRACTION	14	CHAIN N
15	X-RAY DIFFRACTION	15	CHAIN O
16	X-RAY DIFFRACTION	16	CHAIN P

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