PDB-2j9l: Cytoplasmic Domain of the Human Chloride Transporter ClC-5 in com...

ID or keywords:

Entry

Database: PDB / ID: 2j9l

Title

Cytoplasmic Domain of the Human Chloride Transporter ClC-5 in complex with ATP

Components

CHLORIDE CHANNEL PROTEIN 5

Keywords

ION CHANNEL / CHLORIDE CHANNEL / ION TRANSPORT / VOLTAGE-GATED CHANNEL

Function / homology

Function and homology information

renal system process / voltage-gated chloride channel activity / chloride transport / antiporter activity / Stimuli-sensing channels / endocytosis / apical part of cell / synaptic vesicle / monoatomic ion transmembrane transport / early endosome ...
Similarity search - Function

Biological species

HOMO SAPIENS (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MAD / Resolution: 2.3 Å

Authors

Meyer, S. / Savaresi, S. / Forster, I.C. / Dutzler, R.

Citation

Journal: Nat.Struct.Mol.Biol. / Year: 2006
Title: Nucleotide Recognition by the Cytoplasmic Domain of the Human Chloride Transporter Clc-5
Authors: Meyer, S. / Savaresi, S. / Forster, I.C. / Dutzler, R.

History

Deposition	Nov 13, 2006	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 4, 2007	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	May 8, 2024	Group: 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

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	2j9l_validation.pdf.gz	2.2 MB	Display	wwPDB validaton report
Full document	2j9l_full_validation.pdf.gz	2.3 MB	Display
Data in XML	2j9l_validation.xml.gz	43.8 KB	Display
Data in CIF	2j9l_validation.cif.gz	58.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/j9/2j9l ftp://data.pdbj.org/pub/pdb/validation_reports/j9/2j9l	HTTPS FTP

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Related structure data

Related structure data	2ja3C C: citing same article (ref.)
Similar structure data	2ja3-d 3p4g-d 3gds-1 3by6-d 6hww-d 4rqy-2 4k3d-d 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
Related items in Molecule of the Month	#140 - Aug 2011 Rhomboid Protease GlpG similarity (4)

Deposited unit

A: CHLORIDE CHANNEL PROTEIN 5

B: CHLORIDE CHANNEL PROTEIN 5

C: CHLORIDE CHANNEL PROTEIN 5

D: CHLORIDE CHANNEL PROTEIN 5

E: CHLORIDE CHANNEL PROTEIN 5

F: CHLORIDE CHANNEL PROTEIN 5

hetero molecules

130 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	122.328, 148.101, 79.883
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	18
Space group name H-M	P2₁2₁2

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	C
3	1	B
4	1	D
1	2	C
2	2	A
1	3	E
2	3	A

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	ARG	ARG	ALA	ALA	6	A	A	589 - 647	20 - 78
2	1	1	ARG	ARG	ALA	ALA	6	C	C	589 - 647	20 - 78
3	1	1	ARG	ARG	ALA	ALA	6	B	B	589 - 647	20 - 78
4	1	1	ARG	ARG	ALA	ALA	6	D	D	589 - 647	20 - 78
1	2	1	LEU	LEU	LEU	LEU	6	A	A	677 - 729	108 - 160
2	2	1	LEU	LEU	LEU	LEU	6	C	C	677 - 729	108 - 160
3	2	1	LEU	LEU	LEU	LEU	6	B	B	677 - 729	108 - 160
4	2	1	LEU	LEU	LEU	LEU	6	D	D	677 - 729	108 - 160
1	1	2	ARG	ARG	VAL	VAL	1	C	C	648 - 654	79 - 85
2	1	2	ARG	ARG	VAL	VAL	1	A	A	648 - 654	79 - 85
1	1	3	ARG	ARG	VAL	VAL	1	E	E	648 - 654	79 - 85
2	1	3	ARG	ARG	VAL	VAL	1	A	A	648 - 654	79 - 85

NCS ensembles :

ID
1
2
3

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.5686, -0.1561, 0.8077), (-0.165, -0.9402, -0.2979), (0.8059, -0.3027, 0.5089)	9.622, 134.3, 21.07
2	given	(0.6588, -0.5556, -0.5074), (0.2652, -0.4596, 0.8476), (-0.7041, -0.6929, -0.1554)	74.54, 22.24, 131.7
3	given	(-0.5402, -0.1832, 0.8214), (-0.1729, -0.9311, -0.3213), (0.8236, -0.3156, 0.4712)	10.31, 134.8, 23.08
4	given	(-0.7176, 0.5633, 0.4097), (0.5523, 0.1019, 0.8274), (0.4243, 0.82, -0.3842)	-1.612, -16.59, 23.81
5	given	(-0.751, 0.6049, 0.2646), (0.5141, 0.2843, 0.8093), (0.4143, 0.7438, -0.5245)	6.257, -23.71, 37.32

Details

AUTHOR COMMENTS: THE PREDOMINANT OLIGOMERIC STATE OF THE CLC-5CYTOPLASMIC DOMAIN IN SOLUTION IS A DIMER. CURRENTLY THERE IS NOEXPERIMENTAL EVIDENCE FOR THE CORRECT DIMER ARRANGEMENT. APUTATIVE ARRANGEMENT IS THE PAIR OF CHAINS AB, CD AND EFRELATED BY TWO-FOLD SYMMETRY IN THE ASYMMETRIC UNIT.

#1: Protein	CHLORIDE CHANNEL PROTEIN 5 / CHLORIDE TRANSPORTER CLC-5 / CLC-5 Mass: 21076.469 Da / Num. of mol.: 6 / Fragment: CYTOPLASMIC DOMAIN, RESIDUES 571-746 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: EPITHELIUM / Organ: KIDNEY / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P51795
#2: Chemical	ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE Mass: 507.181 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₃P₃ / Comment: ATP, energy-carrying molecule*YM
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Cl
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 267 / 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: 2.8 Å³/Da / Density % sol: 56.2 %
Crystal grow	Details: 200 MM (NH4)2SO4, 10 MM TRIS HCL (PH 7.4), 18% PEG 4000

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9195
Detector	Type: MARRESEARCH / Detector: CCD / Details: MIRROR
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9195 Å / Relative weight: 1
Reflection	Resolution: 2.3→20 Å / Num. obs: 60291 / % possible obs: 95.3 % / Observed criterion σ(I): 2.2 / Redundancy: 5.2 % / B_iso Wilson estimate: 59.6 Å² / R_merge(I) obs: 0.07 / Net I/σ(I): 18.1
Reflection shell	Resolution: 2.3→2.38 Å / Redundancy: 1.8 % / R_merge(I) obs: 0.36 / Mean I/σ(I) obs: 2.23 / % possible all: 68.5

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
DENZO		data reduction
TRUNCATE		data scaling
SHELX		phasing

Refinement

Method to determine structure:

MAD / Resolution: 2.3→20 Å / Cor.coef. F_o:F_c: 0.92 / Cor.coef. F_o:F_c free: 0.897 / SU B: 15.572 / SU ML: 0.209 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 2.23 / ESU R: 0.351 / ESU R Free: 0.261
Stereochemistry target values: MAXIMUM LIKELIHOOD, RESTRAINED
Details: HYDROGENS HAVE BEEN ADDED IN THE THE PREDOMINANT OLIGOMERIC STATE OF THE CLC-5 CYTOPLASMIC DOMAIN IN SOLUTION IS A DIMER. CURRENTLY THERE IS NO EXPERIMENTAL EVIDENCE FOR THE CORRECT DIMER ...

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.295	3191	5.07 %	RANDOM
R_work	0.263	-	-	-
obs	0.264	63482	97.5 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK

Displacement parameters

B_iso mean: 36.27 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.368 Å²	0 Å²	0 Å²
2-	-	-0.037 Å²	0 Å²
3-	-	-	-0.331 Å²

Refinement step

Cycle: LAST / Resolution: 2.3→20 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8003	0	196	267	8466

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.005	0.022	8333
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	0.887	2.025	11356
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.205	5	997
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	23.331	23.467	323
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.501	15	1509
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	15.4	15	66
X-RAY DIFFRACTION	r_chiral_restr	0.052	0.2	1415
X-RAY DIFFRACTION	r_gen_planes_refined	0.002	0.02	5913
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.225	0.3	4108
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.324	0.5	5906
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.218	0.5	636
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.187	0.3	68
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.226	0.5	14
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	0.489	2	5183
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.852	3	8369
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	0.391	2	3435
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	0.7	3	2987
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
2	1	C	57	tight positional	0.4	0.05
2	2	A	57	tight positional	0.4	0.05
3	1	E	57	tight positional	0.1	0.05
3	2	A	57	tight positional	0.1	0.05
1	1	A	890	loose positional	0.52	20
1	2	C	890	loose positional	0.51	20
1	3	B	890	loose positional	0.65	20
1	4	D	890	loose positional	0.51	20
1	1	A	890	loose thermal	2.69	50
1	2	C	890	loose thermal	1.19	50
1	3	B	890	loose thermal	1.69	50
1	4	D	890	loose thermal	1.97	50
2	1	C	57	loose thermal	1.11	50
2	2	A	57	loose thermal	1.11	50
3	1	E	57	loose thermal	6.44	50
3	2	A	57	loose thermal	6.44	50

LS refinement shell

Resolution: 2.3→2.36 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.333	207
R_work	0.293	3738

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	12.9608	1.2794	0.3469	3.3313	4.0667	5.083	-0.0054	-0.225	-0.6932	0.1814	-0.0673	0.3746	0.301	-0.7248	0.0726	0.5535	-0.095	0.1304	0.4177	-0.1059	0.4208	7.8478	59.352	49.5224
2	0.7033	-0.3004	-0.586	0.1283	0.2503	0.4882	0.6591	0.1744	0.4567	0.1717	0.0617	1.9337	0.4192	-1.9459	-0.7209	0.6653	-0.0035	0.0646	0.6679	0.0591	0.7674	2.0157	68.9231	45.6521
3	2.2628	-0.9881	-2.132	2.2402	-0.2792	2.8186	0.2547	0.2831	0.1615	-0.1499	-0.2327	0.5309	-0.5607	-0.5035	-0.0219	0.7244	0.0956	0.1018	0.2761	-0.0393	0.413	13.8383	78.4671	38.4868
4	13.1399	0.3111	1.8417	6.9389	-0.4858	7.4497	-0.0955	-0.9243	0.6792	-0.0205	0.4205	-0.3291	-0.6487	-0.0776	-0.3249	1.0686	0.0789	0.2329	0.2486	-0.1301	0.6338	21.4064	87.5052	44.6572
5	7.4445	0.8281	4.6888	6.646	-2.5452	5.8648	-0.1303	0.3178	1.2267	1.3755	0.0042	-1.4441	-0.685	2.4192	0.1261	0.7771	0.0809	0.145	0.6057	-0.0287	0.7314	20.9732	95.9442	35.0002
6	1.922	0.1618	-1.0371	3.3978	-0.3662	2.0356	0.0609	0.0846	0.2094	-0.4077	0.0907	-0.0183	-0.1715	-0.186	-0.1517	0.5603	-0.0069	0.0896	0.2655	-0.103	0.3749	20.9021	73.4378	38.6824
7	3.1091	-0.5319	1.4472	2.1005	1.041	9.4832	0.0528	-0.1301	0.1354	0.0326	0.0762	0.1178	-0.2255	-0.1668	-0.1291	0.4988	0.0261	0.0548	0.2277	-0.0123	0.3513	14.1617	65.4044	49.2452
8	12.3473	-2.5003	2.6457	11.5285	-9.5905	8.0055	0.2569	-0.4561	-2.3574	0.7167	-0.1571	1.3365	1.4083	-0.0891	-0.0998	0.8498	-0.0242	0.0648	0.8567	0.1027	0.6425	6.3193	57.1456	63.3842
9	0.0403	-0.0941	0.4121	0.2201	-0.9635	4.218	0.177	1.1533	-0.3252	-0.1304	-0.0211	2.205	0.2739	-0.4925	-0.1559	0.9784	-0.0173	0.0132	0.7737	0.0888	0.9113	13.3365	52.495	63.2352
10	8.3722	-3.655	-2.757	2.6149	-1.1161	6.1872	0.2274	0.0662	1.095	0.4542	-0.4431	-0.7383	-0.8656	0.8539	0.2156	0.8077	-0.3035	0.1388	0.3988	-0.0331	0.4928	37.2207	63.8088	36.1335
11	0.0903	-0.307	0.3025	1.0472	-1.0334	1.0205	-0.1692	0.505	0.7597	-0.4798	0.1501	-0.9312	-1.0512	1.445	0.019	0.8026	-0.3046	0.1303	0.6139	-0.0282	0.4881	34.7142	55.151	26.767
12	3.1297	-0.104	-0.2768	3.1769	1.1442	1.9869	0.1132	0.4045	0.0647	-0.4715	-0.2002	0.2123	-0.0266	-0.0961	0.0871	0.6129	-0.0176	0.0131	0.2484	-0.0672	0.3336	20.9027	46.7371	28.6309
13	8.0092	-0.6134	-3.2555	7.6825	0.9878	8.8218	-0.144	-0.1484	-0.418	0.196	-0.2422	0.0518	0.7194	0.3739	0.3863	0.7406	-0.0786	0.0017	0.2226	0.0249	0.3466	20.3696	35.0422	35.3541
14	2.5477	-1.9141	-1.2185	5.1028	2.242	4.529	-0.3161	-0.1278	-1.1814	0.5412	-0.1967	1.3136	1.1233	-0.3505	0.5128	0.7724	-0.1871	-0.0327	0.4579	-0.2719	0.6462	11.2746	35.1587	28.57
15	3.1693	4.1318	0.2667	5.3866	0.3477	0.0224	0.1717	0.5209	-0.6751	-1.1723	-0.1966	0.7389	-0.1352	-1.2936	0.0249	1.0648	-0.1078	-0.3134	1.0423	-0.4996	0.748	3.31	41.6804	24.3709
16	3.0634	0.1198	-0.444	1.9726	0.5034	1.9707	-0.0164	-0.0809	0.069	0.1118	0.075	-0.046	-0.0307	0.1725	-0.0585	0.5215	-0.0298	0.0049	0.235	-0.0654	0.299	27.4693	55.1535	40.3188
17	1.1768	3.0373	3.1329	7.8392	8.0858	8.3401	0.2303	1.3091	-0.0872	0.1779	-0.3988	-0.7154	-1.1212	1.6188	0.1686	0.8869	-0.1972	0.0705	0.713	-0.1194	0.5382	49.2685	59.9337	45.056
18	12.0129	-2.6678	2.1853	6.4712	3.4261	3	-0.3061	-0.5181	0.065	0.1507	-0.1206	0.1998	-0.3391	-0.2424	0.4268	1.1667	-0.1853	0.0034	0.4125	-0.0791	0.4991	43.2781	62.1897	52.1676
19	7.7084	1.3714	-4.5871	9.0272	0.914	3.0705	0.0587	0.6242	0.2182	-0.731	0.0178	0.8687	-0.0308	-0.5844	-0.0765	0.5303	0.0871	0.0003	0.3363	0.05	0.3836	23.2801	76.8433	77.1818
20	1.5163	0.3637	-0.7333	0.5447	0.0731	0.4901	-0.1364	0.5565	1.0185	-0.325	0.0614	1.2309	-0.7832	-1.2447	0.075	0.6508	0.1849	-0.021	0.4991	0.0151	0.6492	25.6503	78.6531	89.6603
21	2.555	0.3598	-0.4697	0.0507	-0.0715	2.196	0.1441	-0.3453	0.1521	0.4219	-0.0935	0.1705	-0.3017	0.0837	-0.0506	0.5348	-0.0287	0.0558	0.2653	0.0066	0.2576	40.4779	72.4899	92.9681
22	7.8769	-4.0568	-1.8538	7.2909	0.9343	8.1437	-0.0876	0.0152	-0.5723	0.1026	-0.4797	0.3383	0.4321	-0.3311	0.5672	0.5161	-0.1007	0.0237	0.4538	0.1073	0.343	41.9188	60.3573	94.5849
23	0.0001	0.0002	0	0.0005	0	0	-0.0423	-0.2348	-0.568	-0.0743	0.2124	-0.5398	0.2917	0.2931	-0.1701	0.5891	-0.0486	-0.0197	0.692	0.1503	0.4231	51.4336	61.7985	103.782
24	3.1614	0.5617	0.7145	0.7094	-0.2025	2.2432	-0.0477	-0.0219	-0.0512	0.0187	0.0173	0.0607	-0.2195	0.1799	0.0305	0.4489	-0.0286	0.0269	0.279	0.0363	0.2563	43.538	70.579	84.7411
25	4.6887	1.8289	0.0897	4.9701	0.1876	4.0847	-0.1798	0.004	0.1277	-0.1084	0.1171	0.0745	-0.0995	-0.2435	0.0626	0.4307	0.0343	-0.013	0.3332	0.0403	0.2684	29.9646	71.3984	80.3827
26	9.4657	-4.2235	6.0739	1.8845	-2.7101	3.8975	0.1615	0.7299	1.2174	-0.0067	0.1199	1.2502	-0.8503	-1.4185	-0.2813	0.7706	-0.0093	-0.0085	0.8053	-0.0009	0.651	12.4455	67.9352	76.1952
27	3.0529	0.404	-1.5772	0.1666	-1.098	7.8047	0.2317	-0.4746	-0.3534	-0.7194	0.036	-1.0363	0.4095	-0.252	-0.2678	1.0258	0.4138	0.2476	1.1093	-0.2691	1.0141	16.8287	66.2362	66.9539
28	10.2139	-2.4974	0.4181	4.6332	-0.619	5.9593	0.0623	0.148	-0.529	0.0887	-0.1074	-0.532	0.3547	0.5556	0.0451	0.4061	0.0312	-0.0251	0.2633	0.0145	0.3679	54.2308	70.8727	68.2251
29	2.4685	0.1661	-0.4126	3.7255	-0.4456	4.4557	-0.0891	0.0366	-0.0521	0.2329	0.2352	-0.5965	-0.0639	0.5782	-0.1462	0.5266	0.0145	-0.0278	0.3284	0.0836	0.4243	49.9575	87.2335	66.8856
30	1.2852	-1.1293	-0.7483	2.8401	-0.2696	1.6607	0.1734	0.2707	0.3047	-0.025	-0.2266	-0.2941	-0.4452	0.0822	0.0533	0.5508	0.0469	0.0075	0.3167	0.1395	0.3787	44.3358	90.0451	63.8651
31	3.7558	0.5089	0.5144	5.8168	-0.4013	2.847	0.0582	0.6869	0.1635	-0.5992	0.0319	0.3627	-0.4788	-0.5916	-0.0902	0.7264	0.2081	0.0157	0.5926	0.199	0.4625	35.4857	94.3975	53.2949
32	4.8307	-0.5263	-1.5441	4.4661	0.4054	0.5063	-0.0202	0.1167	0.146	0.3662	-0.1221	0.6161	-0.336	-0.3737	0.1424	0.8398	0.2378	0.1325	0.4009	0.2379	0.5434	34.3815	101.2251	65.7952
33	0.8081	-1.2874	0.0099	2.1953	-0.3881	0.9602	0.0288	-0.0248	0.0629	0.046	0.209	0.1719	-0.2162	-0.3735	-0.2379	0.5544	0.0885	0.022	0.3352	0.1057	0.4169	37.0859	87.7557	67.7852
34	3.2082	0.648	-0.2719	3.1356	0.162	3.0927	-0.1148	0.16	-0.3046	-0.0916	-0.0204	0.1703	0.1578	-0.2551	0.1352	0.4444	-0.0005	0.0184	0.2621	0.0356	0.3243	43.4899	71.2069	67.9929
35	5.1173	3.0695	-1.4311	5.273	2.9226	4.7033	-0.3811	0.5688	-0.6711	-0.4539	0.1313	-0.5975	0.5702	0.3008	0.2499	0.5824	-0.0201	0.0988	0.3171	-0.0192	0.288	49.8633	68.02	58.5878
36	0.1323	0.9676	0.0299	7.0789	0.2188	0.0068	0.4439	-0.732	-0.4079	0.3264	0.4485	-0.678	0.9932	-0.2101	-0.8925	0.8248	-0.1032	0.1272	0.7791	0.0103	0.8404	52.8103	55.2089	59.5222
37	5.8373	-1.023	-2.1602	4.3622	-5.1692	8.1573	0.0232	-0.4791	0.1303	0.2602	-0.0155	0.2308	-0.5363	0.0607	-0.0078	0.7257	0.01	0.2014	0.6038	-0.0278	0.3182	20.7583	39.995	79.1132
38	0.8531	-0.6698	-0.6636	0.5259	0.5211	0.5163	-0.1156	-1.3622	-0.4234	0.7042	-0.5428	1.3479	0.7157	-1.0603	0.6585	0.9973	-0.1182	0.37	0.8661	0.0716	0.6813	14.4025	29.6999	77.5249
39	0.9897	1.0955	1.4927	2.6914	1.1934	2.3938	-0.1119	-0.0659	-0.2568	-0.277	0.0675	0.8308	0.2972	-0.4416	0.0445	0.8645	-0.0817	-0.0072	0.3447	0.1474	0.5177	18.5145	20.8446	62.4112
40	0.5189	-0.4832	0.2493	7.4826	-1.975	7.1238	0.139	-0.7912	-0.6119	-0.1405	0.3737	0.5742	0.3507	-0.3138	-0.5128	0.753	-0.0308	0.1158	0.4108	0.0543	0.3035	27.564	23.7129	68.3777
41	8.9491	3.0434	-1.1678	7.4528	-0.9923	6.0969	0.2398	0.8738	0.6362	-0.5863	-0.1559	0.0448	-0.0864	0.0191	-0.0838	1.2336	-0.0236	-0.2237	0.3426	0.0595	0.4478	19.4832	24.0491	51.6298
42	0.0002	0.011	-0.0289	0.5212	-1.3649	3.5745	-0.2323	2.4397	-0.7303	-0.7657	-1.1421	-1.2467	-0.2924	1.0886	1.3745	1.0464	-0.0694	-0.0227	0.6414	-0.085	0.7813	21.4009	11.7585	48.228
43	2.1975	-1.0897	-0.0635	4.0523	1.6064	1.1579	-0.024	-0.2169	0.258	-0.3019	0.1762	-0.1891	0.0316	-0.08	-0.1521	0.6756	-0.0725	0.1157	0.3145	0.0524	0.3677	27.0908	30.405	65.6565
44	10.6656	-6.0704	-3.4091	3.6078	2.7545	5.4281	0.7039	-1.6492	0.8618	0.4583	-1.1868	0.7231	-0.1005	-0.2545	0.483	0.8932	-0.3707	-0.1258	0.6593	-0.3328	1.1612	12.2762	50.5277	75.4029
45	6.3209	-8.8653	-2.5666	12.7269	2.5502	4.8017	-0.3279	0.0811	-0.309	-0.3452	0.1282	-0.0358	-0.0796	-0.0612	0.1998	0.5079	-0.1014	0.0032	0.4846	-0.0665	0.5223	19.0161	55.7022	77.2756
46	3.7981	-2.5511	-2.2417	5.2191	2.8122	1.81	-0.1755	1.5456	0.015	-0.1898	0.7698	-0.6262	0.2213	-0.742	-0.5942	0.9902	0.0494	0.3098	0.8068	0.3096	0.9663	46.8438	33.4086	61.27
47	1.4924	-2.0568	-1.622	3.2678	1.3375	3.6244	-0.2983	0.1189	-0.6905	-0.6912	0.5012	-0.3376	0.5444	0.9747	-0.203	0.9551	0.2257	0.1791	0.9976	-0.1471	0.9724	50.9082	30.9365	75.2547
48	0	0	0	0	0	0	-0.2925	-0.5896	0.0382	0.2672	0.0844	-0.6389	-0.3499	0.9212	0.2081	0.9478	0.0113	0.0025	0.9351	0.0198	0.9376	53.0828	36.3677	87.1439
49	5.9821	-2.4818	-0.6756	5.9265	-2.3168	10.1401	-0.0689	-1.2234	0.2746	0.3757	0.0054	-0.6149	0.3955	1.4265	0.0634	0.6155	0.0747	0.0185	0.3593	0.0009	0.6151	43.7855	34.7597	81.182
50	0.5822	-0.1954	0.6484	0.0656	-0.2176	0.7221	-0.0898	-0.276	-0.1005	0.4304	0.1305	-0.4135	-0.0237	0.3255	-0.0408	1.0225	-0.0309	0.0568	1.0076	0.0007	1.0353	44.9	36.8472	97.2452
51	3.9223	1.0466	5.5023	0.5377	1.1707	8.061	-0.4091	-1.9926	-0.9373	1.2626	0.3105	-0.887	0.7087	0.3466	0.0987	0.7228	0.0074	-0.0823	0.9799	-0.1887	0.8264	39.932	39.3017	93.74
52	5.621	-0.0836	-0.1819	1.3736	-0.366	4.1895	0.039	0.5689	0.6851	-0.317	-0.1469	-0.735	0.0917	0.5681	0.1078	0.7194	-0.0054	0.2813	0.3869	0.1641	0.7346	38.3234	38.6341	70.1614
53	6.4163	0.5102	0.3492	4.8914	-0.5574	4.638	-0.13	0.0262	0.7755	0.0781	0.1128	-0.2154	-0.1961	-0.4205	0.0173	0.6242	0.009	0.3222	0.4503	0.2017	0.7627	40.6417	39.0344	68.4125
54	0.0016	-0.016	0.1023	0.1651	-1.0522	6.7053	0.1939	1.2335	-0.7835	-1.4485	-0.2762	-0.0323	-0.2335	0.246	0.0823	0.8138	-0.0466	-0.0464	0.8985	0.159	0.9794	48.0405	45.822	57.6255

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	578 - 588
2	X-RAY DIFFRACTION	2	A	589 - 595
3	X-RAY DIFFRACTION	3	A	596 - 636
4	X-RAY DIFFRACTION	4	A	637 - 647
5	X-RAY DIFFRACTION	5	A	648 - 657
6	X-RAY DIFFRACTION	6	A	658 - 707
7	X-RAY DIFFRACTION	7	A	708 - 733
8	X-RAY DIFFRACTION	8	A	734 - 745
9	X-RAY DIFFRACTION	9	A	746 - 751
10	X-RAY DIFFRACTION	10	B	578 - 586
11	X-RAY DIFFRACTION	11	B	587 - 595
12	X-RAY DIFFRACTION	12	B	596 - 636
13	X-RAY DIFFRACTION	13	B	637 - 647
14	X-RAY DIFFRACTION	14	B	648 - 663
15	X-RAY DIFFRACTION	15	B	664 - 675
16	X-RAY DIFFRACTION	16	B	676 - 732
17	X-RAY DIFFRACTION	17	B	733 - 746
18	X-RAY DIFFRACTION	18	B	747 - 753
19	X-RAY DIFFRACTION	19	C	578 - 587
20	X-RAY DIFFRACTION	20	C	588 - 595
21	X-RAY DIFFRACTION	21	C	596 - 636
22	X-RAY DIFFRACTION	22	C	637 - 644
23	X-RAY DIFFRACTION	23	C	645 - 657
24	X-RAY DIFFRACTION	24	C	658 - 708
25	X-RAY DIFFRACTION	25	C	709 - 732
26	X-RAY DIFFRACTION	26	C	733 - 738
27	X-RAY DIFFRACTION	27	C	744 - 754
28	X-RAY DIFFRACTION	28	D	578 - 589
29	X-RAY DIFFRACTION	29	D	590 - 602
30	X-RAY DIFFRACTION	30	D	603 - 636
31	X-RAY DIFFRACTION	31	D	637 - 650
32	X-RAY DIFFRACTION	32	D	651 - 670
33	X-RAY DIFFRACTION	33	D	671 - 695
34	X-RAY DIFFRACTION	34	D	696 - 721
35	X-RAY DIFFRACTION	35	D	722 - 736
36	X-RAY DIFFRACTION	36	D	737 - 752
37	X-RAY DIFFRACTION	37	E	578 - 588
38	X-RAY DIFFRACTION	38	E	589 - 595
39	X-RAY DIFFRACTION	39	E	596 - 621
40	X-RAY DIFFRACTION	40	E	622 - 636
41	X-RAY DIFFRACTION	41	E	637 - 647
42	X-RAY DIFFRACTION	42	E	648 - 657
43	X-RAY DIFFRACTION	43	E	658 - 731
44	X-RAY DIFFRACTION	44	E	732 - 737
45	X-RAY DIFFRACTION	45	E	745 - 751
46	X-RAY DIFFRACTION	46	F	578 - 588
47	X-RAY DIFFRACTION	47	F	589 - 600
48	X-RAY DIFFRACTION	48	F	601 - 618
49	X-RAY DIFFRACTION	49	F	619 - 638
50	X-RAY DIFFRACTION	50	F	639 - 675
51	X-RAY DIFFRACTION	51	F	676 - 680
52	X-RAY DIFFRACTION	52	F	681 - 699
53	X-RAY DIFFRACTION	53	F	700 - 724
54	X-RAY DIFFRACTION	54	F	725 - 749

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