PDB-3ooj: C1A mutant of E. coli GlmS in complex with glucose-6P and glutamate

ID or keywords:

Entry

Database: PDB / ID: 3ooj

Title

C1A mutant of E. coli GlmS in complex with glucose-6P and glutamate

Components

Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

Keywords

TRANSFERASE / ammonia channel /

glutamine amidotransferase

Function / homology

Function and homology information

glutamine-fructose-6-phosphate transaminase (isomerizing) /

glutamine-fructose-6-phosphate transaminase (isomerizing) activity / UDP-N-acetylglucosamine metabolic process / UDP-N-acetylglucosamine biosynthetic process / carbohydrate derivative binding / fructose 6-phosphate metabolic process / protein N-linked glycosylation / glutamine metabolic process / carbohydrate metabolic process /

cytosol
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.5 Å

Authors

Mouilleron, S. / Golinelli-Pimpaneau, B.

Citation

Journal: J.Biol.Chem. / Year: 2012
Title: Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer.
Authors: Mouilleron, S. / Badet-Denisot, M.A. / Pecqueur, L. / Madiona, K. / Assrir, N. / Badet, B. / Golinelli-Pimpaneau, B.

History

Deposition	Aug 31, 2010	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 19, 2011	Provider: repository / Type: Initial release
Revision 1.1	Jul 29, 2020	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_ref_seq_dif / struct_site / struct_site_gen Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_ref_seq_dif.details Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.2	Sep 13, 2023	Group: Data collection / Database references / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / citation / citation_author / database_2 Item: _chem_comp.pdbx_synonyms / _citation.country ..._chem_comp.pdbx_synonyms / _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3ooj.cif.gz	1.8 MB	Display	PDBx/mmCIF format
PDB format	pdb3ooj.ent.gz	1.5 MB	Display	PDB format
PDBx/mmJSON format	3ooj.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/oo/3ooj ftp://data.pdbj.org/pub/pdb/validation_reports/oo/3ooj	HTTPS FTP

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Related structure data

Related structure data	2j6h 2vf4 2vf5 4amv
Similar structure data	5kbu-d 8821 5y3r-d 9714 11941 5wem-d 5byv-d 8688 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
Related items in Molecule of the Month	#166 - Oct 2013 Proteasome similarity (1) #235 - Jul 2019 AMPA Receptor similarity (1) #80 - Aug 2006 AAA+ Proteases similarity (1) #191 - Nov 2015 Glutamate-gated Chloride Receptors similarity (1) #176 - Aug 2014 Dynein similarity (1) #60 - Dec 2004 Ubiquitin similarity (1)

Deposited unit

A: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

B: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

C: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

D: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

E: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

F: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

G: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

H: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

hetero molecules

541 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

2

B: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

D: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

E: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

F: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

H: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

hetero molecules

B: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

D: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

E: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

F: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

H: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

hetero molecules

B: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

D: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

E: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

F: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

H: Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

hetero molecules

defined by author&software
1.01 MDa, 15 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	247.599, 247.599, 630.862
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	155
Space group name H-M	H32

Components on special symmetry positions

ID	Model	Components
1	1	H-676- HOH

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Protein / Sugars , 2 types, 16 molecules ABCDEFGH

#1: Protein

Glucosamine/fructose-6-phosphate aminotransferase, isomerizing

Mass: 66813.945 Da / Num. of mol.: 8 / Fragment: glucosamine-6P synthase / Mutation: C1A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Plasmid: PMA1 / Production host:

Escherichia coli (E. coli) / Strain (production host): HB101 / References: UniProt: C9QXA7, UniProt: P17169*PLUS

#3: Sugar

ChemComp-G6P / 6-O-phosphono-alpha-D-glucopyranose / ALPHA-D-GLUCOSE-6-PHOSPHATE / 6-O-phosphono-alpha-D-glucose / 6-O-phosphono-D-glucose / 6-O-phosphono-glucose

Type: D-saccharide, alpha linking / Mass: 260.136 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C₆H₁₃O₉P

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Non-polymers , 4 types, 1477 molecules

#2: Chemical	ChemComp-GLU / GLUTAMIC ACID / Glutamic acid Type: L-peptide linking / Mass: 147.129 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₅H₉NO₄
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Chemical	ChemComp-G6Q / GLUCOSE-6-PHOSPHATE / Glucose 6-phosphate Mass: 260.136 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Formula: C₆H₁₃O₉P
#6: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 1453 / 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: 3.48 Å³/Da / Density % sol: 64.67 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 22% PEG3350, 0.2 ammonium acetate, 0.1M HEPES pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å
Detector	Type: ADSC / Detector: CCD / Date: Mar 14, 2004
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.933 Å / Relative weight: 1
Reflection	Resolution: 2.5→30 Å / Num. obs: 250723 / % possible obs: 98.6 % / Redundancy: 7.9 % / R_sym value: 0.113 / Net I/σ(I): 5.3
Reflection shell	Resolution: 2.5→2.64 Å / Redundancy: 4.6 % / R_merge(I) obs: 0.648 / Mean I/σ(I) obs: 1.1 / % possible all: 91.3

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Processing

Software

Name	Version	Classification
PHASER		phasing
PHENIX	(phenix.refine: 1.5_2)	refinement
MOSFLM		data reduction
SCALA		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.5→19.993 Å / SU ML: 0.82 / σ(F): 1.34 / Phase error: 21.7 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2204	12632	5.04 %
R_work	0.1784	-	-
obs	0.1805	250721	98.51 %

Solvent computation

Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 55.223 Å² / k_sol: 0.341 e/Å³

Displacement parameters

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.0299 Å²	-0 Å²	0 Å²
2-	-	-0.0299 Å²	0 Å²
3-	-	-	0.0598 Å²

Refinement step

Cycle: LAST / Resolution: 2.5→19.993 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	37120	0	384	1453	38957

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	38279
X-RAY DIFFRACTION	f_angle_d	1.178	51885
X-RAY DIFFRACTION	f_dihedral_angle_d	17.574	14271
X-RAY DIFFRACTION	f_chiral_restr	0.078	5959
X-RAY DIFFRACTION	f_plane_restr	0.005	6724

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 (%)
2.5-2.5284	0.3335	391	0.2792	6941	X-RAY DIFFRACTION	87
2.5284-2.558	0.2842	403	0.2458	7123	X-RAY DIFFRACTION	89
2.558-2.5892	0.2964	396	0.2568	7363	X-RAY DIFFRACTION	92
2.5892-2.6219	0.3168	411	0.2476	7511	X-RAY DIFFRACTION	94
2.6219-2.6563	0.2839	409	0.2282	7695	X-RAY DIFFRACTION	96
2.6563-2.6926	0.2638	435	0.2183	7889	X-RAY DIFFRACTION	98
2.6926-2.731	0.2834	453	0.2191	7956	X-RAY DIFFRACTION	100
2.731-2.7716	0.2984	414	0.221	8023	X-RAY DIFFRACTION	100
2.7716-2.8148	0.2606	432	0.2081	8028	X-RAY DIFFRACTION	100
2.8148-2.8609	0.2855	395	0.2153	8020	X-RAY DIFFRACTION	100
2.8609-2.91	0.2427	438	0.2073	8019	X-RAY DIFFRACTION	100
2.91-2.9628	0.2669	434	0.2101	8033	X-RAY DIFFRACTION	100
2.9628-3.0196	0.2448	405	0.2021	8019	X-RAY DIFFRACTION	100
3.0196-3.081	0.2788	422	0.2057	7984	X-RAY DIFFRACTION	100
3.081-3.1478	0.2361	432	0.1911	8039	X-RAY DIFFRACTION	100
3.1478-3.2207	0.2467	413	0.1954	8040	X-RAY DIFFRACTION	100
3.2207-3.3009	0.23	432	0.1902	8022	X-RAY DIFFRACTION	100
3.3009-3.3897	0.2487	477	0.1957	8013	X-RAY DIFFRACTION	100
3.3897-3.4889	0.2445	430	0.195	8020	X-RAY DIFFRACTION	100
3.4889-3.6009	0.2202	422	0.1813	8019	X-RAY DIFFRACTION	100
3.6009-3.7288	0.2293	430	0.1832	8035	X-RAY DIFFRACTION	100
3.7288-3.8771	0.2135	388	0.1702	8083	X-RAY DIFFRACTION	100
3.8771-4.0522	0.1962	418	0.1632	8061	X-RAY DIFFRACTION	100
4.0522-4.2639	0.1726	430	0.1421	8047	X-RAY DIFFRACTION	100
4.2639-4.5281	0.1636	395	0.1338	8110	X-RAY DIFFRACTION	100
4.5281-4.873	0.1736	402	0.1316	8157	X-RAY DIFFRACTION	100
4.873-5.3549	0.1895	436	0.1458	8095	X-RAY DIFFRACTION	100
5.3549-6.1103	0.1925	429	0.1725	8167	X-RAY DIFFRACTION	100
6.1103-7.6266	0.2191	413	0.1752	8227	X-RAY DIFFRACTION	100
7.6266-19.994	0.1672	447	0.1557	8350	X-RAY DIFFRACTION	100

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	0.0948	0.0417	-0.0273	0.074	-0.0037	0.0514	0.149	-0.2431	-0.1611	0.0773	-0.0558	0.0045	0.1873	-0.0313	0.0103	0.3126	-0.1075	-0.0941	0.2113	0.0818	0.2977	-41.8049	-72.2583	-45.453
2	0.1914	0.1009	-0.0688	0.0816	0.002	0.2041	-0.016	-0.0124	-0.045	0.0068	-0.0061	0.0385	0.0423	-0.0017	-0.0283	0.1901	-0.031	-0.0531	0.1366	-0.0101	0.1834	-29.5226	-53.3377	-71.4381
3	0.0513	-0.0273	0.0164	0.0358	0.0013	0.0439	0.0277	0.2149	-0.2722	-0.1899	-0.0268	0.1996	-0.0593	0.0335	-0	0.3817	-0.0886	0.0194	0.5097	-0.1937	0.5624	-12.3329	-82.5125	-115.7691
4	0.1722	0.0183	-0.0355	0.0612	-0.0267	0.1016	-0.0331	0.0555	0.019	-0.0411	0.0424	-0.0001	-0.0234	0.0276	0.0237	0.2491	-0.0628	-0.0418	0.167	-0.0185	0.1418	-12.6214	-43.3184	-92.4306
5	0.0825	-0.0795	0.0441	0.0885	-0.0326	0.0377	0.0416	-0.0284	-0.2353	0.0114	0.0596	0.0634	0.2382	0.0417	0.0701	0.6156	0.5882	-0.05	0.1805	0.0825	0.2946	29.1032	-69.0807	-17.9412
6	0.1775	-0.0608	-0.0089	0.1232	-0.007	0.1627	0.0025	-0.0259	-0.0323	0.0118	-0.0049	-0.0018	0.0548	0.0162	-0.022	0.107	0.0056	-0.0092	0.0723	-0.0181	0.0716	7.1234	-42.8558	-24.3872
7	0.0208	0.0104	-0.0098	0.027	0.0024	0.0211	0.1146	-0.1112	0.0591	0.3472	-0.2182	0.2568	0.1286	-0.2397	-0.0019	0.5321	-0.268	0.1364	0.702	-0.1404	0.3646	-50.663	-51.1412	-12.0792
8	0.1584	0.0066	0.0904	0.1453	0.0132	0.1384	-0.0072	-0.0214	0.0035	-0.0279	-0.0129	0.0158	-0.0225	-0.0307	-0.0349	0.114	0.0092	0.0004	0.1215	-0.0057	0.1062	-14.7863	-27.4665	-33.233
9	0.0418	0.0491	-0.0232	0.1601	-0.0145	0.0455	0.0241	0.3874	0.0776	-0.0082	0.1129	-0.0568	-0.0684	-0.304	0.0667	0.3058	0.0876	0.1402	0.5057	0.074	0.2696	42.8539	4.0694	-161.614
10	0.0679	0.055	-0.0593	0.2095	-0.0606	0.1121	0.0383	0.1105	-0.0824	-0.0646	-0.048	-0.1523	-0.0451	0.0269	-0.0098	0.1181	0.0355	0.013	0.2355	-0.0034	0.2058	31.4446	-15.1644	-135.2227
11	0.034	0.0085	0.0116	0.0225	0.022	0.0435	-0.0134	0.0186	-0.0478	0.0504	-0.0305	-0.0379	0.1218	0.0494	-0.001	0.2915	0.1059	0.0743	0.6975	-0.2746	0.6155	12.8518	-63.7158	-152.0205
12	0.1704	0.0969	-0.0328	0.1279	-0.1294	0.1342	0.051	-0.0081	-0.107	0.0686	-0.0359	-0.067	0.0165	-0.0175	-0	0.2369	0.0113	-0.031	0.1839	-0.0279	0.2259	15.3175	-31.6694	-118.8418
13	0.0274	-0.0237	-0.0032	0.0175	0.0056	0.0237	-0.1323	-0.1162	-0.1146	0.0105	-0.0616	-0.011	0.0028	0.1418	-0	0.4766	0.2251	0.0264	0.7156	0.1966	0.662	66.6789	-62.5745	-30.7264
14	0.1377	0.1071	-0.0341	0.1368	0.0432	0.0985	-0.0085	-0.0314	0.0203	-0.0258	0.0166	-0.0626	0.0031	0.0362	0.0061	0.1268	0.0302	0.0225	0.1608	-0.0305	0.1715	38.9486	-37.3885	-60.4357
15	0.0984	-0.0016	-0.0067	0.0733	0.0494	0.0556	-0.1114	0.0691	-0.1945	0.1516	0.0327	0.0064	0.2511	-0.0369	-0.0351	0.4394	-0.0439	0.1412	0.2396	-0.0753	0.5103	17.4249	-87.9666	-89.7574
16	0.1874	0.0491	0.1036	0.1944	0.0746	0.1091	0.0135	-0.1203	-0.4184	-0.1304	0.2356	0.0591	0.1688	-0.14	0.3536	0.147	0.1065	0.2399	-0.0516	-0.2808	0.0257	30.6313	-58.3957	-77.8995
17	-0.0039	0.0236	0.0026	-0.0019	-0.0081	-0.0022	-0.0243	-0.0024	-0.0074	0.0114	0.0039	-0.0088	0.0077	0.0275	-0	0.5482	-0.0389	-0.0367	0.5794	-0.0037	0.5706	4.7472	-34.6579	-76.7594

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	(CHAIN A AND RESID 1:239) OR (CHAIN I AND RESID 701:701)	A	1 - 239
2	X-RAY DIFFRACTION	1	(CHAIN A AND RESID 1:239) OR (CHAIN I AND RESID 701:701)	I	701
3	X-RAY DIFFRACTION	2	(CHAIN A AND RESID 240:608) OR (CHAIN T AND RESID 611:611)	A	240 - 608
4	X-RAY DIFFRACTION	2	(CHAIN A AND RESID 240:608) OR (CHAIN T AND RESID 611:611)	T	611
5	X-RAY DIFFRACTION	3	(CHAIN B AND RESID 1:239)	B	1 - 239
6	X-RAY DIFFRACTION	4	(CHAIN B AND RESID 240:608) OR (CHAIN T AND RESID 612:612)	B	240 - 608
7	X-RAY DIFFRACTION	4	(CHAIN B AND RESID 240:608) OR (CHAIN T AND RESID 612:612)	T	612
8	X-RAY DIFFRACTION	5	(CHAIN C AND RESID 1:236)	C	1 - 236
9	X-RAY DIFFRACTION	6	(CHAIN C AND RESID 244:608) OR (CHAIN T AND RESID 610:610)	C	244 - 608
10	X-RAY DIFFRACTION	6	(CHAIN C AND RESID 244:608) OR (CHAIN T AND RESID 610:610)	T	610
11	X-RAY DIFFRACTION	7	(CHAIN D AND RESID 1:235)	D	1 - 235
12	X-RAY DIFFRACTION	8	(CHAIN U AND RESID 1:1) OR (CHAIN D AND RESID 242:608) OR (CHAIN T AND RESID 609:609)	U	1
13	X-RAY DIFFRACTION	8	(CHAIN U AND RESID 1:1) OR (CHAIN D AND RESID 242:608) OR (CHAIN T AND RESID 609:609)	D	242 - 608
14	X-RAY DIFFRACTION	8	(CHAIN U AND RESID 1:1) OR (CHAIN D AND RESID 242:608) OR (CHAIN T AND RESID 609:609)	T	609
15	X-RAY DIFFRACTION	9	(CHAIN E AND RESID 1:236)	E	1 - 236
16	X-RAY DIFFRACTION	10	(CHAIN E AND RESID 243:608) OR (CHAIN T AND RESID 616:616)	E	243 - 608
17	X-RAY DIFFRACTION	10	(CHAIN E AND RESID 243:608) OR (CHAIN T AND RESID 616:616)	T	616
18	X-RAY DIFFRACTION	11	(CHAIN F AND RESID 1:230)	F	1 - 230
19	X-RAY DIFFRACTION	12	(CHAIN T AND RESID 615:615) OR (CHAIN F AND RESID 245:608)	T	615
20	X-RAY DIFFRACTION	12	(CHAIN T AND RESID 615:615) OR (CHAIN F AND RESID 245:608)	F	245 - 608
21	X-RAY DIFFRACTION	13	(CHAIN G AND RESID 1:238)	G	1 - 238
22	X-RAY DIFFRACTION	14	(CHAIN T AND RESID 613:613) OR (CHAIN G AND RESID 242:608)	T	613
23	X-RAY DIFFRACTION	14	(CHAIN T AND RESID 613:613) OR (CHAIN G AND RESID 242:608)	G	242 - 608
24	X-RAY DIFFRACTION	15	(CHAIN H AND RESID 1:240)	H	1 - 240
25	X-RAY DIFFRACTION	16	(CHAIN H AND RESID 241:608) OR (CHAIN T AND RESID 614:614)	H	241 - 608
26	X-RAY DIFFRACTION	16	(CHAIN H AND RESID 241:608) OR (CHAIN T AND RESID 614:614)	T	614
27	X-RAY DIFFRACTION	17	(CHAIN V AND RESID 1:8)	V	1 - 8

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Feb 9, 2022. New format data for meta-information of EMDB entries

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