PDB-7qqg: Crystal structure of MYORG bound to 1-deoxygalactonojirimycin

ID or keywords:

Entry

Database: PDB / ID: 7qqg

Title

Crystal structure of MYORG bound to 1-deoxygalactonojirimycin

Components

Myogenesis-regulating glycosidase

Keywords

HYDROLASE / GH31 / Glycoside hydrolase / MYORG / NET37 / galactosidase

Function / homology

Function and homology information

Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / positive regulation of insulin-like growth factor receptor signaling pathway / skeletal muscle fiber development / hydrolase activity, hydrolyzing O-glycosyl compounds / nuclear membrane / carbohydrate metabolic process / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endoplasmic reticulum membrane
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.43 Å

Authors

Meek, R.W. / Davies, G.J.

Funding support

United Kingdom, 1items

Citation

Journal: Plos Biol. / Year: 2022
Title: The primary familial brain calcification-associated protein MYORG is an alpha-galactosidase with restricted substrate specificity.
Authors: Meek, R.W. / Brockerman, J. / Fordwour, O.B. / Zandberg, W.F. / Davies, G.J. / Vocadlo, D.J.

History

Deposition	Jan 7, 2022	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Aug 31, 2022	Provider: repository / Type: Initial release
Revision 1.1	Jan 18, 2023	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _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 / _citation_author.identifier_ORCID
Revision 1.2	Jan 31, 2024	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_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

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	7qqg.cif.gz	894.5 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	7qqg_validation.pdf.gz	4 MB	Display	wwPDB validaton report
Full document	7qqg_full_validation.pdf.gz	4 MB	Display
Data in XML	7qqg_validation.xml.gz	82.3 KB	Display
Data in CIF	7qqg_validation.cif.gz	112.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qq/7qqg ftp://data.pdbj.org/pub/pdb/validation_reports/qq/7qqg	HTTPS FTP

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Related structure data

Related structure data	7qqfC 7qqhC 2f2hS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	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: Myogenesis-regulating glycosidase

B: Myogenesis-regulating glycosidase

C: Myogenesis-regulating glycosidase

D: Myogenesis-regulating glycosidase

hetero molecules

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

1

A: Myogenesis-regulating glycosidase

D: Myogenesis-regulating glycosidase

hetero molecules

defined by author
Evidence: gel filtration, SEC-MALLS
148 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Myogenesis-regulating glycosidase

C: Myogenesis-regulating glycosidase

hetero molecules

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

Unit cell

Length a, b, c (Å)	73.113, 78.882, 176.221
Angle α, β, γ (deg.)	80.777, 80.209, 62.641
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	2	A
4	2	C
5	3	A
6	3	D
7	4	B
8	4	C
9	5	B
10	5	D
11	6	C
12	6	D

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	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	LEU	LEU	TRP	TRP	A	A	92 - 712	14 - 634
2	2	1	LEU	LEU	TRP	TRP	B	B	92 - 712	14 - 634
3	3	2	LEU	LEU	ALA	ALA	A	A	92 - 713	14 - 635
4	4	2	LEU	LEU	ALA	ALA	C	C	92 - 713	14 - 635
5	5	3	TRP	TRP	TRP	TRP	A	A	185 - 712	107 - 634
6	6	3	TRP	TRP	TRP	TRP	D	D	185 - 712	107 - 634
7	7	4	LEU	LEU	ALA	ALA	B	B	92 - 713	14 - 635
8	8	4	LEU	LEU	ALA	ALA	C	C	92 - 713	14 - 635
9	9	5	TRP	TRP	TRP	TRP	B	B	185 - 712	107 - 634
10	10	5	TRP	TRP	TRP	TRP	D	D	185 - 712	107 - 634
11	11	6	TRP	TRP	TRP	TRP	C	C	185 - 712	107 - 634
12	12	6	TRP	TRP	TRP	TRP	D	D	185 - 712	107 - 634

NCS ensembles :

ID	Details
1	Local NCS retraints between domains: 1 2
2	Local NCS retraints between domains: 3 4
3	Local NCS retraints between domains: 5 6
4	Local NCS retraints between domains: 7 8
5	Local NCS retraints between domains: 9 10
6	Local NCS retraints between domains: 11 12

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Myogenesis-regulating glycosidase / Uncharacterized family 31 glucosidase KIAA1161 Mass: 72463.234 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MYORG, KIAA1161 / Production host: Trichoplusia ni (cabbage looper) / Variant (production host): Hi Five References: UniProt: Q6NSJ0, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

#1: Protein

Myogenesis-regulating glycosidase / Uncharacterized family 31 glucosidase KIAA1161

Mass: 72463.234 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: MYORG, KIAA1161 / Production host:

Trichoplusia ni (cabbage looper) / Variant (production host): Hi Five
References: UniProt: Q6NSJ0, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

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Sugars , 3 types, 17 molecules

#2: Polysaccharide

2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose

Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source

Descriptor	Type	Program
DGlcpNAcb1-4DGlcpNAcb1-ROH	Glycam Condensed Sequence	GMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1	WURCS	PDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}	LINUCS	PDB-CARE

#3: Polysaccharide

2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...

Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source

Descriptor	Type	Program
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH	Glycam Condensed Sequence	GMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1	WURCS	PDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}	LINUCS	PDB-CARE

#4: Sugar

ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE

Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₈H₁₅NO₆

Identifier	Type	Program
DGlcpNAcb	CONDENSED IUPAC CARBOHYDRATE SYMBOL	GMML 1.0
N-acetyl-b-D-glucopyranosamine	COMMON NAME	GMML 1.0
b-D-GlcpNAc	IUPAC CARBOHYDRATE SYMBOL	PDB-CARE 1.0
GlcNAc	SNFG CARBOHYDRATE SYMBOL	GMML 1.0

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Non-polymers , 3 types, 239 molecules

#5: Chemical	ChemComp-DGJ / (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol / 1-deoxygalactonojirimycin Mass: 163.172 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₆H₁₃NO₄ / Feature type: SUBJECT OF INVESTIGATION / Comment: medication, Galafold*YM
#6: Chemical	ChemComp-MLI / MALONATE ION Mass: 102.046 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₃H₂O₄
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 233 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.06 Å³/Da / Density % sol: 59.74 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 100 mM HEPES pH 7.0, 10% PEG MME5000, 5% tasimate pH 7.0

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

Diamond

/ Beamline: I04 / Wavelength: 0.9795 Å

Detector

Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Feb 20, 2020

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.9795 Å / Relative weight: 1

Reflection

Resolution: 2.43→69.75 Å / Num. obs: 127078 / % possible obs: 98.3 % / Redundancy: 3.5 % / CC_1/2: 0.995 / R_merge(I) obs: 0.073 / R_pim(I) all: 0.073 / R_rim(I) all: 0.103 / Net I/σ(I): 8.4

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all
13.31-69.75	3.6	0.023	24.4	776	0.998	0.023	0.032
2.43-2.47	3.7	0.724	1.4	6328	0.555	0.724	1.024

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0267	refinement
DIALS		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2F2H

2f2h

Resolution: 2.43→69.75 Å / Cor.coef. F_o:F_c: 0.934 / Cor.coef. F_o:F_c free: 0.918 / SU B: 21.247 / SU ML: 0.223 / Cross valid method: THROUGHOUT / ESU R: 0.375 / ESU R Free: 0.249
Details: Hydrogens have been added in their riding positions

	R_factor	Num. reflection	% reflection
R_free	0.2497	6096	4.802 %
R_work	0.2239	120841	-
all	0.225	-	-
obs	-	126937	98.126 %

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT

Displacement parameters

B_iso mean: 56.614 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-2.596 Å²	0.001 Å²	2.982 Å²
2-	-	0.311 Å²	-1.895 Å²
3-	-	-	2.49 Å²

Refinement step

Cycle: LAST / Resolution: 2.43→69.75 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	18863	0	404	233	19500

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.006	0.013	19895
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.015	18068
X-RAY DIFFRACTION	r_angle_refined_deg	1.428	1.675	27168
X-RAY DIFFRACTION	r_angle_other_deg	1.166	1.601	41474
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.435	5	2338
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	26.366	20.097	1133
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.865	15	2879
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	20.098	15	188
X-RAY DIFFRACTION	r_chiral_restr	0.061	0.2	2494
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	22344
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	5013
X-RAY DIFFRACTION	r_nbd_refined	0.191	0.2	3497
X-RAY DIFFRACTION	r_symmetry_nbd_other	0.184	0.2	17194
X-RAY DIFFRACTION	r_nbtor_refined	0.167	0.2	9438
X-RAY DIFFRACTION	r_symmetry_nbtor_other	0.074	0.2	9273
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.157	0.2	534
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_other	0.046	0.2	9
X-RAY DIFFRACTION	r_symmetry_nbd_refined	0.096	0.2	10
X-RAY DIFFRACTION	r_nbd_other	0.209	0.2	58
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_refined	0.28	0.2	6
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.172	0.2	1
X-RAY DIFFRACTION	r_mcbond_it	1.1	3.096	9391
X-RAY DIFFRACTION	r_mcbond_other	1.1	3.096	9390
X-RAY DIFFRACTION	r_mcangle_it	1.804	4.643	11716
X-RAY DIFFRACTION	r_mcangle_other	1.804	4.643	11717
X-RAY DIFFRACTION	r_scbond_it	1.042	3.194	10504
X-RAY DIFFRACTION	r_scbond_other	1.041	3.195	10505
X-RAY DIFFRACTION	r_scangle_it	1.706	4.758	15452
X-RAY DIFFRACTION	r_scangle_other	1.706	4.759	15453
X-RAY DIFFRACTION	r_lrange_it	4.222	58.932	84108
X-RAY DIFFRACTION	r_lrange_other	4.218	58.923	84070
X-RAY DIFFRACTION	r_ncsr_local_group_1	0.076	0.05	20904
X-RAY DIFFRACTION	r_ncsr_local_group_2	0.073	0.05	20754
X-RAY DIFFRACTION	r_ncsr_local_group_3	0.067	0.05	16623
X-RAY DIFFRACTION	r_ncsr_local_group_4	0.075	0.05	20787
X-RAY DIFFRACTION	r_ncsr_local_group_5	0.078	0.05	16469
X-RAY DIFFRACTION	r_ncsr_local_group_6	0.071	0.05	16465

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Refine-ID	Type	Rms dev position (Å)	Weight position
1	1	A	X-RAY DIFFRACTION	Local ncs	0.07581	0.0501
1	2	B	X-RAY DIFFRACTION	Local ncs	0.07581	0.0501
2	3	A	X-RAY DIFFRACTION	Local ncs	0.07276	0.0501
2	4	C	X-RAY DIFFRACTION	Local ncs	0.07276	0.0501
3	5	A	X-RAY DIFFRACTION	Local ncs	0.06654	0.0501
3	6	D	X-RAY DIFFRACTION	Local ncs	0.06654	0.0501
4	7	B	X-RAY DIFFRACTION	Local ncs	0.07507	0.0501
4	8	C	X-RAY DIFFRACTION	Local ncs	0.07507	0.0501
5	9	B	X-RAY DIFFRACTION	Local ncs	0.07786	0.05009
5	10	D	X-RAY DIFFRACTION	Local ncs	0.07786	0.05009
6	11	C	X-RAY DIFFRACTION	Local ncs	0.07133	0.05009
6	12	D	X-RAY DIFFRACTION	Local ncs	0.07133	0.05009

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 (%)
2.43-2.493	0.309	449	0.304	8856	X-RAY DIFFRACTION	97.1599
2.493-2.561	0.294	424	0.291	8681	X-RAY DIFFRACTION	97.3797
2.561-2.636	0.299	443	0.277	8435	X-RAY DIFFRACTION	97.4855
2.636-2.717	0.309	437	0.284	8201	X-RAY DIFFRACTION	97.6376
2.717-2.806	0.282	453	0.25	7850	X-RAY DIFFRACTION	97.7744
2.806-2.904	0.26	387	0.251	7635	X-RAY DIFFRACTION	97.889
2.904-3.014	0.278	363	0.229	7484	X-RAY DIFFRACTION	98.1734
3.014-3.137	0.256	346	0.221	7158	X-RAY DIFFRACTION	98.0018
3.137-3.276	0.227	398	0.209	6821	X-RAY DIFFRACTION	98.2043
3.276-3.436	0.26	321	0.208	6627	X-RAY DIFFRACTION	98.4415
3.436-3.622	0.226	287	0.208	6276	X-RAY DIFFRACTION	98.5583
3.622-3.841	0.223	283	0.211	5927	X-RAY DIFFRACTION	98.5714
3.841-4.107	0.242	272	0.208	5602	X-RAY DIFFRACTION	98.7559
4.107-4.435	0.24	236	0.2	5217	X-RAY DIFFRACTION	98.8937
4.435-4.858	0.188	240	0.187	4815	X-RAY DIFFRACTION	99.0788
4.858-5.431	0.219	215	0.209	4304	X-RAY DIFFRACTION	99.0791
5.431-6.27	0.256	178	0.225	3843	X-RAY DIFFRACTION	99.015
6.27-7.677	0.263	147	0.234	3264	X-RAY DIFFRACTION	99.1858
7.677-10.846	0.235	148	0.2	2483	X-RAY DIFFRACTION	99.283
10.846-69.75	0.407	69	0.317	1362	X-RAY DIFFRACTION	98.4859

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	0.9406	0.1213	-0.1732	1.1205	0.2148	1.1169	0.0753	-0.0663	0.0603	0.0768	-0.0725	0.0582	0.08	-0.1488	-0.0029	0.2188	-0.0655	0.0248	0.0637	0.0036	0.0159	14.8248	-12.8556	-38.549
2	1.0826	-0.0004	-0.0907	1.2041	-0.0565	1.276	0.0931	0.0441	0.1247	-0.1512	-0.0507	-0.0466	0.0026	0.1636	-0.0423	0.2274	0.0437	0.0494	0.0576	0.0466	0.078	-44.0529	8.7368	94.3605
3	1.1884	-0.1456	-0.3411	1.2655	0.1901	1.5302	0.0345	0.1233	-0.1124	0.0008	0.0485	-0.031	-0.0192	0.0665	-0.0831	0.3325	-0.095	0.1261	0.4681	0.0411	0.1768	-12.2573	4.1186	43.1601
4	4.2947	0.3193	-1.5474	0.4197	-0.0648	1.6353	-0.0075	-0.3222	-0.1673	0.0238	-0.0443	0.1037	-0.0555	0.088	0.0519	0.3447	0.015	0.1353	0.4821	-0.0419	0.2461	-29.5312	-2.9841	3.7607

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	ALL	A	92 - 713
2	X-RAY DIFFRACTION	1	ALL	A	801
3	X-RAY DIFFRACTION	1	ALL	E	1
4	X-RAY DIFFRACTION	1	ALL	F	1
5	X-RAY DIFFRACTION	1	ALL	A	802
6	X-RAY DIFFRACTION	1	ALL	G	1
7	X-RAY DIFFRACTION	1	ALL	G	2
8	X-RAY DIFFRACTION	1	ALL	E	2
9	X-RAY DIFFRACTION	1	ALL	A	803
10	X-RAY DIFFRACTION	1	ALL	F	3
11	X-RAY DIFFRACTION	1	ALL	A	804
12	X-RAY DIFFRACTION	1	ALL	F	2
13	X-RAY DIFFRACTION	2	ALL	B	88 - 713
14	X-RAY DIFFRACTION	2	ALL	B	801
15	X-RAY DIFFRACTION	2	ALL	H	1
16	X-RAY DIFFRACTION	2	ALL	B	802
17	X-RAY DIFFRACTION	2	ALL	B	803
18	X-RAY DIFFRACTION	2	ALL	B	804
19	X-RAY DIFFRACTION	2	ALL	I	1
20	X-RAY DIFFRACTION	2	ALL	J	1
21	X-RAY DIFFRACTION	2	ALL	I	2
22	X-RAY DIFFRACTION	2	ALL	H	2
23	X-RAY DIFFRACTION	3	ALL	C	92 - 713
24	X-RAY DIFFRACTION	3	ALL	K	1
25	X-RAY DIFFRACTION	3	ALL	K	2
26	X-RAY DIFFRACTION	3	ALL	C	801
27	X-RAY DIFFRACTION	3	ALL	C	802
28	X-RAY DIFFRACTION	3	ALL	C	803
29	X-RAY DIFFRACTION	4	ALL	D	185 - 713
30	X-RAY DIFFRACTION	4	ALL	D	1000
31	X-RAY DIFFRACTION	4	ALL	D	1001

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

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