PDB-4cq7: The crystal structure of the allene oxide cyclase 2 from Arabidop...

ID or keywords:

Entry

Database: PDB / ID: 4cq7

Title

The crystal structure of the allene oxide cyclase 2 from Arabidopsis thaliana with bound product - OPDA

Components

ALLENE OXIDE CYCLASE 2, CHLOROPLASTIC

Keywords

ISOMERASE / JASMONATES / CYCLIZATION / ALLENE OXIDE / OXYLIPINS

Function / homology

Function and homology information

allene-oxide cyclase / allene-oxide cyclase activity / stromule / jasmonic acid biosynthetic process / chloroplast envelope / chloroplast stroma / chloroplast thylakoid membrane / response to cold / chloroplast / cytosol
Similarity search - Function

Biological species

ARABIDOPSIS THALIANA (thale cress)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.7 Å

Authors

Terlecka, B.A. / Pollmann, S. / Hofmann, E.

Citation

Journal: To be Published
Title: The Ligand-Bound Structures of the Aoc2 from A. Thaliana and the Implications for the Catalytic Mechanism
Authors: Terlecka, B.A. / Pollmann, S. / Hofmann, E.

History

Deposition	Feb 11, 2014	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Mar 4, 2015	Provider: repository / Type: Initial release
Revision 2.0	Oct 23, 2019	Group: Atomic model / Data collection / Other / Category: atom_site / pdbx_database_status Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _pdbx_database_status.status_code_sf
Revision 2.1	Dec 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_sheet / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_sheet.number_strands / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Remark 700

SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4cq7.cif.gz	219.6 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	4cq7_validation.pdf.gz	975.3 KB	Display	wwPDB validaton report
Full document	4cq7_full_validation.pdf.gz	979.2 KB	Display
Data in XML	4cq7_validation.xml.gz	29.6 KB	Display
Data in CIF	4cq7_validation.cif.gz	45.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cq/4cq7 ftp://data.pdbj.org/pub/pdb/validation_reports/cq/4cq7	HTTPS FTP

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Related structure data

Related structure data	4cq6C 2ginS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	2q4i-d 1z8k-d 2dio-d 4cq6-d 2gin-2 2brj-d 5xvx-d 1m0n-d 6csd-2 2ve3-1 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: ALLENE OXIDE CYCLASE 2, CHLOROPLASTIC

B: ALLENE OXIDE CYCLASE 2, CHLOROPLASTIC

C: ALLENE OXIDE CYCLASE 2, CHLOROPLASTIC

hetero molecules

63.3 kDa, 3 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)	64.500, 100.400, 105.600
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 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	1	CHAIN B AND (RESSEQ 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	1	CHAIN C AND (RESSEQ 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	2	CHAIN A AND (RESSEQ 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	2	CHAIN B AND (RESSEQ 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	2	CHAIN C AND (RESSEQ 16:23 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	3	CHAIN A AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	3	CHAIN B AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	3	CHAIN C AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	4	CHAIN A AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	4	CHAIN B AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	4	CHAIN C AND (RESSEQ 25:26 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	5	CHAIN A AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	5	CHAIN B AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	5	CHAIN C AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	6	CHAIN A AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	6	CHAIN B AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	6	CHAIN C AND (RESSEQ 28:35 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	7	CHAIN A AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	7	CHAIN B AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	7	CHAIN C AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	8	CHAIN A AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	8	CHAIN B AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	8	CHAIN C AND (RESSEQ 43:78 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	9	CHAIN A AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	9	CHAIN B AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	9	CHAIN C AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	10	CHAIN A AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	10	CHAIN B AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	10	CHAIN C AND (RESSEQ 82:101 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	11	CHAIN A AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	11	CHAIN B AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	11	CHAIN C AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	12	CHAIN A AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	12	CHAIN B AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	12	CHAIN C AND (RESSEQ 106:122 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	13	CHAIN A AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	13	CHAIN B AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	13	CHAIN C AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	14	CHAIN A AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	14	CHAIN B AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	14	CHAIN C AND (RESSEQ 141:160 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	15	CHAIN A AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	15	CHAIN B AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	15	CHAIN C AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	16	CHAIN A AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	16	CHAIN B AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	16	CHAIN C AND (RESSEQ 174:177 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	17	CHAIN A AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	17	CHAIN B AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	17	CHAIN C AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	18	CHAIN A AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	18	CHAIN B AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	18	CHAIN C AND (RESSEQ 179:184 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
1	1	19	CHAIN A AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
2	1	19	CHAIN B AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
3	1	19	CHAIN C AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND BACKBONE
1	1	20	CHAIN A AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
2	1	20	CHAIN B AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN
3	1	20	CHAIN C AND (RESSEQ 186:187 ) AND (NOT ELEMENT H) AND (NOT ELEMENT D)AND SIDECHAIN

NCS ensembles :
NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.4783, -0.8688, 0.128), (0.857, -0.4936, -0.148), (0.1918, 0.0389, 0.9807)	-30.1272, -40.1432, 1.7893
2	given	(-0.486, 0.8551, 0.1803), (-0.8665, -0.4984, 0.028), (0.1138, -0.1427, 0.9832)	19.649, -46.0872, -3.7149

#1: Protein	ALLENE OXIDE CYCLASE 2, CHLOROPLASTIC Mass: 20859.670 Da / Num. of mol.: 3 / Fragment: RESIDUE 78-253 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PQE30 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ER2566 / References: UniProt: Q9LS02, allene-oxide cyclase
#2: Chemical	ChemComp-WHW / 9S,13R-12-OXOPHYTODIENOIC ACID Mass: 292.413 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₈H₂₈O₃
#3: Chemical	ChemComp-MRD / (4R)-2-METHYLPENTANE-2,4-DIOL Mass: 118.174 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₆H₁₄O₂ / Comment: precipitant*YM
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 767 / 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: 55 % / Description: NONE
Crystal grow	pH: 5.6 Details: 0.1 M MG-ACETATE, 0.1 M NA-CITRATE PH 5.6, 8% PEG10000

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.914
Detector	Type: ADSC CCD / Detector: CCD / Date: May 18, 2012 / Details: MIRRORS
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.914 Å / Relative weight: 1
Reflection	Resolution: 1.7→60 Å / Num. obs: 76040 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 6.5 % / B_iso Wilson estimate: 12.2 Å² / R_merge(I) obs: 0.17 / Net I/σ(I): 7.6
Reflection shell	Resolution: 1.7→1.74 Å / Redundancy: 7 % / R_merge(I) obs: 0.68 / Mean I/σ(I) obs: 2.7 / % possible all: 100

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Processing

Software

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

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2GIN

2gin

Resolution: 1.7→54.267 Å / SU ML: 0.13 / σ(F): 2.08 / Phase error: 17.8 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1896	3840	5.1 %
R_work	0.1652	-	-
obs	0.1665	75940	99.81 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso mean: 16.1 Å²

Refinement step

Cycle: LAST / Resolution: 1.7→54.267 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4065	0	50	767	4882

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	4246
X-RAY DIFFRACTION	f_angle_d	1.317	5770
X-RAY DIFFRACTION	f_dihedral_angle_d	12.677	1566
X-RAY DIFFRACTION	f_chiral_restr	0.049	632
X-RAY DIFFRACTION	f_plane_restr	0.006	743

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type	Rms dev position (Å)
1	1	A	32	X-RAY DIFFRACTION	POSITIONAL
1	2	B	32	X-RAY DIFFRACTION	POSITIONAL	0.109
1	3	C	32	X-RAY DIFFRACTION	POSITIONAL	0.133
2	1	A	35	X-RAY DIFFRACTION	POSITIONAL
2	2	B	35	X-RAY DIFFRACTION	POSITIONAL	0.228
2	3	C	35	X-RAY DIFFRACTION	POSITIONAL	0.272
3	1	A	8	X-RAY DIFFRACTION	POSITIONAL
3	2	B	8	X-RAY DIFFRACTION	POSITIONAL	0.027
3	3	C	8	X-RAY DIFFRACTION	POSITIONAL	0.02
4	1	A	9	X-RAY DIFFRACTION	POSITIONAL
4	2	B	9	X-RAY DIFFRACTION	POSITIONAL	0.079
4	3	C	9	X-RAY DIFFRACTION	POSITIONAL	0.049
5	1	A	32	X-RAY DIFFRACTION	POSITIONAL
5	2	B	32	X-RAY DIFFRACTION	POSITIONAL	0.081
5	3	C	32	X-RAY DIFFRACTION	POSITIONAL	0.102
6	1	A	35	X-RAY DIFFRACTION	POSITIONAL
6	2	B	35	X-RAY DIFFRACTION	POSITIONAL	0.279
6	3	C	35	X-RAY DIFFRACTION	POSITIONAL	0.188
7	1	A	144	X-RAY DIFFRACTION	POSITIONAL
7	2	B	144	X-RAY DIFFRACTION	POSITIONAL	0.094
7	3	C	144	X-RAY DIFFRACTION	POSITIONAL	0.101
8	1	A	128	X-RAY DIFFRACTION	POSITIONAL
8	2	B	128	X-RAY DIFFRACTION	POSITIONAL	0.153
8	3	C	128	X-RAY DIFFRACTION	POSITIONAL	0.176
9	1	A	80	X-RAY DIFFRACTION	POSITIONAL
9	2	B	80	X-RAY DIFFRACTION	POSITIONAL	0.091
9	3	C	80	X-RAY DIFFRACTION	POSITIONAL	0.09
10	1	A	87	X-RAY DIFFRACTION	POSITIONAL
10	2	B	87	X-RAY DIFFRACTION	POSITIONAL	0.207
10	3	C	87	X-RAY DIFFRACTION	POSITIONAL	0.144
11	1	A	68	X-RAY DIFFRACTION	POSITIONAL
11	2	B	68	X-RAY DIFFRACTION	POSITIONAL	0.087
11	3	C	68	X-RAY DIFFRACTION	POSITIONAL	0.107
12	1	A	57	X-RAY DIFFRACTION	POSITIONAL
12	2	B	57	X-RAY DIFFRACTION	POSITIONAL	0.227
12	3	C	57	X-RAY DIFFRACTION	POSITIONAL	0.194
13	1	A	80	X-RAY DIFFRACTION	POSITIONAL
13	2	B	80	X-RAY DIFFRACTION	POSITIONAL	0.189
13	3	C	80	X-RAY DIFFRACTION	POSITIONAL	0.178
14	1	A	81	X-RAY DIFFRACTION	POSITIONAL
14	2	B	81	X-RAY DIFFRACTION	POSITIONAL	0.293
14	3	C	81	X-RAY DIFFRACTION	POSITIONAL	0.29
15	1	A	16	X-RAY DIFFRACTION	POSITIONAL
15	2	B	16	X-RAY DIFFRACTION	POSITIONAL	0.034
15	3	C	16	X-RAY DIFFRACTION	POSITIONAL	0.059
16	1	A	11	X-RAY DIFFRACTION	POSITIONAL
16	2	B	11	X-RAY DIFFRACTION	POSITIONAL	0.115
16	3	C	11	X-RAY DIFFRACTION	POSITIONAL	0.165
17	1	A	23	X-RAY DIFFRACTION	POSITIONAL
17	2	B	23	X-RAY DIFFRACTION	POSITIONAL	0.086
17	3	C	24	X-RAY DIFFRACTION	POSITIONAL	0.063
18	1	A	12	X-RAY DIFFRACTION	POSITIONAL
18	2	B	12	X-RAY DIFFRACTION	POSITIONAL	0.128
18	3	C	14	X-RAY DIFFRACTION	POSITIONAL	0.12
19	1	A	8	X-RAY DIFFRACTION	POSITIONAL
19	2	B	8	X-RAY DIFFRACTION	POSITIONAL	0.024
19	3	C	8	X-RAY DIFFRACTION	POSITIONAL	0.042
20	1	A	11	X-RAY DIFFRACTION	POSITIONAL
20	2	B	11	X-RAY DIFFRACTION	POSITIONAL	0.034
20	3	C	11	X-RAY DIFFRACTION	POSITIONAL	0.099

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 (%)
1.7-1.7215	0	0	0.196	2777	X-RAY DIFFRACTION	100
1.7215-1.7442	0	0	0.1846	2798	X-RAY DIFFRACTION	100
1.7442-1.7681	0	0	0.1814	2769	X-RAY DIFFRACTION	100
1.7681-1.7934	0.2107	482	0.1738	2316	X-RAY DIFFRACTION	100
1.7934-1.8201	0	0	0.1693	2767	X-RAY DIFFRACTION	100
1.8201-1.8486	0	0	0.1689	2786	X-RAY DIFFRACTION	100
1.8486-1.8789	0.1938	445	0.1667	2314	X-RAY DIFFRACTION	100
1.8789-1.9113	0	0	0.164	2791	X-RAY DIFFRACTION	100
1.9113-1.946	0	0	0.1684	2797	X-RAY DIFFRACTION	100
1.946-1.9835	0.2004	405	0.1603	2360	X-RAY DIFFRACTION	100
1.9835-2.024	0	0	0.1535	2818	X-RAY DIFFRACTION	100
2.024-2.068	0.1761	372	0.156	2409	X-RAY DIFFRACTION	100
2.068-2.1161	0	0	0.1488	2773	X-RAY DIFFRACTION	100
2.1161-2.169	0	0	0.1488	2806	X-RAY DIFFRACTION	100
2.169-2.2276	0.1826	333	0.1455	2484	X-RAY DIFFRACTION	100
2.2276-2.2932	0	0	0.145	2807	X-RAY DIFFRACTION	100
2.2932-2.3672	0.1782	299	0.1391	2471	X-RAY DIFFRACTION	100
2.3672-2.4518	0.1519	70	0.1393	2764	X-RAY DIFFRACTION	100
2.4518-2.55	0.1853	179	0.136	2614	X-RAY DIFFRACTION	100
2.55-2.666	0.1699	230	0.1436	2601	X-RAY DIFFRACTION	100
2.666-2.8066	0.1415	24	0.1463	2806	X-RAY DIFFRACTION	100
2.8066-2.9824	0.1775	177	0.1483	2645	X-RAY DIFFRACTION	100
2.9824-3.2127	0.1892	178	0.152	2655	X-RAY DIFFRACTION	100
3.2127-3.5359	0.182	153	0.1605	2707	X-RAY DIFFRACTION	100
3.5359-4.0474	0.1781	247	0.1682	2619	X-RAY DIFFRACTION	100
4.0474-5.0987	0.2016	126	0.19	2748	X-RAY DIFFRACTION	100
5.0987-54.2942	0.2843	120	0.2508	2898	X-RAY DIFFRACTION	99

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-Yorodumi

-
Movie

-
Structure viewers

+
Viewer log

-
This page

-
This web site

-
Options

+
Open data

-
Basic information

-
Structure visualization

-
Downloads & links

-
Download

-
Validation report

-
Related structure data

-
Links

-
Assembly

-
Components

-
Experimental details

-
Experiment

-
Sample preparation

-
Data collection

-
Processing

+
About Yorodumi

-
News

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

-
Aug 12, 2020. Covid-19 info

+
Mar 5, 2020. Novel coronavirus structure data

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

+
Jul 12, 2017. Major update of PDB

-
Yorodumi