PDB-4evi: Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransfe...

ID or keywords:

Entry

Database: PDB / ID: 4evi

Title

Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum in Complex with Coniferyl Alcohol 9-Methyl Ether and S -Adenosyl-L-Homocysteine

Components

Coniferyl alcohol 9-O-methyltransferase

Keywords

TRANSFERASE / Rossmann fold / Dimer / small molecule O-methyltransferase / S-Adenosyl-L-methionine / coniferyl alcohol / S -Adenosyl-L-homocysteine

Function / homology

Function and homology information

acetylserotonin O-methyltransferase activity / melatonin biosynthetic process / methylation / protein dimerization activity
Similarity search - Function

Biological species

Linum nodiflorum (plant)

Method

X-RAY DIFFRACTION /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.015 Å

Authors

Wolters, S. / Heine, A. / Petersen, M.

Citation

Journal: Acta Crystallogr.,Sect.D / Year: 2013
Title: Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.
Authors: Wolters, S. / Neeb, M. / Berim, A. / Schulze Wischeler, J. / Petersen, M. / Heine, A.

History

Deposition	Apr 26, 2012	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 1, 2013	Provider: repository / Type: Initial release
Revision 1.1	May 15, 2013	Group: Database references
Revision 1.2	Sep 13, 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_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

-
Download

PDBx/mmCIF format	4evi.cif.gz	303.9 KB	Display	PDBx/mmCIF format
PDB format	pdb4evi.ent.gz	243.6 KB	Display	PDB format
PDBx/mmJSON format	4evi.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

-
Validation report

Summary document	4evi_validation.pdf.gz	762 KB	Display	wwPDB validaton report
Full document	4evi_full_validation.pdf.gz	767.4 KB	Display
Data in XML	4evi_validation.xml.gz	31.4 KB	Display
Data in CIF	4evi_validation.cif.gz	45.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ev/4evi ftp://data.pdbj.org/pub/pdb/validation_reports/ev/4evi	HTTPS FTP

-
Related structure data

Related structure data	4e70C 4emsSC C: citing same article (ref.) S: Starting model for refinement
Similar structure data	4ems-d 4e70-d 6tz6-1 6brg-3 2pqg-d 6brg-4 6i6n-d 6brk-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

-
Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Coniferyl alcohol 9-O-methyltransferase

B: Coniferyl alcohol 9-O-methyltransferase

hetero molecules

88 kDa, 2 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)	75.842, 105.042, 108.983
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

-
Protein , 1 types, 2 molecules AB

#1: Protein	Coniferyl alcohol 9-O-methyltransferase / S-adenosyl-L-methionine-dependent coniferyl alcohol 9-O-methyltransferase Mass: 43425.492 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Linum nodiflorum (plant) / Gene: CA9OMT / Plasmid: pet15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: A6XNE6

#1: Protein

Coniferyl alcohol 9-O-methyltransferase / S-adenosyl-L-methionine-dependent coniferyl alcohol 9-O-methyltransferase

Mass: 43425.492 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Linum nodiflorum (plant) / Gene: CA9OMT / Plasmid: pet15b / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: A6XNE6

-
Non-polymers , 5 types, 456 molecules

#2: Chemical	ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₄H₂₀N₆O₅S
#3: Chemical	ChemComp-C9M / 2-methoxy-4-[(1E)-3-methoxyprop-1-en-1-yl]phenol Mass: 194.227 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₁H₁₄O₃
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Chemical	ChemComp-N7I / 4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol / Coniferyl alcohol Mass: 180.200 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₀H₁₂O₃
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 449 / Source method: isolated from a natural source / Formula: H₂O

-
Experiment

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

-
Sample preparation

Crystal	Density Matthews: 2.5 Å³/Da / Density % sol: 50.78 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 1 M Na/K phosphate, 0,7M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

-
Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source: SEALED TUBE / Type: OTHER / Wavelength: 1.54178 Å

Detector

Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Aug 8, 2011

Radiation

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

Radiation wavelength

Wavelength: 1.54178 Å / Relative weight: 1

Reflection

Resolution: 2.015→10 Å / Num. all: 57450 / Num. obs: 57450 / % possible obs: 99.8 % / Redundancy: 5.2 % / R_sym value: 0.091 / Χ²: 1.039 / Net I/σ(I): 9.7

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
2.015-2.05	5.1	0.502	2840	0.998	1	99.9
2.05-2.09	5.1	0.429	2799	1.043	1	99.8
2.09-2.13	5.1	0.395	2860	1.025	1	100
2.13-2.17	5.1	0.316	2875	0.997	1	100
2.17-2.22	5.1	0.295	2820	1.055	1	99.8
2.22-2.27	5.1	0.274	2815	1.055	1	99.9
2.27-2.33	5.2	0.228	2880	1.035	1	100
2.33-2.39	5.2	0.207	2835	1.06	1	99.9
2.39-2.46	5.2	0.187	2874	1.048	1	99.9
2.46-2.54	5.2	0.168	2855	1.066	1	99.9
2.54-2.63	5.2	0.145	2855	1.026	1	100
2.63-2.73	5.2	0.127	2863	1.064	1	100
2.73-2.85	5.3	0.115	2868	1.037	1	100
2.85-3	5.2	0.101	2848	1.051	1	99.8
3-3.18	5.2	0.083	2910	1.072	1	99.9
3.18-3.42	5.3	0.066	2901	1.044	1	100
3.42-3.74	5.3	0.056	2890	1.059	1	100
3.74-4.25	5.3	0.051	2940	1.007	1	100
4.25-5.22	5.2	0.043	2951	1.099	1	100
5.22-10	4.6	0.044	2971	0.919	1	97.6

-
Phasing

Phasing

Method:

molecular replacement

Phasing MR

R_factor: 28.42 / Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	2.6 Å	24.91 Å
Translation	2.6 Å	24.91 Å

-
Processing

Software

Name	Version	Classification
SCALEPACK		data scaling
PHASER	2.1.4	phasing
PHENIX	1.7.1_743	refinement
PDB_EXTRACT	3.11	data extraction
MAR345dtb		data collection
HKL-2000		data reduction
HKL-2000		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4EMS

4ems

Resolution: 2.015→9.34 Å / Occupancy max: 1 / Occupancy min: 0.34 / FOM work R set: 0.8789 / SU ML: 0.48 / σ(F): 1.34 / Phase error: 19 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2031	2903	5.07 %	RANDOM
R_work	0.1759	-	-	-
obs	0.1773	57246	99.5 %	-
all	-	57246	-	-

Solvent computation

Shrinkage radii: 1.06 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 52.478 Å² / k_sol: 0.447 e/Å³

Displacement parameters

B_iso max: 71.43 Å² / B_iso mean: 25.3694 Å² / B_iso min: 8.56 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.7907 Å²	0 Å²	0 Å²
2-	-	1.6305 Å²	0 Å²
3-	-	-	0.1602 Å²

Refinement step

Cycle: LAST / Resolution: 2.015→9.34 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5515	0	77	449	6041

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	5855
X-RAY DIFFRACTION	f_angle_d	1.01	7980
X-RAY DIFFRACTION	f_chiral_restr	0.065	887
X-RAY DIFFRACTION	f_plane_restr	0.005	1022
X-RAY DIFFRACTION	f_dihedral_angle_d	13.51	2086

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 21

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.015-2.0477	0.272	127	0.2224	2428	2555	95
2.0477-2.0827	0.2495	148	0.2055	2535	2683	100
2.0827-2.1201	0.2416	133	0.1991	2591	2724	100
2.1201-2.1604	0.2579	118	0.1816	2589	2707	100
2.1604-2.2039	0.2215	138	0.1805	2555	2693	100
2.2039-2.2512	0.2458	138	0.1793	2577	2715	100
2.2512-2.3028	0.2192	146	0.1686	2575	2721	100
2.3028-2.3595	0.1973	143	0.1668	2563	2706	100
2.3595-2.4222	0.2115	134	0.1645	2584	2718	100
2.4222-2.4922	0.2212	140	0.1608	2581	2721	100
2.4922-2.571	0.1858	156	0.1561	2558	2714	100
2.571-2.6608	0.2081	137	0.1606	2577	2714	100
2.6608-2.7647	0.2035	126	0.1725	2622	2748	100
2.7647-2.887	0.2204	148	0.1777	2586	2734	100
2.887-3.0342	0.2086	138	0.1741	2608	2746	100
3.0342-3.217	0.2181	132	0.1783	2605	2737	100
3.217-3.4537	0.2011	154	0.1702	2604	2758	100
3.4537-3.7802	0.1799	125	0.1635	2646	2771	100
3.7802-4.2805	0.1698	158	0.1557	2610	2768	100
4.2805-5.2303	0.1691	136	0.1452	2680	2816	100
5.2303-9.34	0.2083	128	0.2665	2669	2797	97

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	1.472	0.6789	-0.5646	0.8821	-0.112	1.3386	0.0231	-0.0458	-0.1031	-0.0997	-0.0205	-0.1579	-0.1078	0.1471	-0.0197	0.2158	0.0218	0.018	0.1707	-0.0203	0.1214	0.0318	-14.725	21.9952
2	0.9735	0.4855	0.6387	1.6041	-0.6443	2.9038	-0.1168	0.0186	0.0201	-0.4877	0.1002	0.1546	0.0686	-0.1955	0.0011	0.245	0.012	-0.032	0.1709	-0.0379	0.1006	-18.0007	-30.5686	16.5614
3	0.9312	0.9545	0.6795	2.7339	0.5641	0.9192	0.1409	-0.0577	0.0558	-0.7519	-0.2714	0.1789	-0.197	-0.163	0.0609	0.0791	0.0314	-0.0052	0.1402	-0.0381	0.0442	-14.0662	-23.5515	29.8256
4	3.4466	0.5459	-1.2038	2.1642	-0.5715	2.4444	0.311	-0.3845	-0.1266	0.1379	-0.4632	0.9795	-0.329	-0.7962	-0.2144	0.1028	0.1427	0.1199	0.3068	-0.2199	0.2653	-17.0706	-2.412	44.275
5	0.9345	0.6282	-0.2695	1.9373	-0.6416	1.7328	-0.03	-0.0597	-0.1486	-0.0388	0.1111	0.0823	0.0315	-0.1056	-0.0848	0.0643	-0.0089	0.0095	0.1668	-0.0305	0.1108	-16.1122	-30.3894	51.0942
6	1.0531	0.0388	-0.2675	1.2008	0.1775	0.7527	0.0643	-0.1635	0.0207	0.1464	-0.0289	0.2531	-0.0667	-0.1397	-0.0245	0.0915	0.006	0.032	0.1972	-0.0162	0.1191	-20.4009	-24.2265	57.7565
7	1.2748	-0.5787	-0.2822	2.5155	0.454	2.6065	0.1227	-0.3766	0.1504	0.2705	0.0668	-0.0567	-0.1409	0.1381	-0.1013	0.0714	-0.0446	-0.0047	0.2259	-0.0472	0.0819	-5.3003	-20.9151	59.4555
8	0.9625	-0.1598	0.29	1.536	-0.5226	1.2639	0.0234	-0.1061	0.0185	0.0073	-0.0167	-0.178	-0.0638	0.1136	-0.0043	0.0616	-0.0188	0.0264	0.1446	-0.021	0.0966	-2.438	-19.6983	51.8622
9	0.5717	0.4724	0.0718	1.5983	-0.0005	0.5644	-0.0194	0.0222	-0.0116	-0.2132	0.0093	-0.1387	-0.0237	-0.0898	-0.0104	0.1216	0.0123	0.0189	0.1789	-0.0275	0.084	-8.1572	-22.1011	35.7895
10	3.2692	0.6602	-0.6928	2.5481	-0.0192	2.7934	0.0628	-0.0728	0.167	-0.0078	-0.0906	-0.211	-0.3161	0.0728	0.034	0.1583	-0.0252	0.0257	0.09	-0.0156	0.1104	5.3219	-1.0647	40.2178
11	2.2674	0.4433	0.7821	1.1764	0.263	0.9827	-0.072	0.0488	0.1085	-0.2035	0.0445	-0.0825	-0.2175	0.0039	0.033	0.1958	0.0108	0.05	0.0869	-0.0257	0.0984	0.2355	-6.5947	27.2152
12	3.6846	2.3466	0.2481	4.3646	-0.2815	1.5132	-0.2291	0.2476	0.6183	-0.7987	0.2196	0.6313	-0.1258	-0.1513	0.049	0.3762	0.0846	-0.11	0.2809	0.0154	0.2466	-19.8216	-7.424	11.4901
13	9.9872	-3.1811	-4.1626	2.9548	2.5467	3.0706	0.2284	-0.0147	0.3388	-0.1344	-0.037	-0.1154	-0.3601	0.0889	-0.2509	0.2937	-0.0338	0.0224	0.1775	0.0201	0.1553	4.5543	-3.6787	12.3998
14	3.3349	1.7767	1.1395	1.9676	-1.6873	6.0124	-0.1913	-0.1808	0.1229	-0.3445	0.0103	-0.2779	-0.1898	0.3548	0.1827	0.301	-0.0482	0.0943	0.1943	-0.0264	0.204	12.3013	-5.2223	0.0117
15	6.5854	-0.4378	-0.0986	4.427	0.8125	3.8787	-0.0244	-0.245	0.4348	-0.6919	-0.0493	0.1125	-0.6579	0.1018	0.0694	0.3306	0.0146	0.0015	0.156	-0.0122	0.2084	8.6749	2.3377	-1.6547
16	1.6961	0.3205	-0.7116	0.8375	0.0217	1.9326	0.0068	0.4207	0.1575	-0.3137	0.0007	-0.0488	-0.0456	-0.0368	0.0558	0.2731	0.0089	0.0462	0.2018	0.0223	0.102	-1.0915	-14.6874	2.2113
17	1.5247	-0.0587	-0.7065	0.4745	0.6919	3.0386	0.0494	0.2636	-0.108	-0.2369	0.0121	-0.1198	0.1388	-0.1115	-0.0432	0.3366	-0.0146	0.0703	0.189	-0.0189	0.1381	2.7958	-20.6079	0.191

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 (resseq 1:34)	A	1 - 34
2	X-RAY DIFFRACTION	2	chain 'A' and (resseq 35:77)	A	35 - 77
3	X-RAY DIFFRACTION	3	chain 'A' and (resseq 78:138)	A	78 - 138
4	X-RAY DIFFRACTION	4	chain 'A' and (resseq 139:168)	A	139 - 168
5	X-RAY DIFFRACTION	5	chain 'A' and (resseq 169:221)	A	169 - 221
6	X-RAY DIFFRACTION	6	chain 'A' and (resseq 222:274)	A	222 - 274
7	X-RAY DIFFRACTION	7	chain 'A' and (resseq 275:312)	A	275 - 312
8	X-RAY DIFFRACTION	8	chain 'A' and (resseq 313:368)	A	313 - 368
9	X-RAY DIFFRACTION	9	chain 'B' and (resseq -7:34)	B	-7 - 34
10	X-RAY DIFFRACTION	10	chain 'B' and (resseq 35:77)	B	35 - 77
11	X-RAY DIFFRACTION	11	chain 'B' and (resseq 78:138)	B	78 - 138
12	X-RAY DIFFRACTION	12	chain 'B' and (resseq 139:168)	B	139 - 168
13	X-RAY DIFFRACTION	13	chain 'B' and (resseq 169:193)	B	169 - 193
14	X-RAY DIFFRACTION	14	chain 'B' and (resseq 194:221)	B	194 - 221
15	X-RAY DIFFRACTION	15	chain 'B' and (resseq 222:250)	B	222 - 250
16	X-RAY DIFFRACTION	16	chain 'B' and (resseq 251:329)	B	251 - 329
17	X-RAY DIFFRACTION	17	chain 'B' and (resseq 330:368)	B	330 - 368

-
News

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

New format data for meta-information of EMDB entries

Version 3 of the EMDB header file is now the official format.
The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
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

Thousand views of thousand structures

Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and 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

-
Protein , 1 types, 2 molecules AB

-
Non-polymers , 5 types, 456 molecules

-
Experimental details

-
Experiment

-
Sample preparation

-
Data collection

-
Phasing

-
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

-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

-Protein , 1 types, 2 molecules AB

-Non-polymers , 5 types, 456 molecules

-Experimental details

-Experiment

-Sample preparation

-Data collection

-Phasing

-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

-
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

-
Protein , 1 types, 2 molecules AB

-
Non-polymers , 5 types, 456 molecules

-
Experimental details

-
Experiment

-
Sample preparation

-
Data collection

-
Phasing

-
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