PDB-9s88: Amuc0121_S1_15 in complex with O6 sulfated Lewis A antigen (6'S-LeA)

ID or keywords:

Entry

Database: PDB / ID: 9s88

Title

Amuc0121_S1_15 in complex with O6 sulfated Lewis A antigen (6'S-LeA)

Components

Sulfatase

Keywords

HYDROLASE / Carbohydrate sulfatase / mucin / Akkermansia muciniphila / Sulfation

Function / homology

Function and homology information

hydrolase activity
Similarity search - Function

Biological species

Akkermansia muciniphila ATCC BAA-835 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.92 Å

Authors

Dey, D. / Cartmell, A.

Funding support

United Kingdom, 1items

Citation

Journal: To Be Published
Title: The role of Akkermansia muciniphila sulfatases in colonic mucin utilisation
Authors: Dey, D. / Salman, N.D. / Tomlinson, C.W.E. / Gugel, S. / Chunsheng, J. / Raba, G. / Nilsson, M. / McIver, Z. / Simpkin, A. / Davy, M. / Rigden, D.J. / Czjzek, M. / Byrne, D.P. / Case, A. / ...

History

Deposition	Aug 5, 2025	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 3, 2026	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

-
Download

PDBx/mmCIF format	9s88.cif.gz	496 KB	Display	PDBx/mmCIF format
PDB format	pdb9s88.ent.gz	395.5 KB	Display	PDB format
PDBx/mmJSON format	9s88.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

-
Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/s8/9s88 ftp://data.pdbj.org/pub/pdb/validation_reports/s8/9s88	HTTPS FTP

-
Related structure data

Related structure data	9s7xC 9s85C 9s8aC 9s8fC 9s8xC 9s8yC 9sf6C C: citing same article (ref.)
Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

-
Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (1) #261 - Sep 2021 DNA-Sequencing Nanopores similarity (1) #22 - Oct 2001 Photosystem I similarity (1) #262 - Oct 2021 Fifty Years of Open Access to PDB Structures similarity (1) #29 - May 2002 Penicillin-binding Proteins similarity (1) #95 - Nov 2007 Multidrug Resistance Transporters similarity (1) #122 - Feb 2010 Enhanceosome similarity (1) #220 - Apr 2018 Dehalogenases similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#50 - Feb 2004
Glycolytic Enzymes
similarity (1)
#261 - Sep 2021
DNA-Sequencing Nanopores
similarity (1)
#22 - Oct 2001
Photosystem I
similarity (1)
#262 - Oct 2021
Fifty Years of Open Access to PDB Structures
similarity (1)
#29 - May 2002
Penicillin-binding Proteins
similarity (1)
#95 - Nov 2007
Multidrug Resistance Transporters
similarity (1)
#122 - Feb 2010
Enhanceosome
similarity (1)
#220 - Apr 2018
Dehalogenases
similarity (1)

Deposited unit

A: Sulfatase

B: Sulfatase

C: Sulfatase

D: Sulfatase

E: Sulfatase

hetero molecules

276 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Sulfatase

hetero molecules

defined by author
Evidence: light scattering
55.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Sulfatase

hetero molecules

defined by author
55.1 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Sulfatase

hetero molecules

defined by author
55.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Sulfatase

hetero molecules

defined by author
55.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: Sulfatase

hetero molecules

defined by author
55.4 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	135.04, 64.15, 151.36
Angle α, β, γ (deg.)	90, 104.88, 90
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
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	VAL	VAL	ARG	ARG	A	A	26 - 511	2 - 487
2	1	1	VAL	VAL	ARG	ARG	B	B	26 - 511	2 - 487
3	2	2	VAL	VAL	ARG	ARG	A	A	26 - 511	2 - 487
4	2	2	VAL	VAL	ARG	ARG	C	C	26 - 511	2 - 487
5	3	3	VAL	VAL	ARG	ARG	A	A	26 - 511	2 - 487
6	3	3	VAL	VAL	ARG	ARG	D	D	26 - 511	2 - 487
7	4	4	THR	THR	ARG	ARG	A	A	25 - 511	1 - 487
8	4	4	THR	THR	ARG	ARG	E	E	25 - 511	1 - 487
9	5	5	VAL	VAL	ARG	ARG	B	B	26 - 511	2 - 487
10	5	5	VAL	VAL	ARG	ARG	C	C	26 - 511	2 - 487
11	6	6	VAL	VAL	ARG	ARG	B	B	26 - 511	2 - 487
12	6	6	VAL	VAL	ARG	ARG	D	D	26 - 511	2 - 487
13	7	7	VAL	VAL	ARG	ARG	B	B	26 - 511	2 - 487
14	7	7	VAL	VAL	ARG	ARG	E	E	26 - 511	2 - 487
15	8	8	VAL	VAL	SER	SER	C	C	26 - 512	2 - 488
16	8	8	VAL	VAL	SER	SER	D	D	26 - 512	2 - 488
17	9	9	VAL	VAL	SER	SER	C	C	26 - 512	2 - 488
18	9	9	VAL	VAL	SER	SER	E	E	26 - 512	2 - 488
19	10	10	VAL	VAL	SER	SER	D	D	26 - 512	2 - 488
20	10	10	VAL	VAL	SER	SER	E	E	26 - 512	2 - 488

NCS ensembles :

ID	Details (eV)
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
7	Local NCS retraints between domains: 13 14
8	Local NCS retraints between domains: 15 16
9	Local NCS retraints between domains: 17 18
10	Local NCS retraints between domains: 19 20

-
Protein / Sugars , 2 types, 10 molecules ABCDE

#1: Protein

Sulfatase

Mass: 54466.852 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Akkermansia muciniphila ATCC BAA-835 (bacteria)
Gene: Amuc_0121 / Production host:

Escherichia coli (E. coli) / References: UniProt: B2ULS2

#2: Polysaccharide

6-O-sulfo-beta-D-galactopyranose-(1-3)-[alpha-L-fucopyranose-(1-4)]2-acetamido-2-deoxy-alpha-D-glucopyranose

Type: oligosaccharide / Mass: 609.553 Da / Num. of mol.: 5 / Source method: obtained synthetically

Descriptor	Type	Program
DGalp[6S]b1-3[LFucpa1-4]DGlcpNAca1-ROH	Glycam Condensed Sequence	GMML 1.0
WURCS=2.0/3,3,2/[a2122h-1a_1-5_2NCC/3=O][a2112h-1b_1-5_6OSO/3=O/3=O][a1221m-1a_1-5]/1-2-3/a3-b1_a4-c1	WURCS	PDB2Glycan 1.1.0
[][a-D-GlcpNAc]{[(3+1)][b-D-Galp6SO3]{}[(4+1)][a-L-Fucp]{}}	LINUCS	PDB-CARE

-
Non-polymers , 4 types, 376 molecules

#3: Chemical	ChemComp-IOD / IODIDE ION Mass: 126.904 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: I
#4: Chemical	ChemComp-BR / BROMIDE ION Mass: 79.904 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Br
#5: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Ca
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 363 / Source method: isolated from a natural source / Formula: H₂O

-
Details

Has ligand of interest	Y
Has protein modification	N

-
Experiment

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

-
Sample preparation

Crystal	Density Matthews: 2.36 Å³/Da / Density % sol: 47.85 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Morpheus B1: 30 % Precipitant mix 1 (40% v/v PEG 500 MME; 20 % w/v PEG 20000) 0.1 M Buffer system 1 pH 6.5 (Imidazole; MES monohydrate acid) 0.09 M Halogens (0.3M Sodium fluoride; 0.3M ...Details: Morpheus B1: 30 % Precipitant mix 1 (40% v/v PEG 500 MME; 20 % w/v PEG 20000) 0.1 M Buffer system 1 pH 6.5 (Imidazole; MES monohydrate acid) 0.09 M Halogens (0.3M Sodium fluoride; 0.3M Sodium bromide; 0.3M Sodium iodide) 36 mgml Amuc0121_C78S ,Co-crystallised with 1 mM 6S-LeA and soaked with ~5 mM ~72h

Crystal

Density Matthews: 2.36 Å³/Da / Density % sol: 47.85 %

Crystal grow

Temperature: 293 K / Method: vapor diffusion, sitting drop
Details: Morpheus B1: 30 % Precipitant mix 1 (40% v/v PEG 500 MME; 20 % w/v PEG 20000) 0.1 M Buffer system 1 pH 6.5 (Imidazole; MES monohydrate acid) 0.09 M Halogens (0.3M Sodium fluoride; 0.3M ...

-
Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97625 Å
Detector	Type: DECTRIS EIGER2 S 16M / Detector: PIXEL / Date: Jul 1, 2025
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97625 Å / Relative weight: 1
Reflection	Resolution: 1.92→58.75 Å / Num. obs: 1313104 / % possible obs: 99.4 % / Redundancy: 6.8 % / CC_1/2: 0.991 / Net I/σ(I): 9.3
Reflection shell	Resolution: 1.92→1.95 Å / Num. unique obs: 56063 / CC_1/2: 0.421

-
Processing

Software

Name	Version	Classification
REFMAC	5.8.0430 (refmacat 0.4.105)	refinement
xia2		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.92→57.856 Å / Cor.coef. F_o:F_c: 0.957 / Cor.coef. F_o:F_c free: 0.945 / SU B: 5.616 / SU ML: 0.148 / Cross valid method: FREE R-VALUE / ESU R: 0.177 / ESU R Free: 0.151
Details: Hydrogens have been added in their riding positions

	R_factor	Num. reflection	% reflection
R_free	0.236	9703	5.056 %
R_work	0.2076	182211	-
all	0.209	-	-
obs	-	191914	99.367 %

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: 39.568 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.339 Å²	-0 Å²	0.88 Å²
2-	-	0.332 Å²	-0 Å²
3-	-	-	-2.75 Å²

Refinement step

Cycle: LAST / Resolution: 1.92→57.856 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	18886	0	213	363	19462

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.012	19767
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.016	18816
X-RAY DIFFRACTION	r_angle_refined_deg	1.558	1.828	26750
X-RAY DIFFRACTION	r_angle_other_deg	0.538	1.785	43620
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.479	5	2484
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	9.55	5	134
X-RAY DIFFRACTION	r_dihedral_angle_other_2_deg	2.211	5	10
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.671	10	3430
X-RAY DIFFRACTION	r_dihedral_angle_6_deg	15.214	10	848
X-RAY DIFFRACTION	r_chiral_restr	0.072	0.2	2869
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	23241
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	4325
X-RAY DIFFRACTION	r_nbd_refined	0.219	0.2	3645
X-RAY DIFFRACTION	r_symmetry_nbd_other	0.201	0.2	16810
X-RAY DIFFRACTION	r_nbtor_refined	0.174	0.2	9549
X-RAY DIFFRACTION	r_symmetry_nbtor_other	0.081	0.2	9990
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.134	0.2	631
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_other	0.071	0.2	2
X-RAY DIFFRACTION	r_metal_ion_refined	0.126	0.2	17
X-RAY DIFFRACTION	r_symmetry_nbd_refined	0.333	0.2	32
X-RAY DIFFRACTION	r_nbd_other	0.242	0.2	99
X-RAY DIFFRACTION	r_symmetry_xyhbond_nbd_refined	0.201	0.2	20
X-RAY DIFFRACTION	r_mcbond_it	3.083	3.729	9888
X-RAY DIFFRACTION	r_mcbond_other	3.083	3.73	9889
X-RAY DIFFRACTION	r_mcangle_it	4.115	6.692	12388
X-RAY DIFFRACTION	r_mcangle_other	4.115	6.693	12389
X-RAY DIFFRACTION	r_scbond_it	3.886	4.091	9879
X-RAY DIFFRACTION	r_scbond_other	3.885	4.091	9880
X-RAY DIFFRACTION	r_scangle_it	5.778	7.327	14362
X-RAY DIFFRACTION	r_scangle_other	5.778	7.327	14363
X-RAY DIFFRACTION	r_lrange_it	6.859	35.646	21312
X-RAY DIFFRACTION	r_lrange_other	6.859	35.611	21274
X-RAY DIFFRACTION	r_ncsr_local_group_1	0.059	0.05	16620
X-RAY DIFFRACTION	r_ncsr_local_group_2	0.063	0.05	16586
X-RAY DIFFRACTION	r_ncsr_local_group_3	0.061	0.05	16578
X-RAY DIFFRACTION	r_ncsr_local_group_4	0.052	0.05	16703
X-RAY DIFFRACTION	r_ncsr_local_group_5	0.057	0.05	16327
X-RAY DIFFRACTION	r_ncsr_local_group_6	0.059	0.05	16259
X-RAY DIFFRACTION	r_ncsr_local_group_7	0.059	0.05	16233
X-RAY DIFFRACTION	r_ncsr_local_group_8	0.052	0.05	16406
X-RAY DIFFRACTION	r_ncsr_local_group_9	0.064	0.05	16341
X-RAY DIFFRACTION	r_ncsr_local_group_10	0.061	0.05	16351

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	0.05864	0.0501
1	2	B	X-RAY DIFFRACTION	Local ncs	0.05864	0.0501
2	3	A	X-RAY DIFFRACTION	Local ncs	0.06308	0.0501
2	4	C	X-RAY DIFFRACTION	Local ncs	0.06308	0.0501
3	5	A	X-RAY DIFFRACTION	Local ncs	0.06125	0.0501
3	6	D	X-RAY DIFFRACTION	Local ncs	0.06125	0.0501
4	7	A	X-RAY DIFFRACTION	Local ncs	0.05246	0.0501
4	8	E	X-RAY DIFFRACTION	Local ncs	0.05246	0.0501
5	9	B	X-RAY DIFFRACTION	Local ncs	0.05655	0.0501
5	10	C	X-RAY DIFFRACTION	Local ncs	0.05655	0.0501
6	11	B	X-RAY DIFFRACTION	Local ncs	0.05906	0.0501
6	12	D	X-RAY DIFFRACTION	Local ncs	0.05906	0.0501
7	13	B	X-RAY DIFFRACTION	Local ncs	0.05907	0.0501
7	14	E	X-RAY DIFFRACTION	Local ncs	0.05907	0.0501
8	15	C	X-RAY DIFFRACTION	Local ncs	0.05176	0.0501
8	16	D	X-RAY DIFFRACTION	Local ncs	0.05176	0.0501
9	17	C	X-RAY DIFFRACTION	Local ncs	0.06364	0.0501
9	18	E	X-RAY DIFFRACTION	Local ncs	0.06364	0.0501
10	19	D	X-RAY DIFFRACTION	Local ncs	0.06102	0.0501
10	20	E	X-RAY DIFFRACTION	Local ncs	0.06102	0.0501

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 (%)
1.92-1.965	0.343	700	0.349	12603	X-RAY DIFFRACTION	93.7491
1.965-2.019	0.327	671	0.323	13081	X-RAY DIFFRACTION	99.4144
2.019-2.077	0.319	700	0.304	12726	X-RAY DIFFRACTION	99.5256
2.077-2.141	0.309	669	0.282	12362	X-RAY DIFFRACTION	99.6482
2.141-2.211	0.294	630	0.262	11997	X-RAY DIFFRACTION	99.7315
2.211-2.289	0.279	646	0.237	11605	X-RAY DIFFRACTION	99.8045
2.289-2.375	0.254	613	0.228	11195	X-RAY DIFFRACTION	99.814
2.375-2.472	0.264	599	0.213	10759	X-RAY DIFFRACTION	99.8769
2.472-2.581	0.261	536	0.214	10406	X-RAY DIFFRACTION	99.9726
2.581-2.707	0.257	506	0.211	9951	X-RAY DIFFRACTION	99.9522
2.707-2.853	0.256	519	0.205	9427	X-RAY DIFFRACTION	99.9899
2.853-3.026	0.244	496	0.196	8956	X-RAY DIFFRACTION	99.9788
3.026-3.234	0.221	448	0.204	8428	X-RAY DIFFRACTION	99.9212
3.234-3.492	0.23	411	0.208	7869	X-RAY DIFFRACTION	100
3.492-3.824	0.22	367	0.201	7299	X-RAY DIFFRACTION	99.9739
3.824-4.273	0.198	344	0.17	6592	X-RAY DIFFRACTION	99.9856
4.273-4.93	0.178	288	0.151	5843	X-RAY DIFFRACTION	99.9837
4.93-6.027	0.187	245	0.175	4969	X-RAY DIFFRACTION	99.9425
6.027-8.478	0.178	210	0.159	3879	X-RAY DIFFRACTION	99.9023
8.478-57.856	0.191	105	0.175	2263	X-RAY DIFFRACTION	99.4123

-
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://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 / Sugars , 2 types, 10 molecules ABCDE

-
Non-polymers , 4 types, 376 molecules

-
Details

-
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

-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 / Sugars , 2 types, 10 molecules ABCDE

-Non-polymers , 4 types, 376 molecules

-Details

-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

-
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 / Sugars , 2 types, 10 molecules ABCDE

-
Non-polymers , 4 types, 376 molecules

-
Details

-
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