PDB-4oav: Complete human RNase L in complex with 2-5A (5'-ppp heptamer), AM...

ID or keywords:

Entry

Database: PDB / ID: 4oav

Title

Complete human RNase L in complex with 2-5A (5'-ppp heptamer), AMPPCP and RNA substrate.

Components

PROTEIN (RNase L)
RNA (5'-R(P*(PO4)P*(PO4)P*AP*AP*AP*AP*(PO4))-2')

Keywords

HYDROLASE/RNA / HPC1 / 2-5A / 2' / 5'-oligoadenylate /

interferon /

dsRNA /

kinase /

RNase / RIDD /

Ire1 / RNA decay /

RNase L protein kinase /

pseudokinase / KEN-domain containing / Regulated RNA decay /

innate immune response / antiviral response / dsRNA response / 5'-linked oligoadenylates /

RNA / HYDROLASE-RNA complex

Function / homology

Function and homology information

OAS antiviral response /

Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / negative regulation of viral genome replication / fat cell differentiation / RNA nuclease activity /

RNA processing / ribonucleoprotein complex binding / RNA endonuclease activity / regulation of mRNA stability / positive regulation of glucose import ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.1 Å

Authors

Han, Y. / Donovan, J. / Rath, S. / Whitney, G. / Chitrakar, A. / Korennykh, A.

Citation

Journal: Science / Year: 2014
Title: Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response.
Authors: Han, Y. / Donovan, J. / Rath, S. / Whitney, G. / Chitrakar, A. / Korennykh, A.

History

Deposition	Jan 6, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 12, 2014	Provider: repository / Type: Initial release
Revision 1.1	Apr 2, 2014	Group: Database references
Revision 1.2	Sep 20, 2023	Group: Advisory / Data collection ...Advisory / 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 / pdbx_struct_conn_angle / pdbx_validate_polymer_linkage / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_sheet / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_sheet.number_strands / _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	4oav.cif.gz	592.2 KB	Display	PDBx/mmCIF format
PDB format	pdb4oav.ent.gz	483.6 KB	Display	PDB format
PDBx/mmJSON format	4oav.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

-
Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/oa/4oav ftp://data.pdbj.org/pub/pdb/validation_reports/oa/4oav	HTTPS FTP

-
Related structure data

Related structure data	4oauC 4g8lS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	4oau-1 4o1p-2 6m13-d 6m11-d 4o1p-1 6m12-d 4o1o-2 4o1o-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

-
Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#128 - Aug 2010 Interferons similarity (1) #250 - Oct 2020 Capsaicin Receptor TRPV1 similarity (1) #118 - Oct 2009 Sodium-Potassium Pump similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #195 - Mar 2016 RAF Protein Kinases similarity (1) #223 - Jul 2018 Piezo1 Mechanosensitive Channel similarity (1)

Deposited unit

B: PROTEIN (RNase L)

A: RNA (5'-R(P*(PO4)P*(PO4)P*AP*AP*AP*AP*(PO4))-2')

D: PROTEIN (RNase L)

C: RNA (5'-R(P*(PO4)P*(PO4)P*AP*AP*AP*AP*(PO4))-2')

hetero molecules

163 kDa, 4 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)	58.610, 160.700, 230.800
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

-
Protein / RNA chain , 2 types, 4 molecules BDAC

#1: Protein	PROTEIN (RNase L) Mass: 79416.344 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q05823
#2: RNA chain	RNA (5'-R(P(PO4)P(PO4)PAPAPAPAP(PO4))-2') Mass: 1502.733 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details*: Chemical synthesis

-
Non-polymers , 4 types, 918 molecules

#3: Chemical	ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE Mass: 505.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₁H₁₈N₅O₁₂P₃ / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#4: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical	ChemComp-PUP / (2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-hydroxy-2-({[(S)-hydroxy{[(2R,3S,4S)-4-hydroxy-2-(hydroxymethyl)tetrahydrofuran-3-yl]oxy}phosphoryl]oxy}methyl)tetrahydrofuran-3-yl dihydrogen phosphate Mass: 520.276 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₁₄H₂₂N₂O₁₅P₂
#6: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 911 / 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: 3.41 Å³/Da / Density % sol: 63.95 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion / pH: 6.5 Details: RNase L (21-719) (15 mg/ml in buffer containing 20 mM HEPES pH 7.5, 109 mM NaCl, 5 mM MgCl2, 5 mM DTT, 2.8 mM ATP or AMP-PCP, and 10% glycerol) was mixed with 2-5A and RNA18 at molar ratio 1: ...Details: RNase L (21-719) (15 mg/ml in buffer containing 20 mM HEPES pH 7.5, 109 mM NaCl, 5 mM MgCl2, 5 mM DTT, 2.8 mM ATP or AMP-PCP, and 10% glycerol) was mixed with 2-5A and RNA18 at molar ratio 1:1.5:1, VAPOR DIFFUSION, temperature 277K

Crystal

Density Matthews: 3.41 Å³/Da / Density % sol: 63.95 %

Crystal grow

Temperature: 277 K / Method: vapor diffusion / pH: 6.5
Details: RNase L (21-719) (15 mg/ml in buffer containing 20 mM HEPES pH 7.5, 109 mM NaCl, 5 mM MgCl2, 5 mM DTT, 2.8 mM ATP or AMP-PCP, and 10% glycerol) was mixed with 2-5A and RNA18 at molar ratio 1: ...

-
Data collection

Diffraction	Mean temperature: 77 K
Diffraction source	Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å
Detector	Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 1, 2013
Radiation	Monochromator: Si 111 CHANNEL11 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.075 Å / Relative weight: 1
Reflection	Resolution: 2.1→46.7 Å / Num. all: 128179 / Num. obs: 128124 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0

-
Processing

Software

Name	Version	Classification
CBASS		data collection
PHENIX		model building
PHENIX	(phenix.refine: 1.8_1069)	refinement
XDS		data reduction
XDS		data scaling
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4G8L

4g8l

Resolution: 2.1→46.622 Å / SU ML: 0.24 / σ(F): 1.36 / Phase error: 24.64 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2287	6405	5 %	RANDOM
R_work	0.198	-	-	-
obs	0.1995	128099	99.95 %	-
all	-	128124	-	-

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.1→46.622 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10751	202	99	911	11963

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.004	11270
X-RAY DIFFRACTION	f_angle_d	0.922	15244
X-RAY DIFFRACTION	f_dihedral_angle_d	20.844	6924
X-RAY DIFFRACTION	f_chiral_restr	0.072	1677
X-RAY DIFFRACTION	f_plane_restr	0.003	1913

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 (%)
2.1-2.1239	0.3167	208	0.285	3945	X-RAY DIFFRACTION	100
2.1239-2.1489	0.3021	213	0.277	4042	X-RAY DIFFRACTION	100
2.1489-2.1751	0.3163	211	0.2668	4037	X-RAY DIFFRACTION	100
2.1751-2.2026	0.3233	208	0.2656	3935	X-RAY DIFFRACTION	100
2.2026-2.2316	0.3062	213	0.2551	4047	X-RAY DIFFRACTION	100
2.2316-2.2621	0.2983	213	0.2485	4046	X-RAY DIFFRACTION	100
2.2621-2.2945	0.2963	208	0.244	3949	X-RAY DIFFRACTION	100
2.2945-2.3287	0.2928	212	0.2334	4034	X-RAY DIFFRACTION	100
2.3287-2.3651	0.2847	212	0.2422	4028	X-RAY DIFFRACTION	100
2.3651-2.4039	0.2802	211	0.2378	4016	X-RAY DIFFRACTION	100
2.4039-2.4453	0.2865	212	0.2304	4036	X-RAY DIFFRACTION	100
2.4453-2.4898	0.2952	210	0.2219	4003	X-RAY DIFFRACTION	100
2.4898-2.5377	0.2568	214	0.2239	4049	X-RAY DIFFRACTION	100
2.5377-2.5895	0.2615	211	0.2202	4020	X-RAY DIFFRACTION	100
2.5895-2.6458	0.2831	212	0.2137	4021	X-RAY DIFFRACTION	100
2.6458-2.7073	0.2258	212	0.2143	4025	X-RAY DIFFRACTION	100
2.7073-2.775	0.257	213	0.2139	4045	X-RAY DIFFRACTION	100
2.775-2.85	0.2576	211	0.2154	4024	X-RAY DIFFRACTION	100
2.85-2.9339	0.2783	216	0.2098	4091	X-RAY DIFFRACTION	100
2.9339-3.0285	0.2553	210	0.2065	4006	X-RAY DIFFRACTION	100
3.0285-3.1368	0.2482	214	0.2074	4060	X-RAY DIFFRACTION	100
3.1368-3.2623	0.2173	216	0.2051	4101	X-RAY DIFFRACTION	100
3.2623-3.4108	0.2339	213	0.1974	4038	X-RAY DIFFRACTION	100
3.4108-3.5905	0.1938	214	0.1838	4076	X-RAY DIFFRACTION	100
3.5905-3.8154	0.22	215	0.179	4089	X-RAY DIFFRACTION	100
3.8154-4.1098	0.1901	216	0.1667	4101	X-RAY DIFFRACTION	100
4.1098-4.5231	0.171	218	0.159	4146	X-RAY DIFFRACTION	100
4.5231-5.1768	0.1647	217	0.1572	4124	X-RAY DIFFRACTION	100
5.1768-6.5194	0.222	222	0.1919	4200	X-RAY DIFFRACTION	100
6.5194-46.6334	0.193	230	0.1795	4360	X-RAY DIFFRACTION	99

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	0.6028	0.8611	0.0414	3.5428	-0.3807	0.4215	-0.0289	-0.061	-0.0636	-0.0147	0.0863	0.0097	0.0304	0.0136	-0.0518	0.312	0.0432	0.033	0.3882	-0.0013	0.3249	13.7076	-15.3912	107.7443
2	4.4469	0.9971	1.6002	2.771	0.6983	3.0227	-0.0473	0.0927	-0.0024	-0.1812	0.1201	-0.0492	-0.0036	0.0369	-0.071	0.4404	-0.0663	-0.0018	0.3465	-0.0161	0.2545	12.6427	11.9779	82.3975
3	2.6427	0.3638	1.0175	1.9443	-0.2662	6.8643	-0.0677	0.3197	-0.0116	-0.2103	0.0909	0.0373	-0.1989	-0.3621	-0.0184	0.5571	-0.0869	-0.0338	0.5361	-0.0108	0.3302	0.2438	12.6849	60.0183
4	3.5898	-0.7616	-0.9733	3.0221	0.0659	6.7573	0.1404	-0.0528	-0.0525	-0.059	-0.1885	-0.0311	-0.0845	-0.1645	0.0276	0.5925	-0.1224	-0.0496	0.5813	0.0341	0.3332	5.6871	8.6889	28.5636
5	0.7005	0.8144	0.1696	2.3519	0.3471	0.3027	-0.0653	-0.0899	0.0798	-0.0338	0.037	0.2134	-0.0027	-0.0485	0.0265	0.2899	0.0243	-0.0221	0.3556	-0.034	0.3111	8.5128	15.3748	107.172
6	4.1373	0.4143	-1.6277	2.7522	-1.1078	3.1384	-0.0368	0.0804	-0.0942	-0.0304	0.1671	0.1632	-0.0859	-0.1928	-0.1227	0.4674	-0.0809	0.0045	0.3717	-0.0254	0.2883	11.5027	-12.4956	82.5443
7	3.6831	0.0325	-1.7812	2.0537	0.0268	7.1815	0.0108	0.2434	-0.0347	-0.165	0.0291	-0.0785	0.1792	0.3085	-0.0075	0.4993	-0.0766	0.018	0.4342	-0.0295	0.3101	26.5704	-13.2543	61.88
8	3.3502	-0.5285	0.6378	3.8942	0.3491	7.7383	0.0275	0.3432	-0.0897	-0.4595	-0.0722	0.0159	0.3068	0.146	0.0414	0.6183	-0.0464	0.0447	0.6951	0.008	0.3207	26.5898	-9.1532	29.9256

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	( CHAIN C AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN D AND RESID 26:327 )	C	1 - 6
2	X-RAY DIFFRACTION	1	( CHAIN C AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN D AND RESID 26:327 )	C	7
3	X-RAY DIFFRACTION	1	( CHAIN C AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN D AND RESID 26:327 )	D	26 - 327
4	X-RAY DIFFRACTION	2	( CHAIN D AND RESID 336:436 )	D	336 - 436
5	X-RAY DIFFRACTION	3	( CHAIN D AND ( RESID 437:586 OR RESID 1001:1003 ) )	D	437 - 586
6	X-RAY DIFFRACTION	3	( CHAIN D AND ( RESID 437:586 OR RESID 1001:1003 ) )	D	1001 - 1003
7	X-RAY DIFFRACTION	4	( CHAIN D AND ( RESID 587:719 OR RESID 1004:1004 ) )	D	587 - 719
8	X-RAY DIFFRACTION	4	( CHAIN D AND ( RESID 587:719 OR RESID 1004:1004 ) )	D	1004
9	X-RAY DIFFRACTION	5	( CHAIN A AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN B AND RESID 24:327 )	A	1 - 6
10	X-RAY DIFFRACTION	5	( CHAIN A AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN B AND RESID 24:327 )	A	7
11	X-RAY DIFFRACTION	5	( CHAIN A AND ( RESID 1:6 OR RESID 7:7 ) ) OR ( CHAIN B AND RESID 24:327 )	B	24 - 327
12	X-RAY DIFFRACTION	6	( CHAIN B AND RESID 336:436 )	B	336 - 436
13	X-RAY DIFFRACTION	7	( CHAIN B AND ( RESID 437:586 OR RESID 801:803 ) )	B	437 - 586
14	X-RAY DIFFRACTION	7	( CHAIN B AND ( RESID 437:586 OR RESID 801:803 ) )	B	801 - 803
15	X-RAY DIFFRACTION	8	( CHAIN B AND ( RESID 587:717 OR RESID 1012:1014 ) )	B	587 - 717
16	X-RAY DIFFRACTION	8	( CHAIN B AND ( RESID 587:717 OR RESID 1012:1014 ) )	B	1012 - 1014

-
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 / RNA chain , 2 types, 4 molecules BDAC

-
Non-polymers , 4 types, 918 molecules

-
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 / RNA chain , 2 types, 4 molecules BDAC

-Non-polymers , 4 types, 918 molecules

-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 / RNA chain , 2 types, 4 molecules BDAC

-
Non-polymers , 4 types, 918 molecules

-
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