PDB-3blr: Crystal Structure of Human CDK9/cyclinT1 in complex with Flavopiridol

ID or keywords:

Entry

Database: PDB / ID: 3blr

Title

Crystal Structure of Human CDK9/cyclinT1 in complex with Flavopiridol

Components

Cell division protein kinase 9
Cyclin-T1

Keywords

TRANSCRIPTION / transcriptional CDK-cyclin complex /

phosphorylated / Flavopiridol /

Alternative splicing / ATP-binding /

Kinase / Nucleotide-binding /

Nucleus /

Phosphoprotein / Polymorphism /

Serine/threonine-protein kinase /

Transcription regulation /

Transferase /

Acetylation /

Cell cycle /

Cell division /

Coiled coil / Host-virus interaction

Function / homology

Function and homology information

P-TEFb complex / Interactions of Tat with host cellular proteins / 7SK snRNA binding / cyclin/CDK positive transcription elongation factor complex / regulation of muscle cell differentiation / regulation of mRNA 3'-end processing / positive regulation of protein localization to chromatin / nucleus localization / cyclin-dependent protein serine/threonine kinase activator activity / positive regulation by host of viral transcription ...

P-TEFb complex / Interactions of Tat with host cellular proteins / 7SK snRNA binding / cyclin/CDK positive transcription elongation factor complex / regulation of muscle cell differentiation / regulation of mRNA 3'-end processing / positive regulation of protein localization to chromatin / nucleus localization / cyclin-dependent protein serine/threonine kinase activator activity / positive regulation by host of viral transcription /

RNA polymerase binding / negative regulation of protein localization to chromatin / [RNA-polymerase]-subunit kinase / positive regulation of DNA-templated transcription, elongation / transcription elongation-coupled chromatin remodeling / replication fork processing / cellular response to cytokine stimulus / regulation of cyclin-dependent protein serine/threonine kinase activity / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat /

regulation of DNA repair /

cyclin-dependent kinase / Formation of HIV elongation complex in the absence of HIV Tat / cyclin-dependent protein serine/threonine kinase activity / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / molecular condensate scaffold activity / RNA Polymerase II Pre-transcription Events / RNA polymerase II CTD heptapeptide repeat kinase activity / transcription elongation factor complex / transcription elongation by RNA polymerase II /

transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / TP53 Regulates Transcription of DNA Repair Genes / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription /

transcription coactivator binding / cytoplasmic ribonucleoprotein granule / PML body /

kinase activity / DNA-binding transcription factor binding / cell population proliferation / Estrogen-dependent gene expression / transcription by RNA polymerase II / transcription cis-regulatory region binding /

regulation of cell cycle /

protein kinase activity / response to xenobiotic stimulus /

cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding /

cell division /

protein phosphorylation /

DNA repair / protein serine kinase activity / protein serine/threonine kinase activity /

chromatin binding / regulation of transcription by RNA polymerase II /

protein kinase binding / positive regulation of transcription by RNA polymerase II /

DNA binding /

nucleoplasm /

ATP binding /

membrane /

nucleus /

cytosol
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.8 Å

Authors

Baumli, S. / Lolli, G. / Lowe, E.D. / Johnson, L.N.

Citation

Journal: Embo J. / Year: 2008
Title: The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
Authors: Baumli, S. / Lolli, G. / Lowe, E.D. / Troiani, S. / Rusconi, L. / Bullock, A.N. / Debreczeni, J.E. / Knapp, S. / Johnson, L.N.

History

Deposition	Dec 11, 2007	Deposition site: RCSB / Processing site: PDBJ
Revision 1.0	Jul 1, 2008	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Nov 10, 2021	Group: Database references / Derived calculations Category: database_2 / struct_conn ...database_2 / struct_conn / 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_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3	Nov 1, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	3blr.cif.gz	243.7 KB	Display	PDBx/mmCIF format
PDB format	pdb3blr.ent.gz	197.3 KB	Display	PDB format
PDBx/mmJSON format	3blr.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/bl/3blr ftp://data.pdbj.org/pub/pdb/validation_reports/bl/3blr	HTTPS FTP

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Related structure data

Related structure data	2ivxC 3blhSC 3blqC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	4bch-d 4bcj-d 3blq-d 4bcf-d 4ec9-d 4bci-d 3lq5-d 3my1-d 4bcg-d 3tnh-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

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#236 - Aug 2019 Cyclin and Cyclin-dependent Kinase similarity (6) #240 - Dec 2019 Hypoxia-Inducible Factors similarity (11) #67 - Jul 2005 TATA-Binding Protein similarity (5) #47 - Nov 2003 Simian Virus 40 similarity (3) #112 - Apr 2009 Oct and Sox Transcription Factors similarity (2) #31 - Jul 2002 p53 Tumor Suppressor similarity (1) #60 - Dec 2004 Ubiquitin similarity (1) #122 - Feb 2010 Enhanceosome similarity (1) #213 - Sep 2017 Sirtuins similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (2) #221 - May 2018 Human Papillomavirus and Vaccines similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#236 - Aug 2019
Cyclin and Cyclin-dependent Kinase
similarity (6)
#240 - Dec 2019
Hypoxia-Inducible Factors
similarity (11)
#67 - Jul 2005
TATA-Binding Protein
similarity (5)
#47 - Nov 2003
Simian Virus 40
similarity (3)
#112 - Apr 2009
Oct and Sox Transcription Factors
similarity (2)
#31 - Jul 2002
p53 Tumor Suppressor
similarity (1)
#60 - Dec 2004
Ubiquitin
similarity (1)
#122 - Feb 2010
Enhanceosome
similarity (1)
#213 - Sep 2017
Sirtuins
similarity (1)
#234 - Jun 2019
MDM2 and Cancer
similarity (2)
#221 - May 2018
Human Papillomavirus and Vaccines
similarity (1)

Deposited unit

A: Cell division protein kinase 9

B: Cyclin-T1

hetero molecules

68.9 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)	173.922, 173.922, 97.173
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	146
Space group name H-M	H3

#1: Protein	Cell division protein kinase 9 / / Cyclin-dependent kinase 9 / Serine/threonine-protein kinase PITALRE / C-2K / Cell division cycle 2- ...Cyclin-dependent kinase 9 / Serine/threonine-protein kinase PITALRE / C-2K / Cell division cycle 2-like protein kinase 4 Mass: 38054.082 Da / Num. of mol.: 1 / Fragment: UNP residues 2-330 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CDK9 / Plasmid: pVL1392 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 References: UniProt: P50750, cyclin-dependent kinase, [RNA-polymerase]-subunit kinase
#2: Protein	Cyclin-T1 / CycT1 / Cyclin-T Mass: 30119.426 Da / Num. of mol.: 1 / Fragment: UNP residues 2-259 / Mutation: Q77R, E96G, F241L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCNT1 / Plasmid: pVL1392 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: O60563
#3: Chemical	ChemComp-PO4 / PHOSPHATE ION / Phosphate Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO₄
#4: Chemical	ChemComp-CPB / 2-(2-CHLORO-PHENYL)-5,7-DIHYDROXY-8-(3-HYDROXY-1-METHYL-PIPERIDIN-4-YL)-4H-BENZOPYRAN-4-ONE / FLAVOPIRIDOL / Alvocidib Mass: 401.840 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂₁H₂₀ClNO₅ / Comment: inhibitor, alkaloid*YM
#5: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 20 / 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: 4.15 Å³/Da / Density % sol: 70.35 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.2 Details: 0.1M NaK phosphate, 20% PEG 1000, 0.2M NaCl, 4mM TCEP, 0.1mM Flavopiridol , pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

ESRF

/ Beamline: ID14-4 / Wavelength: 0.9765 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 18, 2007

Radiation

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

Radiation wavelength

Wavelength: 0.9765 Å / Relative weight: 1

Reflection

Resolution: 2.8→38.378 Å / Num. all: 26960 / Num. obs: 26960 / % possible obs: 99.8 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 5.7 % / R_merge(I) obs: 0.093 / R_sym value: 0.093 / Net I/σ(I): 5

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured all	Num. unique all	R_sym value	% possible all
2.8-2.95	5.8	0.585	1.2	22770	3943	0.585	100
2.95-3.13	5.8	0.334	2.1	21584	3732	0.334	100
3.13-3.35	5.8	0.19	3.7	20370	3525	0.19	100
3.35-3.61	5.8	0.124	5.5	18839	3263	0.124	100
3.61-3.96	5.8	0.094	7.1	17189	2981	0.094	100
3.96-4.43	5.7	0.078	8	15803	2751	0.078	100
4.43-5.11	5.7	0.079	7.8	13556	2379	0.079	100
5.11-6.26	5.6	0.097	6.2	11384	2017	0.097	99.8
6.26-8.85	5.4	0.07	7.8	8305	1551	0.07	100
8.85-59.55	5.3	0.064	9.5	4363	818	0.064	95.4

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Processing

Software

Name	Classification
ProDC	data collection
PHASES	phasing
PHENIX	refinement
MOSFLM	data reduction
SCALA	data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3BLH

3blh

Resolution: 2.8→36.96 Å / FOM work R set: 0.84 / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ml

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.228	2699	5.02 %	RANDOM
R_work	0.176	-	-	-
all	-	26960	-	-
obs	-	26956	99.55 %	-

Solvent computation

B_sol: 50.12 Å² / k_sol: 0.306 e/Å³

Displacement parameters

B_iso max: 223.93 Å² / B_iso mean: 89.79 Å² / B_iso min: 39.02 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	1.301 Å²	-0 Å²	-0 Å²
2-	-	1.301 Å²	0 Å²
3-	-	-	-2.602 Å²

Refinement step

Cycle: LAST / Resolution: 2.8→36.96 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4488	0	43	20	4551

Refine LS restraints

Refine-ID	Type	Dev ideal	Weight
X-RAY DIFFRACTION	f_angle_d	0.66	1
X-RAY DIFFRACTION	f_bond_d	0.004	1
X-RAY DIFFRACTION	f_chiral_restr	0.049	1
X-RAY DIFFRACTION	f_dihedral_angle_d	10.303	1
X-RAY DIFFRACTION	f_plane_restr	0.002	1
X-RAY DIFFRACTION	f_nbd_refined	4.075	1

LS refinement shell

Resolution (Å)	R_factor R_work	Num. reflection R_work	Refine-ID	Total num. of bins used	% reflection obs (%)
2.8-2.809	0.243	471	X-RAY DIFFRACTION	102	95
2.809-2.819	0.275	543	X-RAY DIFFRACTION	102	97
2.819-2.828	0.272	510	X-RAY DIFFRACTION	102	92
2.828-2.838	0.258	492	X-RAY DIFFRACTION	102	93
2.838-2.847	0.257	556	X-RAY DIFFRACTION	102	94
2.847-2.857	0.249	444	X-RAY DIFFRACTION	102	93
2.857-2.867	0.254	507	X-RAY DIFFRACTION	102	94
2.867-2.877	0.266	469	X-RAY DIFFRACTION	102	95
2.877-2.888	0.238	530	X-RAY DIFFRACTION	102	97
2.888-2.898	0.245	483	X-RAY DIFFRACTION	102	94
2.898-2.908	0.271	526	X-RAY DIFFRACTION	102	99
2.908-2.919	0.262	519	X-RAY DIFFRACTION	102	96
2.919-2.93	0.261	556	X-RAY DIFFRACTION	102	93
2.93-2.941	0.241	448	X-RAY DIFFRACTION	102	95
2.941-2.952	0.255	459	X-RAY DIFFRACTION	102	94
2.952-2.964	0.239	486	X-RAY DIFFRACTION	102	94
2.964-2.975	0.244	525	X-RAY DIFFRACTION	102	93
2.975-2.987	0.231	540	X-RAY DIFFRACTION	102	96
2.987-2.999	0.232	457	X-RAY DIFFRACTION	102	95
2.999-3.011	0.244	546	X-RAY DIFFRACTION	102	96
3.011-3.024	0.22	480	X-RAY DIFFRACTION	102	95
3.024-3.036	0.244	518	X-RAY DIFFRACTION	102	95
3.036-3.049	0.235	446	X-RAY DIFFRACTION	102	94
3.049-3.062	0.221	507	X-RAY DIFFRACTION	102	95
3.062-3.075	0.218	549	X-RAY DIFFRACTION	102	96
3.075-3.088	0.216	488	X-RAY DIFFRACTION	102	96
3.088-3.102	0.222	506	X-RAY DIFFRACTION	102	93
3.102-3.116	0.221	513	X-RAY DIFFRACTION	102	94
3.116-3.13	0.215	460	X-RAY DIFFRACTION	102	95
3.13-3.145	0.205	574	X-RAY DIFFRACTION	102	95
3.145-3.159	0.2	422	X-RAY DIFFRACTION	102	94
3.159-3.174	0.194	531	X-RAY DIFFRACTION	102	94
3.174-3.19	0.225	462	X-RAY DIFFRACTION	102	95
3.19-3.205	0.218	533	X-RAY DIFFRACTION	102	94
3.205-3.221	0.217	551	X-RAY DIFFRACTION	102	94
3.221-3.237	0.207	428	X-RAY DIFFRACTION	102	95
3.237-3.253	0.206	484	X-RAY DIFFRACTION	102	95
3.253-3.27	0.205	552	X-RAY DIFFRACTION	102	96
3.27-3.288	0.215	507	X-RAY DIFFRACTION	102	96
3.288-3.305	0.196	535	X-RAY DIFFRACTION	102	98
3.305-3.323	0.197	468	X-RAY DIFFRACTION	102	95
3.323-3.342	0.209	539	X-RAY DIFFRACTION	102	96
3.342-3.36	0.194	427	X-RAY DIFFRACTION	102	94
3.36-3.379	0.18	551	X-RAY DIFFRACTION	102	96
3.379-3.399	0.198	498	X-RAY DIFFRACTION	102	94
3.399-3.419	0.185	511	X-RAY DIFFRACTION	102	95
3.419-3.44	0.181	490	X-RAY DIFFRACTION	102	95
3.44-3.461	0.196	501	X-RAY DIFFRACTION	102	95
3.461-3.482	0.181	505	X-RAY DIFFRACTION	102	95
3.482-3.505	0.208	518	X-RAY DIFFRACTION	102	96
3.505-3.527	0.189	493	X-RAY DIFFRACTION	102	93
3.527-3.551	0.185	468	X-RAY DIFFRACTION	102	92
3.551-3.575	0.187	472	X-RAY DIFFRACTION	102	91
3.575-3.599	0.175	516	X-RAY DIFFRACTION	102	93
3.599-3.625	0.196	557	X-RAY DIFFRACTION	102	96
3.625-3.651	0.175	460	X-RAY DIFFRACTION	102	95
3.651-3.677	0.174	509	X-RAY DIFFRACTION	102	95
3.677-3.705	0.173	500	X-RAY DIFFRACTION	102	94
3.705-3.734	0.164	490	X-RAY DIFFRACTION	102	94
3.734-3.763	0.176	509	X-RAY DIFFRACTION	102	94
3.763-3.793	0.173	473	X-RAY DIFFRACTION	102	97
3.793-3.825	0.157	530	X-RAY DIFFRACTION	102	95
3.825-3.857	0.163	516	X-RAY DIFFRACTION	102	96
3.857-3.89	0.167	513	X-RAY DIFFRACTION	102	94
3.89-3.925	0.162	464	X-RAY DIFFRACTION	102	94
3.925-3.961	0.161	498	X-RAY DIFFRACTION	102	97
3.961-3.998	0.15	542	X-RAY DIFFRACTION	102	95
3.998-4.037	0.157	476	X-RAY DIFFRACTION	102	94
4.037-4.077	0.143	505	X-RAY DIFFRACTION	102	93
4.077-4.12	0.136	486	X-RAY DIFFRACTION	102	94
4.12-4.163	0.133	497	X-RAY DIFFRACTION	102	94
4.163-4.209	0.147	534	X-RAY DIFFRACTION	102	95
4.209-4.257	0.132	479	X-RAY DIFFRACTION	102	97
4.257-4.307	0.14	489	X-RAY DIFFRACTION	102	96
4.307-4.359	0.135	492	X-RAY DIFFRACTION	102	95
4.359-4.414	0.124	586	X-RAY DIFFRACTION	102	96
4.414-4.472	0.127	443	X-RAY DIFFRACTION	102	96
4.472-4.533	0.136	518	X-RAY DIFFRACTION	102	94
4.533-4.598	0.137	512	X-RAY DIFFRACTION	102	96
4.598-4.667	0.129	486	X-RAY DIFFRACTION	102	93
4.667-4.739	0.14	486	X-RAY DIFFRACTION	102	93
4.739-4.817	0.117	513	X-RAY DIFFRACTION	102	94
4.817-4.9	0.126	480	X-RAY DIFFRACTION	102	97
4.9-4.989	0.121	534	X-RAY DIFFRACTION	102	95
4.989-5.084	0.126	472	X-RAY DIFFRACTION	102	96
5.084-5.188	0.129	494	X-RAY DIFFRACTION	102	91
5.188-5.3	0.134	516	X-RAY DIFFRACTION	102	95
5.3-5.423	0.149	512	X-RAY DIFFRACTION	102	95
5.423-5.558	0.136	494	X-RAY DIFFRACTION	102	95
5.558-5.708	0.16	518	X-RAY DIFFRACTION	102	97
5.708-5.876	0.159	477	X-RAY DIFFRACTION	102	93
5.876-6.064	0.163	499	X-RAY DIFFRACTION	102	94
6.064-6.28	0.185	499	X-RAY DIFFRACTION	102	94
6.28-6.53	0.182	507	X-RAY DIFFRACTION	102	96
6.53-6.826	0.173	474	X-RAY DIFFRACTION	102	92
6.826-7.183	0.162	491	X-RAY DIFFRACTION	102	95
7.183-7.629	0.16	520	X-RAY DIFFRACTION	102	95
7.629-8.212	0.139	504	X-RAY DIFFRACTION	102	94
8.212-9.028	0.13	502	X-RAY DIFFRACTION	102	96
9.028-10.31	0.116	495	X-RAY DIFFRACTION	102	94
10.31-12.897	0.13	464	X-RAY DIFFRACTION	102	88
12.897-36.96	0.256	461	X-RAY DIFFRACTION	102	86

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	1.1558	-0.0481	0.2308	2.3252	0.1658	1.7915	0.285	0.1592	-0.3481	0.4787	-0.2628	0.085	0.5758	-0.0003	-0.0105	0.4702	-0.0968	-0.0915	0.3886	0.0145	0.551	47.9636	-17.5831	-2.0273
2	2.1264	-0.4559	-0.22	1.0889	0.1026	1.4084	0.1268	0.0799	0.2013	0.1104	-0.071	-0.3659	-0.1029	0.0886	-0.045	0.3344	-0.0381	-0.1093	0.4676	-0.0606	0.4375	21.4353	3.7177	-20.7099

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain A	A	7 - 326
2	X-RAY DIFFRACTION	2	chain B	B	9 - 259

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-Aug 12, 2020. Covid-19 info

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+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

-
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