PDB-9b2b: Estrogen Receptor Alpha Ligand Binding Domain in Complex with a C...

ID or keywords:

Entry

Database: PDB / ID: 9b2b

Title

Estrogen Receptor Alpha Ligand Binding Domain in Complex with a Complete Estrogen Receptor Antagonists that Favors Tetramer Formation

Components

Estrogen receptor

Keywords

TRANSCRIPTION / estrogen receptor / antiestrogen / alpha helical bundle

Function / homology

Function and homology information

regulation of epithelial cell apoptotic process / antral ovarian follicle growth / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / nuclear estrogen receptor activity / epithelial cell development / steroid hormone receptor signaling pathway / epithelial cell proliferation involved in mammary gland duct elongation ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / nuclear estrogen receptor activity / epithelial cell development / steroid hormone receptor signaling pathway / epithelial cell proliferation involved in mammary gland duct elongation / prostate epithelial cord elongation / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / mammary gland branching involved in pregnancy / negative regulation of smooth muscle cell apoptotic process / uterus development / vagina development / TFIIB-class transcription factor binding / androgen metabolic process / mammary gland alveolus development / cellular response to estrogen stimulus / estrogen response element binding / Mitochondrial unfolded protein response (UPRmt) / nuclear receptor-mediated steroid hormone signaling pathway / positive regulation of DNA-binding transcription factor activity / negative regulation of DNA-binding transcription factor activity / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / positive regulation of nitric-oxide synthase activity / estrogen receptor signaling pathway / protein localization to chromatin / steroid binding / 14-3-3 protein binding / negative regulation of canonical NF-kappaB signal transduction / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / negative regulation of miRNA transcription / ESR-mediated signaling / TBP-class protein binding / nitric-oxide synthase regulator activity / nuclear estrogen receptor binding / transcription coregulator binding / transcription corepressor binding / stem cell differentiation / SUMOylation of intracellular receptors / cellular response to estradiol stimulus / euchromatin / beta-catenin binding / Nuclear Receptor transcription pathway / response to estrogen / Regulation of RUNX2 expression and activity / transcription coactivator binding / male gonad development / nuclear receptor activity / Ovarian tumor domain proteases / positive regulation of fibroblast proliferation / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of nitric oxide biosynthetic process / sequence-specific double-stranded DNA binding / response to estradiol / PIP3 activates AKT signaling / positive regulation of cytosolic calcium ion concentration / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / regulation of inflammatory response / DNA-binding transcription activator activity, RNA polymerase II-specific / fibroblast proliferation / phospholipase C-activating G protein-coupled receptor signaling pathway / transcription regulator complex / Estrogen-dependent gene expression / DNA-binding transcription factor activity, RNA polymerase II-specific / calmodulin binding / Extra-nuclear estrogen signaling / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of gene expression / chromatin binding / regulation of transcription by RNA polymerase II / protein kinase binding / regulation of DNA-templated transcription / chromatin / positive regulation of DNA-templated transcription / enzyme binding / negative regulation of transcription by RNA polymerase II / Golgi apparatus / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.08 Å

Authors

Fink, E.C. / Chawla, R. / Wells, K.S. / Barratt, S. / Myles, D.C. / Pena, G. / Robello, B.W. / Ng, R. / Fanning, S.W.

Funding support

United States, 1items

Citation

Journal: To Be Published
Title: Estrogen Receptor Alpha Ligand Binding Domain in Complex with a Complete Estrogen Receptor Antagonists that Favors Tetramer Formation
Authors: Fanning, S.W.

History

Deposition	Mar 14, 2024	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 27, 2025	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

-
Download

PDBx/mmCIF format	9b2b.cif.gz	369.7 KB	Display	PDBx/mmCIF format
PDB format	pdb9b2b.ent.gz		Display	PDB format
PDBx/mmJSON format	9b2b.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

-
Validation report

Summary document	9b2b_validation.pdf.gz	1.4 MB	Display	wwPDB validaton report
Full document	9b2b_full_validation.pdf.gz	1.4 MB	Display
Data in XML	9b2b_validation.xml.gz	47.5 KB	Display
Data in CIF	9b2b_validation.cif.gz	60.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/b2/9b2b ftp://data.pdbj.org/pub/pdb/validation_reports/b2/9b2b	HTTPS FTP

-
Related structure data

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	#45 - Sep 2003 Estrogen Receptor similarity (12) #126 - Jun 2010 Epidermal Growth Factor similarity (1) #267 - Mar 2022 Vascular Endothelial Growth Factor (VegF similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (1) #60 - Dec 2004 Ubiquitin similarity (1)

Deposited unit

A: Estrogen receptor

B: Estrogen receptor

C: Estrogen receptor

D: Estrogen receptor

hetero molecules

118 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Estrogen receptor

hetero molecules

C: Estrogen receptor

hetero molecules

defined by author&software
59.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Estrogen receptor

D: Estrogen receptor

hetero molecules

defined by author&software
59.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	102.097, 57.419, 174.803
Angle α, β, γ (deg.)	90.00, 102.16, 90.00
Int Tables number	5
Space group name H-M	C121

#1: Protein	Estrogen receptor / ER / ER-alpha / Estradiol receptor / Nuclear receptor subfamily 3 group A member 1 Mass: 29033.018 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli (E. coli) / References: UniProt: P03372
#2: Chemical	ChemComp-A1AI0 / 2-chloro-3-{[{[1-(2-fluorophenyl)cyclopentyl]methyl}(4-{[1-(3-fluoropropyl)azetidin-3-yl]oxy}phenyl)amino]methyl}phenol Mass: 541.072 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃₁H₃₅ClF₂N₂O₂ / Feature type: SUBJECT OF INVESTIGATION
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 399 / Source method: isolated from a natural source / Formula: H₂O
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: 2.32 Å³/Da / Density % sol: 46.91 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: Ammonium acetate

-
Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.99 Å
Detector	Type: MAR CCD 300 mm / Detector: CCD / Date: Feb 15, 2022
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.99 Å / Relative weight: 1
Reflection	Resolution: 2.08→50 Å / Num. obs: 53471 / % possible obs: 95.1 % / Redundancy: 3.1 % / CC_1/2: 0.99 / R_pim(I) all: 0.043 / Net I/σ(I): 464
Reflection shell	Resolution: 2.08→2.14 Å / Num. unique obs: 2832 / CC_1/2: 0.633 / R_pim(I) all: 0.865

-
Processing

Software

Name	Version	Classification
PHENIX	1.18.2_3874	refinement
HKL-3000		data reduction
HKL-3000		data scaling
HKL-3000		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.08→49.19 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 42.38 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.3182	2608	4.88 %
R_work	0.2592	-	-
obs	0.262	53471	88.82 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.08→49.19 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7093	0	76	399	7568

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	7331
X-RAY DIFFRACTION	f_angle_d	0.997	9918
X-RAY DIFFRACTION	f_dihedral_angle_d	8.955	972
X-RAY DIFFRACTION	f_chiral_restr	0.049	1168
X-RAY DIFFRACTION	f_plane_restr	0.006	1213

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 (%)
2.08-2.11	0.3852	72	0.2915	1246	X-RAY DIFFRACTION	42
2.11-2.15	0.3081	142	0.2839	2586	X-RAY DIFFRACTION	87
2.15-2.2	0.2922	116	0.2911	2637	X-RAY DIFFRACTION	88
2.2-2.25	0.3149	136	0.278	2730	X-RAY DIFFRACTION	91
2.25-2.3	0.3287	149	0.2646	2739	X-RAY DIFFRACTION	92
2.3-2.36	0.2764	142	0.2641	2854	X-RAY DIFFRACTION	95
2.36-2.42	0.31	167	0.2637	2858	X-RAY DIFFRACTION	96
2.42-2.49	0.3541	165	0.2758	2901	X-RAY DIFFRACTION	96
2.49-2.57	0.3247	165	0.2602	2906	X-RAY DIFFRACTION	98
2.57-2.66	0.2792	140	0.26	2949	X-RAY DIFFRACTION	97
2.66-2.77	0.3374	157	0.2663	2888	X-RAY DIFFRACTION	97
2.77-2.9	0.2906	155	0.2453	2876	X-RAY DIFFRACTION	96
2.9-3.05	0.3535	144	0.2555	2856	X-RAY DIFFRACTION	95
3.05-3.24	0.3282	149	0.2591	2852	X-RAY DIFFRACTION	94
3.24-3.49	0.3343	130	0.2514	2752	X-RAY DIFFRACTION	91
3.49-3.84	0.3165	136	0.2357	2623	X-RAY DIFFRACTION	87
3.84-4.4	0.2779	123	0.2241	2524	X-RAY DIFFRACTION	83
4.4-5.54	0.3017	118	0.2462	2544	X-RAY DIFFRACTION	83
5.54-49.19	0.3595	102	0.2942	2542	X-RAY DIFFRACTION	79

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	1.7728	0.2935	1.4575	3.3328	2.9444	3.8015	0.1412	0.1047	-0.0788	0.2671	0.1193	-0.6482	0.1031	0.1681	-0.2883	0.1387	-0.0144	0.0168	0.4308	0.0985	0.3116	29.4173	-8.8444	66.297
2	1.4535	-0.4199	-0.4296	2.3539	0.1583	2.9949	0.1951	0.0521	0.0302	-0.3075	-0.2528	-0.1611	-0.2171	-0.0331	0.0554	0.147	-0.0087	0.0078	0.3135	0.0466	0.1366	19.2053	-10.958	62.9459
3	0.7457	-0.4094	0.5431	2.0419	-0.7099	0.6377	0.0205	-0.0917	0.0567	0.0229	-0.0087	-0.173	-0.0676	-0.1196	0.0171	0.0882	0.0931	-0.0039	0.5187	0.0094	0.2639	16.1531	-1.5821	70.5445
4	1.6627	-0.5305	0.2122	5.0986	-2.4343	3.4433	-0.3032	0.0155	0.2792	-0.0469	-0.0355	-0.1524	0.0268	-0.3782	0.4055	0.1036	0.01	-0.0062	0.2828	-0.0449	0.4407	3.2331	-37.5582	19.124
5	1.0637	0.3709	-0.5958	0.8477	-0.3596	0.936	0.008	-0.2991	-0.0706	0.1839	-0.0469	0.0859	0.0472	0.0224	0.0546	0.1333	-0.303	0.042	0.2566	0.0548	0.2724	13.4878	-39.7564	22.5036
6	2.1969	0.189	-0.0255	2.8735	0.3581	3.1163	-0.1449	0.3191	-0.0218	-0.1543	0.0662	0.1542	-0.0018	-0.0548	0.0333	0.1713	0.0678	-0.0233	0.1285	-0.0261	0.2735	13.7382	-24.6104	12.3964
7	0.8525	0.2571	0.0911	1.327	0.1933	1.4856	0.0303	-0.0925	-0.1027	0.0284	-0.1595	-0.1842	0.0839	-0.1208	0.054	0.1401	-0.0291	0.0355	0.1269	0.0003	0.0366	19.5384	-36.2247	17.6965
8	2.3269	1.9184	0.3445	1.6078	0.1853	3.8515	-0.1267	0.4278	0.4271	-0.1462	0.1349	0.6751	-0.8275	-0.0393	0.0593	0.474	0.1053	-0.0079	0.2886	0.1775	0.4945	50.8433	-6.411	58.8314
9	2.2361	-0.1765	-0.6799	2.1168	0.6019	2.3319	-0.046	0.0029	-0.1616	0.1628	-0.1008	0.2869	0.1702	-0.1716	0.1984	0.1616	0.1402	0.0581	0.2411	-0.0401	0.395	35.5525	-23.3199	65.3363
10	1.5244	0.1506	-0.4028	1.4248	0.2998	1.0343	-0.217	0.0417	0.1811	0.0572	0.0047	-0.0924	0.079	0.0053	0.1291	0.1698	0.0871	0.0303	0.4128	0.0639	0.1461	45.0205	-23.3922	64.4497
11	4.8189	-4.5344	-0.4663	6.0835	0.7804	0.1095	-0.2482	-1.2887	-0.5869	0.6903	0.0791	0.4471	0.1081	-0.4833	0.1553	0.3157	0.0275	0.0158	0.6403	-0.0091	0.2497	39.2368	-32.4893	81.8039
12	3.4506	2.4127	-1.0761	5.4636	0.4591	3.5683	-0.0948	-0.4245	-0.0509	0.4246	0.228	-0.3528	0.0305	-0.0562	-0.0267	0.3058	0.0488	0.0429	0.3584	-0.1106	0.1953	51.0324	-26.1551	78.44
13	1.7298	0.4571	-0.3064	1.029	0.4042	4.7229	-0.1426	-0.1214	0.0638	0.1266	-0.179	0.3024	0.1046	0.1464	0.1863	0.1825	-0.0354	0.0093	0.1	0.0066	0.0944	52.6882	-18.5892	63.3397
14	1.0333	0.57	0.1042	1.4137	1.2944	2.5821	0.0148	0.1141	0.0146	0.0212	0.0913	-0.057	-0.1337	-0.1867	-0.0058	0.2811	-0.048	0.0195	0.0109	0.0076	0.1298	59.402	-13.959	57.4894
15	2.1681	0.5975	0.3817	2.9173	0.7096	0.92	0.065	-0.2032	0.0804	0.0337	0.0174	-0.0023	-0.0188	0.0329	-0.0928	-0.0019	0.016	0.0865	0.0715	0.0061	0.1979	56.1046	-26.3398	69.3149
16	4.255	-0.0321	0.3682	7.1274	-4.9637	9.4575	0.224	0.3673	-0.4002	-0.4096	0.43	0.0218	0.0097	-0.6726	-0.7416	0.3011	-0.1288	-0.0146	0.505	-0.0334	0.2713	37.783	-27.6949	50.7454
17	3.2135	-2.2445	-0.2448	4.4522	-0.2613	4.2902	-0.0412	-0.8922	0.1263	0.3478	-0.0381	0.1695	-0.5521	-0.4952	0.0968	0.3836	0.0469	-0.1027	0.5109	-0.028	0.165	32.7537	-6.3803	26.6881
18	0.8014	0.6552	0.6173	2.835	-0.1941	0.6896	-0.06	0.229	0.1369	-0.1716	0.0292	-0.5442	-0.1477	0.1226	0.0967	0.1479	-0.0566	-0.0144	0.4976	-0.0124	0.2232	50.5619	-20.2624	15.4113
19	1.8212	-1.0906	-0.4209	1.8095	-0.1768	2.7997	-0.06	-0.0262	0.001	-0.0695	-0.0573	0.0375	0.2541	-0.0551	-0.0389	0.1831	0.0203	-0.0255	0.4588	0.0391	0.0613	47.006	-24.745	22.2727
20	0.2562	-0.1029	-0.3308	0.2919	0.1383	3.2214	-0.0338	-0.1963	-0.069	0.1174	0.0736	-0.0403	-0.0599	0.0082	0.0059	0.1251	0.0622	-0.0715	0.1741	0.1372	0.2348	36.8911	-23.8479	27.1366
21	5.131	1.9897	1.2853	1.5607	-0.7152	2.7362	0.0925	0.4283	-0.6199	-0.0947	-0.1759	-0.2218	0.0898	0.2575	0.011	0.1478	0.0477	0.0269	0.3298	-0.0374	0.2735	43.6755	-26.7281	4.9951
22	2.9205	0.492	-0.4831	3.2828	-0.3609	0.5635	0.0579	0.1663	-0.1212	0.019	-0.2891	0.1576	-0.0125	-0.0171	0.0156	0.0766	-0.0829	-0.0096	0.4007	-0.1014	0.1807	32.6671	-26.1827	6.9949
23	1.455	0.0737	-0.4068	0.6666	0.0082	0.4857	0.0059	-0.2549	0.2658	0.1627	-0.071	0.1561	0.0007	-0.2451	0.0175	0.171	-0.1318	0.0162	0.5219	-0.1052	0.2978	26.9896	-15.8289	25.5848
24	1.704	-0.1573	-0.0064	2.1897	0.4951	1.2564	-0.1228	-0.1476	-0.3712	-0.0707	0.1419	0.0454	0.027	0.1254	-0.0411	0.2539	-0.0534	0.0169	0.5241	0.0097	0.1634	32.4036	-27.7549	20.5128
25	5.4072	0.5937	5.0547	6.9636	4.3793	6.8456	-0.0764	-0.1162	0.211	-0.1832	-0.1322	-0.2783	-0.7013	0.7225	0.5466	0.3189	-0.2188	-0.0684	0.7399	0.2291	0.2722	50.4778	-16.9813	41.0126

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 307 through 341 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 342 through 437 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 438 through 546 )
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 307 through 341 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 342 through 437 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 438 through 496 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 497 through 545 )
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 307 through 321 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 322 through 363 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 364 through 407 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 408 through 422 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 423 through 438 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 439 through 465 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 466 through 496 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 497 through 527 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 528 through 548 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 307 through 321 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 322 through 341 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 342 through 363 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 364 through 394 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 395 through 422 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 423 through 438 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 439 through 496 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 497 through 544 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 545 through 550 )

-
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

-
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

-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

-
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