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- PDB-7uj7: Estrogen Receptor Alpha Ligand Binding Domain Y537S Mutant in Com... -

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Basic information

Entry
Database: PDB / ID: 7uj7
TitleEstrogen Receptor Alpha Ligand Binding Domain Y537S Mutant in Complex with RU39411
ComponentsEstrogen receptor
KeywordsTRANSCRIPTION / Estrogen Receptor / Hormone / SERM / RU39411 / Activating Mutations / Y537S
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / 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 / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / epithelial cell proliferation involved in mammary gland duct elongation ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / 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 / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / epithelial cell proliferation involved in mammary gland duct elongation / prostate epithelial cord elongation / epithelial cell development / mammary gland branching involved in pregnancy / uterus development / negative regulation of smooth muscle cell apoptotic process / vagina development / TFIIB-class transcription factor binding / steroid hormone receptor signaling pathway / 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 / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / negative regulation of canonical NF-kappaB signal transduction / estrogen receptor signaling pathway / protein localization to chromatin / steroid binding / 14-3-3 protein binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / TBP-class protein binding / nitric-oxide synthase regulator activity / negative regulation of miRNA transcription / positive regulation of nitric-oxide synthase activity / ESR-mediated signaling / transcription coregulator binding / transcription corepressor binding / nuclear estrogen receptor binding / positive regulation of DNA-binding transcription factor activity / stem cell differentiation / cellular response to estradiol stimulus / SUMOylation of intracellular receptors / negative regulation of DNA-binding transcription factor activity / transcription coactivator binding / euchromatin / beta-catenin binding / Nuclear Receptor transcription pathway / response to estrogen / nuclear receptor activity / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of fibroblast proliferation / male gonad development / Regulation of RUNX2 expression and activity / sequence-specific double-stranded DNA binding / positive regulation of nitric oxide biosynthetic process / Ovarian tumor domain proteases / PIP3 activates AKT signaling / response to estradiol / ATPase binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cytosolic calcium ion concentration / DNA-binding transcription activator activity, RNA polymerase II-specific / regulation of inflammatory response / 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 / Extra-nuclear estrogen signaling / calmodulin binding / 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 DNA-templated transcription / regulation of transcription by RNA polymerase II / protein kinase binding / chromatin / positive regulation of DNA-templated transcription / enzyme binding / Golgi apparatus / negative regulation of transcription by RNA polymerase II / 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
Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor ...Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Double treble clef zinc finger, C4 type / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-NYU / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.68 Å
AuthorsFanning, S.W. / Greene, G.L.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Elife / Year: 2022
Title: Stereospecific lasofoxifene derivatives reveal the interplay between estrogen receptor alpha stability and antagonistic activity in ESR1 mutant breast cancer cells.
Authors: Hosfield, D.J. / Weber, S. / Li, N.S. / Suavage, M. / Joiner, C.F. / Hancock, G.R. / Sullivan, E.A. / Ndukwe, E. / Han, R. / Cush, S. / Laine, M. / Mader, S.C. / Greene, G.L. / Fanning, S.W.
History
DepositionMar 30, 2022Deposition site: RCSB / Processing site: RCSB
SupersessionMay 4, 2022ID: 6VJ1
Revision 1.0May 4, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 15, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: Estrogen receptor
B: Estrogen receptor
A: Estrogen receptor
C: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)122,3318
Polymers120,5894
Non-polymers1,7424
Water10,215567
1
D: Estrogen receptor
B: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,1664
Polymers60,2942
Non-polymers8712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2800 Å2
ΔGint-12 kcal/mol
Surface area18990 Å2
MethodPISA
2
A: Estrogen receptor
C: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,1664
Polymers60,2942
Non-polymers8712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2960 Å2
ΔGint-15 kcal/mol
Surface area18160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.110, 58.980, 87.880
Angle α, β, γ (deg.)101.830, 90.010, 119.510
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Estrogen receptor / ER / ER-alpha / Estradiol receptor / Nuclear receptor subfamily 3 group A member 1


Mass: 30147.186 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-NYU / 11alpha-{4-[2-(dimethylamino)ethoxy]phenyl}estra-1(10),2,4-triene-3,17beta-diol


Mass: 435.598 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C28H37NO3 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 567 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.77 %
Crystal growTemperature: 298.15 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, Tris pH 7.5, MgCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 0.987 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Jun 19, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 1.68→50 Å / Num. obs: 105736 / % possible obs: 94.4 % / Redundancy: 3.6 % / Rpim(I) all: 0.031 / Net I/σ(I): 22
Reflection shellResolution: 1.68→1.74 Å / Num. unique obs: 4825 / CC1/2: 0.51

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UFX

5ufx


Resolution: 1.68→29.22 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 24.88 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.24 5269 4.98 %
Rwork0.198 100467 -
obs0.2 105736 94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 87.42 Å2 / Biso mean: 36.08 Å2 / Biso min: 11.47 Å2
Refinement stepCycle: final / Resolution: 1.68→29.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6820 0 128 567 7515
Biso mean--20 41.75 -
Num. residues----872
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.68-1.70.33151790.32293316349593
1.7-1.720.3441760.31643303347993
1.72-1.740.29751880.29683340352893
1.74-1.760.32771800.28753345352594
1.76-1.790.33411530.27623369352294
1.79-1.810.32421460.27283346349294
1.81-1.840.28111990.27283349354894
1.84-1.860.32181820.27113325350794
1.86-1.890.2991780.25583365354394
1.89-1.920.29981490.24853388353795
1.92-1.960.26111910.23273392358394
1.96-1.990.23141620.21773379354195
1.99-2.030.29841720.21923444361695
2.03-2.070.24521730.21513344351795
2.07-2.120.26181880.21433401358995
2.12-2.170.25881990.2053315351495
2.17-2.220.21911910.19733371356295
2.22-2.280.25892060.19173412361896
2.28-2.350.23751810.19073429361096
2.35-2.420.22471350.19783419355495
2.42-2.510.22161800.18853443362395
2.51-2.610.24951900.18923336352696
2.61-2.730.21431710.18643416358795
2.73-2.870.22951640.19193353351794
2.87-3.050.22831850.18093311349693
3.05-3.290.19912000.18333405360595
3.29-3.620.22171590.1733398355796
3.62-4.140.21631720.15683421359395
4.14-5.210.21741590.16733325348493
5.21-29.220.26451610.22812707286876
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°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)
14.03760.49192.23545.1511-1.95342.72650.284-0.04930.11740.73470.24411.3422-0.351-1.2646-0.52220.27780.05620.14230.6277-0.02710.58221.553-9.96-17.066
26.76545.1334-4.22719.2722-3.89196.58690.1442-0.19920.2827-0.2728-0.1510.3739-0.66930.32020.02310.35260.0914-0.01890.23950.00540.197217.9627.832-27.586
38.72216.8174-4.89889.7749-5.52387.2507-0.0920.03780.34940.34320.01280.0385-0.5172-0.12040.09030.22970.0824-0.04990.15790.00430.160220.0584.512-20.969
41.86640.2158-0.64143.0034-1.31169.07630.0362-0.0968-0.05830.57320.03560.1352-0.1823-0.1942-0.05870.22110.06240.02870.1126-0.00360.155718.865-5.597-15.639
53.45611.55070.57398.03810.61179.0608-0.21890.6720.3081-0.49210.29290.2792-0.2391-0.2715-0.10120.20250.0662-0.01560.29480.01470.145818.1730.807-37.125
65.11740.1157-0.24177.27310.42717.6054-0.1380.6653-0.0431-0.5819-0.0211-1.1109-0.45081.23330.17710.3933-0.06230.0830.48260.07520.327829.1232.242-38.606
79.77955.75540.60059.7947-0.66466.1829-0.26930.2507-0.2474-0.42920.1656-0.77230.2750.58530.090.24830.13110.03420.321-0.03810.235623.942-8.333-35.975
83.78970.7571-0.78174.3054-0.11229.3081-0.0374-0.0088-0.17390.3810.0520.21920.2442-0.0054-0.06370.1690.04560.04910.1391-0.02140.224515.752-12.455-19.326
96.48170.1944.87593.77670.97727.61350.0458-0.0899-0.43890.52790.05180.71820.0823-0.8771-0.09370.2412-0.00640.15810.3206-0.01990.42039.13-18.113-15.389
105.82384.00081.29154.76681.16353.6171-0.07650.2832-0.393-0.08940.0116-0.31460.26560.080.06280.17290.1052-0.00220.2122-0.03420.278920.686-15.966-27.384
119.1666-2.6735-5.81774.94180.76844.26440.3543-0.30690.85410.51750.005-0.3897-0.49510.2022-0.40180.7573-0.0992-0.04760.3565-0.02740.290422.7393.272-8.338
124.89830.59440.49423.96560.64743.51680.087-0.137-0.34810.2288-0.0887-0.1110.55270.297-0.03320.30750.10790.04780.17550.04020.255737.037-36.2-23.678
132.6499-1.08350.42533.8803-0.44747.0401-0.1679-0.25710.00240.4240.14930.0491-0.1297-0.02440.03210.17830.0830.0370.1531-0.00330.208434.528-28.873-22.116
145.0912-0.35941.23254.10161.89436.1898-0.1921-0.2307-0.26680.4240.03440.3483-0.0127-0.24590.14030.25280.12690.04750.16310.00210.262426.206-26.764-19.969
155.3088-0.2317-0.2584.41820.26392.84950.02390.2273-0.3472-0.1083-0.10320.42660.1979-0.28410.08020.22180.0648-0.01150.1504-0.03780.291420.255-25.612-25.953
164.1488-0.0476-0.79885.77931.54644.4669-0.29910.2557-0.0556-0.02970.2371-0.60330.3870.87480.00940.32010.02070.05880.53180.05350.30443.524-26.824-35.877
171.7916-2.1414-0.91334.0212-1.14114.07990.15880.05510.1524-0.81460.11371.44630.2347-1.3442-0.26790.2409-0.044-0.16660.6961-0.05040.6433-27.442-22.41-68.795
189.9228-2.28031.45925.2617-0.65914.0493-0.0969-0.2308-0.29170.14640.00690.25990.7380.15610.08160.3603-0.07860.03370.2212-0.00110.1906-10.95-40.526-58.27
196.9909-4.82293.13827.4786-3.15154.5562-0.0665-0.122-0.4611-0.35710.14120.17430.4659-0.1965-0.09440.2437-0.08530.04070.16920.01950.1664-9.033-36.822-65.073
201.6118-0.40040.59563.0791-1.04898.43190.01950.02560.0615-0.5611-0.01460.07560.1742-0.17280.00560.2212-0.0741-0.02050.1187-0.01470.1627-10.201-26.647-69.925
213.8547-2.3704-1.71162.01871.54368.9065-0.2187-0.6423-0.24890.46540.26240.20390.4933-0.2484-0.01790.2318-0.08980.00870.28760.03960.1867-9.551-34.037-48.681
222.45312.8896-2.44734.9641-2.07447.4912-0.3293-0.49520.19350.3063-0.0654-0.83420.32312.02310.37110.54420.0588-0.2670.7829-0.04550.64583.676-32.948-48.004
238.4951-6.0991-0.43328.26480.30468.8333-0.162-0.78060.62030.67090.1031-0.5044-0.11270.360.07540.2545-0.1155-0.03260.2884-0.04380.2056-5.649-23.506-49.778
242.9615-0.32170.30074.29360.37477.2162-0.1322-0.34480.11930.0810.07420.5511-0.0247-0.76070.1020.1238-0.0336-0.00730.2578-0.00710.2596-17.188-21.264-60.826
258.3698-1.26362.93198.0343-3.53416.0860.20650.90590.8364-0.7050.2369-0.3963-1.07730.5443-0.40710.5895-0.17070.09190.4899-0.03560.3409-5.524-16.825-76.618
265.1516-0.5406-3.38333.71081.85139.7362-0.10550.13940.3675-0.4083-0.09010.5959-0.2779-1.01430.19530.22460.0127-0.13650.2998-0.02720.4299-19.971-14.188-70.259
279.427-4.8267-1.28628.94721.44853.6362-0.0676-0.37210.48820.0968-0.0292-0.133-0.2558-0.0150.08440.1649-0.0932-0.0150.2024-0.03340.2314-8.827-15.872-58.444
282.0682.39425.71666.13071.03382.06630.01210.5537-1.085-1.49190.7357-0.55040.78520.8104-0.59550.77660.03890.09670.5402-0.08840.3862-6.085-35.706-77.546
293.782-0.0386-0.13163.41250.39493.11750.01810.10980.4806-0.0605-0.069-0.0671-0.4740.2057-0.01960.2976-0.1034-0.05060.17740.03040.26886.6483.495-59.931
302.61960.84750.56153.30140.38324.0399-0.2570.4425-0.0046-0.70620.178-0.00430.2285-0.14370.06830.3014-0.1195-0.01520.22160.01380.22754.785-4.995-68.688
314.92090.5091-0.41693.90650.63794.4240.0442-0.36460.49840.3284-0.19120.6443-0.4609-0.22820.1470.2237-0.04520.01990.2157-0.09130.416-9.194-2.947-56.736
324.6887-0.21540.59872.7858-02.7852-0.25230.0932-0.2761-0.14690.13120.0143-0.09610.16430.14310.2279-0.06560.01710.13080.03310.1837-0.472-8.918-61.599
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 307:321 )A307 - 321
2X-RAY DIFFRACTION2( CHAIN A AND RESID 322:341 )A322 - 341
3X-RAY DIFFRACTION3( CHAIN A AND RESID 342:363 )A342 - 363
4X-RAY DIFFRACTION4( CHAIN A AND RESID 364:394 )A364 - 394
5X-RAY DIFFRACTION5( CHAIN A AND RESID 395:407 )A395 - 407
6X-RAY DIFFRACTION6( CHAIN A AND RESID 408:420 )A408 - 420
7X-RAY DIFFRACTION7( CHAIN A AND RESID 421:437 )A421 - 437
8X-RAY DIFFRACTION8( CHAIN A AND RESID 438:461 )A438 - 461
9X-RAY DIFFRACTION9( CHAIN A AND RESID 466:496 )A466 - 496
10X-RAY DIFFRACTION10( CHAIN A AND RESID 497:525 )A497 - 525
11X-RAY DIFFRACTION11( CHAIN A AND RESID 536:547 )A536 - 547
12X-RAY DIFFRACTION12( CHAIN B AND RESID 307:363 )B307 - 363
13X-RAY DIFFRACTION13( CHAIN B AND RESID 364:421 )B364 - 421
14X-RAY DIFFRACTION14( CHAIN B AND RESID 422:465 )B422 - 465
15X-RAY DIFFRACTION15( CHAIN B AND RESID 466:525 )B466 - 525
16X-RAY DIFFRACTION16( CHAIN B AND RESID 526:545 )B526 - 545
17X-RAY DIFFRACTION17( CHAIN D AND RESID 307:321 )D307 - 321
18X-RAY DIFFRACTION18( CHAIN D AND RESID 322:341 )D322 - 341
19X-RAY DIFFRACTION19( CHAIN D AND RESID 342:363 )D342 - 363
20X-RAY DIFFRACTION20( CHAIN D AND RESID 364:394 )D364 - 394
21X-RAY DIFFRACTION21( CHAIN D AND RESID 395:411 )D395 - 411
22X-RAY DIFFRACTION22( CHAIN D AND RESID 412:421 )D412 - 421
23X-RAY DIFFRACTION23( CHAIN D AND RESID 422:437 )D422 - 437
24X-RAY DIFFRACTION24( CHAIN D AND RESID 438:455 )D438 - 455
25X-RAY DIFFRACTION25( CHAIN D AND RESID 456:465 )D456 - 465
26X-RAY DIFFRACTION26( CHAIN D AND RESID 466:496 )D466 - 496
27X-RAY DIFFRACTION27( CHAIN D AND RESID 497:524 )D497 - 524
28X-RAY DIFFRACTION28( CHAIN D AND RESID 525:547 )D525 - 547
29X-RAY DIFFRACTION29(chain C and resid 307:371)C307 - 371
30X-RAY DIFFRACTION30(chain C and resid 372:437)C372 - 437
31X-RAY DIFFRACTION31(chain C and resid 438:496)C438 - 496
32X-RAY DIFFRACTION32(chain C and resid 497:545)C497 - 545

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Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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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

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