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- PDB-2qse: Crystal Structure of the Estrogen Receptor Alpha Ligand Binding D... -

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Basic information

Entry
Database: PDB / ID: 2qse
TitleCrystal Structure of the Estrogen Receptor Alpha Ligand Binding Domain complexed with Burned Meat Compound 4-OH-PhIP
Components
  • Estrogen receptor
  • Nuclear receptor coactivator 2
KeywordsTRANSCRIPTION / Protein-Ligand Complex / DNA-binding / Lipid-binding / Metal-binding / Nucleus / Phosphorylation / Receptor / Steroid-binding / Transcription regulation / Zinc-finger
Function / homology
Function and homology information


Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Recycling of bile acids and salts / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts / positive regulation of glucocorticoid receptor signaling pathway / Endogenous sterols / HATs acetylate histones / Regulation of lipid metabolism by PPARalpha / Cytoprotection by HMOX1 ...Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Recycling of bile acids and salts / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts / positive regulation of glucocorticoid receptor signaling pathway / Endogenous sterols / HATs acetylate histones / Regulation of lipid metabolism by PPARalpha / Cytoprotection by HMOX1 / nuclear glucocorticoid receptor binding / Estrogen-dependent gene expression / nuclear retinoic acid receptor binding / positive regulation of female receptivity / nuclear thyroid hormone receptor binding / regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / prostate epithelial cord elongation / epithelial cell development / locomotor rhythm / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / aryl hydrocarbon receptor binding / TFIIB-class transcription factor binding / androgen metabolic process / regulation of lipid metabolic process / steroid hormone mediated signaling pathway / cellular response to Thyroglobulin triiodothyronine / regulation of glucose metabolic process / mammary gland alveolus development / intracellular estrogen receptor signaling pathway / cellular response to estrogen stimulus / estrogen response element binding / Nuclear signaling by ERBB4 / positive regulation of phospholipase C activity / DNA polymerase binding / nuclear retinoid X receptor binding / intracellular steroid hormone receptor signaling pathway / negative regulation of canonical NF-kappaB signal transduction / RNA polymerase II preinitiation complex assembly / regulation of cellular response to insulin stimulus / cellular response to hormone stimulus / protein localization to chromatin / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / TBP-class protein binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / steroid binding / nitric-oxide synthase regulator activity / ESR-mediated signaling / 14-3-3 protein binding / transcription corepressor binding / nuclear receptor coactivator activity / negative regulation of miRNA transcription / response to progesterone / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / nuclear estrogen receptor binding / transcription coregulator binding / stem cell differentiation / nuclear receptor binding / circadian regulation of gene expression / euchromatin / SUMOylation of intracellular receptors / mRNA transcription by RNA polymerase II / negative regulation of DNA-binding transcription factor activity / transcription coactivator binding / beta-catenin binding / Nuclear Receptor transcription pathway / circadian rhythm / response to estrogen / RNA polymerase II transcription regulator complex / male gonad development / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / positive regulation of nitric oxide biosynthetic process / positive regulation of DNA-binding transcription factor activity / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / sequence-specific double-stranded DNA binding / response to estradiol / PIP3 activates AKT signaling / phospholipase C-activating G protein-coupled receptor signaling pathway / ATPase binding / positive regulation of cytosolic calcium ion concentration / fibroblast proliferation / regulation of inflammatory response / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
Similarity search - Function
Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear receptor coactivator, DUF1518 ...Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2/3, DUF4927 / Domain of unknown function (DUF4927) / Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear receptor coactivator, DUF1518 / Nuclear receptor coactivator, Ncoa-type, interlocking / Nuclear receptor coactivator, Ncoa-type, interlocking domain superfamily / Nuclear receptor coactivator, DUF1518 / Nuclear receptor coactivator / DUF1518 / Nuclear receptor coactivator, receptor-binding domain / Nuclear receptor coactivator / Steroid receptor coactivator / Unstructured region on nuclear receptor coactivator protein / PAS domain / Nuclear receptor coactivator, interlocking / Helix-loop-helix DNA-binding domain superfamily / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / PAS fold / PAS fold / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / 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-1HP / Estrogen receptor / Nuclear receptor coactivator 2 / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus Musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.85 Å
AuthorsNettles, K.W. / Bruning, J.B.
CitationJournal: Nat.Chem.Biol. / Year: 2008
Title: NFkappaB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses
Authors: Nettles, K.W. / Bruning, J.B. / Gil, G. / Nowak, J. / Sharma, S.K. / Hahm, J.B. / Kulp, K. / Hochberg, R.B. / Zhou, H. / Katzenellenbogen, J.A. / Katzenellenbogen, B.S. / Kim, Y. / Joachmiak, A. / Greene, G.L.
History
DepositionJul 30, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 18, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Refinement description / Source and taxonomy / Category: pdbx_entity_src_syn / software
Item: _pdbx_entity_src_syn.details / _pdbx_entity_src_syn.ncbi_taxonomy_id ..._pdbx_entity_src_syn.details / _pdbx_entity_src_syn.ncbi_taxonomy_id / _pdbx_entity_src_syn.organism_common_name / _pdbx_entity_src_syn.organism_scientific / _software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3Oct 20, 2021Group: Database references / Derived calculations / Category: database_2 / 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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Aug 30, 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
A: Estrogen receptor
B: Estrogen receptor
C: Nuclear receptor coactivator 2
D: Nuclear receptor coactivator 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,4136
Polymers61,9334
Non-polymers4812
Water6,467359
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5450 Å2
ΔGint-27.2 kcal/mol
Surface area20590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.081, 84.044, 58.668
Angle α, β, γ (deg.)90.000, 108.850, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Estrogen receptor / / ER / Estradiol receptor / ER-alpha


Mass: 29386.609 Da / Num. of mol.: 2 / Fragment: Steroid-binding region, residues 298-554 / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Rosetta / References: UniProt: P03372
#2: Protein/peptide Nuclear receptor coactivator 2 /


Mass: 1579.866 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Mus Musculus (house mouse) / References: UniProt: Q8BN74, UniProt: Q61026*PLUS
#3: Chemical ChemComp-1HP / 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol


Mass: 240.261 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H12N4O
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 359 / Source method: isolated from a natural source / Formula: H2O

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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: 41.78 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.2M Magnesium chloride hexahydrate, 0.1M Tris 8.5, 25% Polyehtlyene glycol 3,350, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97946 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Feb 3, 2007 / Details: Flat mirror (vertical focusing)
RadiationMonochromator: single crystal Si(111) bent monochromator (horizontal focusing)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 1.85→15 Å / Num. all: 41792 / Num. obs: 41792 / % possible obs: 95.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 33.7 Å2 / Rmerge(I) obs: 0.064 / Rsym value: 0.064 / Χ2: 1.317 / Net I/σ(I): 17.5
Reflection shellResolution: 1.85→1.92 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.283 / Mean I/σ(I) obs: 3.68 / Num. unique all: 3122 / Rsym value: 0.283 / Χ2: 1.344 / % possible all: 71.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
REFMAC5.2.0019refinement
PDB_EXTRACT3data extraction
HKL-2000data collection
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3ERD
Resolution: 1.85→14.99 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.941 / SU B: 7.342 / SU ML: 0.112 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.144 / ESU R Free: 0.143 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.225 2117 5.1 %RANDOM
Rwork0.169 ---
obs0.171 41769 95 %-
all-41769 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 21.827 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å20 Å20.01 Å2
2---0.01 Å20 Å2
3---0.04 Å2
Refinement stepCycle: LAST / Resolution: 1.85→14.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3944 0 36 359 4339
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0214108
X-RAY DIFFRACTIONr_bond_other_d0.0030.022717
X-RAY DIFFRACTIONr_angle_refined_deg1.4221.9895572
X-RAY DIFFRACTIONr_angle_other_deg0.9573.0016678
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.3595515
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.30624.096166
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.89515765
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.7261521
X-RAY DIFFRACTIONr_chiral_restr0.0820.2660
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.024439
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02760
X-RAY DIFFRACTIONr_nbd_refined0.240.21035
X-RAY DIFFRACTIONr_nbd_other0.1940.22809
X-RAY DIFFRACTIONr_nbtor_refined0.180.21970
X-RAY DIFFRACTIONr_nbtor_other0.0910.22078
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.180.2227
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.330.210
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2890.231
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2480.221
X-RAY DIFFRACTIONr_mcbond_it0.9881.52611
X-RAY DIFFRACTIONr_mcbond_other0.2131.51013
X-RAY DIFFRACTIONr_mcangle_it1.50324063
X-RAY DIFFRACTIONr_scbond_it2.17131706
X-RAY DIFFRACTIONr_scangle_it3.3284.51498
LS refinement shellResolution: 1.85→1.896 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.274 119 -
Rwork0.237 1992 -
all-2111 -
obs-1992 66.22 %
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
135.218942.692-18.365754.9187-25.24912.3923-0.36861.0307-0.8145-0.57431.2118-1.0730.39110.0179-0.84320.03580.1056-0.10990.0686-0.05770.351130.8548-13.612.0437
213.7298-2.26719.97071.0876-1.88828.1762-0.38880.7354-0.6053-0.23670.3149-0.2886-0.07240.48750.07390.1098-0.04450.10060.1884-0.04530.142826.3873-3.0611-5.8466
322.3867-4.8739-2.48575.14980.13060.3172-0.1677-0.1430.9884-0.67970.19010.8413-0.42870.0677-0.02240.3969-0.0017-0.21180.1004-0.04340.25271.33539.4296-16.564
47.2603-4.36364.17633.7701-1.10084.133-0.186-0.0647-0.0001-0.21540.0680.03790.0004-0.0840.1180.2035-0.0525-0.00110.1269-0.0040.10548.0859-2.043-13.0462
50.9621-0.53930.32572.83860.03031.85550.01780.0965-0.1269-0.1183-0.0122-0.03090.1186-0.006-0.00560.1774-0.00640.01440.1036-0.00580.112113.5622-6.9328-2.8094
61.25970.85160.18766.37984.353910.1038-0.27530.14080.2608-0.74510.13120.0431-0.7566-0.22510.14420.36490.0031-0.07410.02010.04380.04459.472914.3555-9.2172
730.4211-7.67378.894215.7318-6.49868.8187-0.02030.9527-0.7934-0.9117-0.04841.69040.0407-0.34380.06870.22110.0823-0.11340.1184-0.04770.2955-2.112111.9184-3.0739
824.3502-0.64585.88841.4047-0.61462.2333-0.46320.18870.62040.04110.1744-0.1522-0.4467-0.12210.28880.2596-0.0088-0.03730.04950.01860.122114.001712.94863.0289
91.23551.63090.1234.544-1.47882.1875-0.08970.1211-0.0871-0.0584-0.0135-0.137-0.08820.04580.10320.1482-0.00320.01660.13310.00320.130220.2269-0.52481.5494
1017.42398.1185-10.842615.3421-9.045530.5377-0.2607-0.92270.10391.07030.15881.18511.54680.17330.10190.1777-0.02520.07860.27290.07660.09869.7819-12.62718.4281
1131.372217.7878-26.584711.9131-15.937622.9366-0.24440.787-1.662-0.3943-0.06651.2934-1.7947-1.80060.31080.641-0.1195-0.17480.47130.09070.592612.8231-22.88259.7757
124.1023.60440.8297.18931.67061.3178-0.08110.1707-0.14550.05020.0675-0.18490.19160.19970.01360.08530.0240.02020.160.00770.153527.3154-4.26858.6365
135.08890.78841.9760.69250.2790.93520.05770.01830.2676-0.0317-0.038-0.054-0.0245-0.0135-0.01970.12440.00140.00420.1403-0.00680.163216.85764.650810.4757
1429.25332.67317.19491.98182.305421.719-0.18120.05260.46930.3164-0.35310.32160.107-1.2370.53430.03230.01410.01790.2351-0.01620.1537-4.7043-0.37-1.9802
158.3245-0.52821.72451.4981-0.38823.748-0.16580.0374-0.2089-0.14040.07580.4385-0.3779-0.66240.090.20890.0027-0.11070.1692-0.02490.1291-3.1572-6.2006-8.3238
168.4482.9309-2.04162.0490.74112.6329-0.0635-0.37880.48990.33530.21460.0321-0.40080.1429-0.15120.1891-0.0426-0.0960.1796-0.07740.118316.95298.345132.1542
175.55234.73661.16584.67320.11681.46270.1264-0.32450.15720.1943-0.19180.34680.16780.06740.06540.13390.01450.0490.1045-0.00690.1802-10.6238-10.010431.6077
185.88046.00092.54256.75733.68672.98190.0409-0.0113-0.10130.1208-0.06020.0289-0.0424-0.0990.01930.10830.0080.00620.1470.02160.1677-9.6836-2.796126.1141
1911.41215.5383-0.218513.77230.18022.47320.2519-0.38130.27290.6155-0.0229-0.1071-0.0960.0901-0.2290.1573-0.00370.02690.1054-0.03570.10875.437710.263928.9836
200.5659-0.4468-0.19494.3648-0.16110.63480.0615-0.04310.0445-0.0258-0.0073-0.0489-0.0838-0.0293-0.05420.13650.00460.01770.13060.01020.14892.68226.225421.6775
210.27340.6655-0.11533.4217-0.03563.4021-0.054-0.0598-0.32980.1488-0.13280.00470.1169-0.0170.18670.14330.00320.05730.09370.01620.1885-1.7512-15.363725.8039
2229.29693.8908-4.2446.2867-3.12871.7551-0.10760.5751-0.2217-0.01270.20690.16190.1735-0.14-0.09940.1596-0.0226-0.0270.1253-0.06380.1019-7.9203-13.37914.8682
2318.58053.10448.44291.34541.1044.1513-0.01080.1091-0.7474-0.10970.0511-0.30020.1854-0.0408-0.04030.14490.02450.03320.0920.00950.19859.2891-12.892119.4362
242.3908-1.39570.29214.6572-2.5911.92150.0075-0.1770.0142-0.00080.0538-0.1411-0.06460.0305-0.06130.1175-0.00770.00120.1588-0.01270.133911.82322.027822.9437
2514.93534.0676-1.372420.6267-0.01020.1329-0.91020.2731.3558-0.43470.8521-0.08640.25660.43320.05810.49810.17630.01650.42960.13190.161410.078119.578613.1135
265.3096-4.17460.06676.6091-1.39970.6050.0658-0.30590.26090.1608-0.0429-0.173-0.21910.2633-0.02290.0987-0.0302-0.03150.1822-0.0440.128322.51314.826722.3718
274.8074-1.12592.29860.6411-0.54691.8478-0.0221-0.2442-0.007-0.02940.0124-0.03720.0834-0.02460.00960.11170.01750.00760.16420.01420.151219.7958-4.406516.3327
2812.8050.3178-1.36370.8120.14720.1860.02320.203-0.0639-0.08460.0260.1134-0.02-0.0201-0.04910.11430.0026-0.01470.17830.01580.1322-6.8866-2.625912.8878
297.64410.6556-0.58747.32263.11279.8928-0.15580.20710.02920.0032-0.20160.136-0.1346-0.4080.35740.05720.0050.01170.0993-0.04420.2166-11.30996.467820.2013
3014.96952.4515-9.73448.714124.375221.6046-1.0041.87251.1812-2.91080.16550.8213-1.3123-1.9750.83850.2629-0.0738-0.07010.32780.07260.0367-7.21487.25139.9855
3134.415-8.99348.712322.56915.65410.71560.73020.5801-1.6405-0.759-0.55251.16360.788-0.4088-0.17770.243-0.0651-0.03420.0612-0.06780.10597.5585-17.0375-11.0528
329.25921.686-3.42217.27774.37876.7217-0.01350.18310.91230.1162-0.28260.7292-0.2512-0.42030.29610.11220.03960.04010.107-0.03840.2266-6.70916.789325.9794
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA305 - 3119 - 15
2X-RAY DIFFRACTION2AA312 - 32616 - 30
3X-RAY DIFFRACTION3AA327 - 34331 - 47
4X-RAY DIFFRACTION4AA344 - 35948 - 63
5X-RAY DIFFRACTION5AA360 - 39664 - 100
6X-RAY DIFFRACTION6AA397 - 412101 - 116
7X-RAY DIFFRACTION7AA413 - 425117 - 129
8X-RAY DIFFRACTION8AA426 - 439130 - 143
9X-RAY DIFFRACTION9AA440 - 455144 - 159
10X-RAY DIFFRACTION10AA456 - 461160 - 165
11X-RAY DIFFRACTION11AA462 - 472166 - 176
12X-RAY DIFFRACTION12AA473 - 497177 - 201
13X-RAY DIFFRACTION13AA498 - 518202 - 222
14X-RAY DIFFRACTION14AA519 - 530223 - 234
15X-RAY DIFFRACTION15AA531 - 549235 - 253
16X-RAY DIFFRACTION16BB306 - 32310 - 27
17X-RAY DIFFRACTION17BB324 - 33828 - 42
18X-RAY DIFFRACTION18BB339 - 35643 - 60
19X-RAY DIFFRACTION19BB357 - 36761 - 71
20X-RAY DIFFRACTION20BB368 - 39572 - 99
21X-RAY DIFFRACTION21BB396 - 415100 - 119
22X-RAY DIFFRACTION22BB416 - 425120 - 129
23X-RAY DIFFRACTION23BB426 - 439130 - 143
24X-RAY DIFFRACTION24BB440 - 458144 - 162
25X-RAY DIFFRACTION25BB459 - 472163 - 176
26X-RAY DIFFRACTION26BB473 - 498177 - 202
27X-RAY DIFFRACTION27BB499 - 512203 - 216
28X-RAY DIFFRACTION28BB513 - 535217 - 239
29X-RAY DIFFRACTION29BB536 - 544240 - 248
30X-RAY DIFFRACTION30BB545 - 550249 - 254
31X-RAY DIFFRACTION31CC687 - 6962 - 11
32X-RAY DIFFRACTION32DD686 - 6961 - 11

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