[English] 日本語
Yorodumi
- PDB-5dzh: Crystal Structure of the ER-alpha Ligand-binding Domain in Comple... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5dzh
TitleCrystal Structure of the ER-alpha Ligand-binding Domain in Complex with the Cyclofenil Derivative 4,4'-{[4-(2-hydroxyethyl)cyclohexylidene]methanediyl}diphenol
Components
  • Estrogen receptor
  • Nuclear receptor coactivator 2
KeywordsTRANSCRIPTION / Nuclear receptor / transcription factor / ligand binding / protein-ligand complex
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / 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 / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding / 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 / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / epithelial cell development / prostate epithelial cord elongation / locomotor rhythm / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / aryl hydrocarbon receptor binding / regulation of lipid metabolic process / TFIIB-class transcription factor binding / androgen metabolic process / steroid hormone mediated signaling pathway / cellular response to Thyroglobulin triiodothyronine / regulation of glucose metabolic process / Synthesis of bile acids and bile salts / mammary gland alveolus development / intracellular estrogen receptor signaling pathway / cellular response to estrogen stimulus / Endogenous sterols / estrogen response element binding / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / : / intracellular steroid hormone receptor signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / regulation of cellular response to insulin stimulus / Recycling of bile acids and salts / cellular response to hormone stimulus / protein localization to chromatin / 14-3-3 protein binding / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / RORA activates gene expression / TBP-class protein binding / Regulation of lipid metabolism by PPARalpha / steroid binding / nitric-oxide synthase regulator activity / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / BMAL1:CLOCK,NPAS2 activates circadian gene expression / SUMOylation of transcription cofactors / Activation of gene expression by SREBF (SREBP) / nuclear receptor coactivator activity / negative regulation of miRNA transcription / response to progesterone / cellular response to estradiol stimulus / transcription coregulator binding / stem cell differentiation / nuclear estrogen receptor binding / nuclear receptor binding / positive regulation of nitric-oxide synthase activity / circadian regulation of gene expression / Heme signaling / SUMOylation of intracellular receptors / euchromatin / mRNA transcription by RNA polymerase II / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Transcriptional activation of mitochondrial biogenesis / negative regulation of DNA-binding transcription factor activity / PPARA activates gene expression / Cytoprotection by HMOX1 / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / response to estrogen / RNA polymerase II transcription regulator complex / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / positive regulation of nitric oxide biosynthetic process / male gonad development / positive regulation of fibroblast proliferation / sequence-specific double-stranded DNA binding / Ovarian tumor domain proteases / Circadian Clock / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / HATs acetylate histones / ATPase binding / positive regulation of cytosolic calcium ion concentration / regulation of inflammatory response / fibroblast proliferation / 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-5KG / Estrogen receptor / Nuclear receptor coactivator 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.11 Å
AuthorsNwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Cavett, V. / Nowak, J. / Houtman, R. ...Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Cavett, V. / Nowak, J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / Katzenellenbogen, J.A. / Zhou, H.B. / Nettles, K.W.
CitationJournal: Mol.Syst.Biol. / Year: 2016
Title: Predictive features of ligand-specific signaling through the estrogen receptor.
Authors: Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Nowak, J. / Wright, N.J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / ...Authors: Nwachukwu, J.C. / Srinivasan, S. / Zheng, Y. / Wang, S. / Min, J. / Dong, C. / Liao, Z. / Nowak, J. / Wright, N.J. / Houtman, R. / Carlson, K.E. / Josan, J.S. / Elemento, O. / Katzenellenbogen, J.A. / Zhou, H.B. / Nettles, K.W.
History
DepositionSep 25, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 4, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2023Group: Data collection / Database references ...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_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
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)62,5826
Polymers61,9334
Non-polymers6492
Water3,135174
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5590 Å2
ΔGint-31 kcal/mol
Surface area19980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.574, 81.954, 58.053
Angle α, β, γ (deg.)90.000, 111.000, 90.000
Int Tables number4
Space group name H-MP1211

-
Components

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


Mass: 29299.535 Da / Num. of mol.: 2 / Fragment: ligand-binding domain / Mutation: Y537S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03372
#2: Protein/peptide Nuclear receptor coactivator 2 / / NCoA-2 / Class E basic helix-loop-helix protein 75 / bHLHe75 / Transcriptional intermediary factor 2 / hTIF2


Mass: 1666.943 Da / Num. of mol.: 2 / Fragment: Nuclear receptor-interacting peptide / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15596
#3: Chemical ChemComp-5KG / 4,4'-{[4-(2-hydroxyethyl)cyclohexylidene]methanediyl}diphenol


Mass: 324.413 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H24O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 174 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 1.96 Å3/Da / Density % sol: 37.32 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.3 / Details: 15% PEG 3350, 0.05M MgCl2, 0.067M NaCl, 0.1M Tris

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 27, 2013
RadiationMonochromator: Side scattering bent cube i-beam single crystal asymmetric cut 4.965 degs
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.11→50 Å / Num. obs: 27404 / % possible obs: 98.9 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.109 / Χ2: 0.764 / Net I/av σ(I): 16.875 / Net I/σ(I): 4.5 / Num. measured all: 185587
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
2.11-2.1560.81713600.46798.6
2.15-2.195.80.72513150.47695.2
2.19-2.236.70.61513660.46799.5
2.23-2.2770.55913780.49599.9
2.27-2.3270.47413840.50499.7
2.32-2.3870.44113580.51399.5
2.38-2.446.90.35913650.52599.3
2.44-2.570.3313660.53699.4
2.5-2.586.90.29313840.57999.1
2.58-2.666.90.24113670.59798.6
2.66-2.756.60.20113530.64198.4
2.75-2.866.10.17813500.69197.8
2.86-2.997.20.14613740.773100
2.99-3.157.10.12713920.86799.9
3.15-3.357.10.11313770.976100
3.35-3.6170.0913901.09199.3
3.61-3.976.60.07413561.18197.9
3.97-4.546.60.06713621.23296.6
4.54-5.727.10.06613881.09799.9
5.72-506.70.06714191.44398.6

-
Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIXrefinement
PDB_EXTRACT3.15data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2B1V

2b1v


Resolution: 2.11→46.318 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 22.98 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2204 1891 7.25 %
Rwork0.1821 24181 -
obs0.1849 26072 93.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 141.59 Å2 / Biso mean: 47.0294 Å2 / Biso min: 12.11 Å2
Refinement stepCycle: final / Resolution: 2.11→46.318 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3808 0 48 174 4030
Biso mean--35.94 43.12 -
Num. residues----491
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0023942
X-RAY DIFFRACTIONf_angle_d0.6095339
X-RAY DIFFRACTIONf_chiral_restr0.023637
X-RAY DIFFRACTIONf_plane_restr0.003661
X-RAY DIFFRACTIONf_dihedral_angle_d13.5561440
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.1024-2.1550.25061130.23361419153278
2.155-2.21330.24491190.22861553167284
2.2133-2.27840.25611280.22681659178790
2.2784-2.35190.2731290.221695182492
2.3519-2.4360.29031450.20711703184893
2.436-2.53350.20421200.20691748186894
2.5335-2.64880.25961360.2141747188395
2.6488-2.78850.24981300.20771761189195
2.7885-2.96310.2121490.2051769191897
2.9631-3.19190.24321440.19371821196598
3.1919-3.5130.22551460.18061814196099
3.513-4.02110.19541410.15461812195397
4.0211-5.06510.18721420.14441812195498
5.0651-46.32960.20491490.17091868201799
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)
14.39271.221-0.76836.951-0.86842.98270.0680.9911.379-0.4795-0.33220.4-0.888-0.32310.10680.64630.244-0.05310.64070.1510.54891.475719.19-4.9102
22.43841.01040.20791.7494-2.76046.8480.03170.9817-0.6678-0.5063-0.7833-0.3221.32510.64320.47410.5910.13460.13190.42380.03390.356520.937-5.1845-6.7415
35.5047-1.5147-2.47195.34891.40654.44780.1590.2179-0.1323-0.02420.03530.0936-0.06920.2666-0.11910.1741-0.0346-0.01520.2257-0.00740.187521.17213.3794-0.8728
44.19720.0568-1.07334.68690.77944.4040.26490.02950.6684-0.1277-0.1383-0.1276-0.41790.0419-0.19960.1920.03310.03520.23340.02530.254614.032211.76654.7476
53.59892.1798-2.34153.4687-0.91874.0152-0.59850.5212-1.3314-0.3544-0.63370.35071.4102-0.70830.09420.4654-0.10440.1130.3748-0.18890.413711.8062-9.5576-2.817
60.9562-1.81580.63726.4442-0.54054.17980.3517-0.1078-0.2398-0.1510.2655-0.44530.86730.83950.0491.19730.15220.18850.54140.14780.859918.8759-13.96568.7636
72.0813-0.78361.22257.75720.42976.4113-0.1822-0.1698-0.81440.3322-0.02890.03860.5429-0.40160.15570.4266-0.08970.12180.28540.00070.37345.9126-7.77536.3648
87.4946-0.0507-0.67557.68550.70564.46870.11690.14080.47380.092-0.09610.0986-0.3316-0.34770.02050.26140.08720.0870.27420.00740.18864.45119.11094.6328
96.77050.9919-0.75836.26730.40194.06920.16560.31360.7629-0.7577-0.42450.3071-0.6091-0.44720.18830.37980.17670.00420.4460.03880.3352-3.987714.88063.1149
102.4281-0.36310.12393.578-0.16892.09490.01180.1371-0.39720.1017-0.10470.08150.0698-0.20150.06490.29780.00560.02390.2492-0.01810.18193.05272.471210.9842
115.6225-1.7563-2.30362.59871.01683.81250.8497-1.671-0.23350.56520.3219-0.9332-0.00810.5251-0.32510.490.0841-0.06141.03540.03160.73929.509-2.250513.7292
120.3791-0.53020.06213.1947-3.78615.6230.1776-0.9748-0.2990.60380.2212-0.4365-0.03470.8885-0.29580.3709-0.017-0.0430.53490.07480.50127.43095.95899.3701
138.10951.78434.14792.7150.90778.38130.2734-0.5923-0.70220.062-0.01180.1520.1364-1.2925-0.18580.27370.05770.04640.44810.03130.3508-9.17594.041131.786
140.7292-0.31542.43620.5267-0.69499.8624-0.123-1.25340.00240.36950.3014-1.36660.08212.277-0.29380.5327-0.0879-0.04471.1138-0.19641.052218.059513.451245.952
152.4314-0.5599-0.88813.42890.59734.5271-0.1408-0.15-0.13710.03530.0240.17520.1984-0.06540.06540.2231-0.00490.03080.22150.02580.19312.49342.34131.7212
164.95090.9875-2.56514.0242-3.52395.77530.6459-0.7898-0.05060.7192-0.3379-1.5094-2.41571.8296-1.05120.7217-0.18360.06640.7299-0.10130.552112.805617.657336.8393
173.54941.91011.24013.76010.96546.2134-0.03740.05120.2025-0.2079-0.0188-0.0961-0.9165-0.12230.04050.32610.00150.03850.2530.0140.2232.036612.229324.3321
188.20273.22341.24772.77893.78467.6869-0.83410.3553-1.1369-1.64180.20760.06451.10150.4651.13180.9519-0.07020.01250.7808-0.01610.57380.3272-10.851315.4117
194.5502-1.34710.72582.456-1.16934.2774-0.079-0.09950.0529-0.05630.00590.1135-0.0362-0.490.09860.2434-0.02070.0430.1979-0.02750.1631-1.82187.057917.9223
207.73941.8177-5.20255.3841-1.36259.0831-0.8198-0.4329-0.6752-0.56870.1794-1.27010.12111.41220.71190.54020.04380.07890.61780.20720.665215.2531-5.546132.496
217.29482.47483.36181.09191.38981.77440.1561-0.24571.30880.0261-0.1463-0.1653-0.99210.66130.08630.3803-0.08410.16270.44120.01340.807826.069518.06861.7026
224.53331.58350.15150.95690.8111.3901-0.5166-0.9635-2.33240.36390.468-0.0421.3863-0.49390.3250.7794-0.03360.05360.43420.28530.74471.0825-13.692635.5983
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 304 through 321 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 322 through 338 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 339 through 363 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 364 through 394 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 395 through 411 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 412 through 421 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 422 through 437 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 438 through 472 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 473 through 496 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 497 through 525 )A0
11X-RAY DIFFRACTION11chain 'A' and (resid 526 through 533 )A0
12X-RAY DIFFRACTION12chain 'A' and (resid 534 through 549 )A0
13X-RAY DIFFRACTION13chain 'B' and (resid 305 through 331 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 332 through 340 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 341 through 405 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 406 through 419 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 420 through 455 )B0
18X-RAY DIFFRACTION18chain 'B' and (resid 456 through 470 )B0
19X-RAY DIFFRACTION19chain 'B' and (resid 471 through 528 )B0
20X-RAY DIFFRACTION20chain 'B' and (resid 529 through 550 )B0
21X-RAY DIFFRACTION21chain 'C' and (resid 687 through 696 )C0
22X-RAY DIFFRACTION22chain 'D' and (resid 687 through 697 )D0

+
About Yorodumi

-
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

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
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

-
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

Read more