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- PDB-9dtx: Crystal structure of PRT3789 in complex with the bromodomain of h... -

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Basic information

Entry
Database: PDB / ID: 9dtx
TitleCrystal structure of PRT3789 in complex with the bromodomain of human BRG1 (SMARCA4) and pVHL:ElonginC:ElonginB
Components
  • Elongin-B
  • Elongin-C
  • Transcription activator BRG1
  • von Hippel-Lindau disease tumor suppressor
KeywordsTRANSCRIPTION / SMARCA2 / Bromodomain / Protein-ligand complex
Function / homology
Function and homology information


positive regulation of glucose mediated signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / regulation of cellular response to hypoxia / bBAF complex / neural retina development / npBAF complex / negative regulation of androgen receptor signaling pathway / nBAF complex / EGR2 and SOX10-mediated initiation of Schwann cell myelination / nucleosome array spacer activity ...positive regulation of glucose mediated signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / regulation of cellular response to hypoxia / bBAF complex / neural retina development / npBAF complex / negative regulation of androgen receptor signaling pathway / nBAF complex / EGR2 and SOX10-mediated initiation of Schwann cell myelination / nucleosome array spacer activity / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / GBAF complex / regulation of G0 to G1 transition / Tat protein binding / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / RNA polymerase I preinitiation complex assembly / RSC-type complex / ATP-dependent chromatin remodeler activity / regulation of nucleotide-excision repair / host-mediated activation of viral transcription / Replication of the SARS-CoV-1 genome / nucleosome disassembly / VCB complex / Cul5-RING ubiquitin ligase complex / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Cul2-RING ubiquitin ligase complex / positive regulation of T cell differentiation / intracellular membraneless organelle / nuclear androgen receptor binding / positive regulation of double-strand break repair / SUMOylation of ubiquitinylation proteins / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of G1/S transition of mitotic cell cycle / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / negative regulation of transcription elongation by RNA polymerase II / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / positive regulation of signal transduction by p53 class mediator / negative regulation of cell differentiation / positive regulation of Wnt signaling pathway / ATP-dependent activity, acting on DNA / positive regulation of myoblast differentiation / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV elongation complex in the absence of HIV Tat / Chromatin modifying enzymes / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / DNA polymerase binding / RNA Polymerase II Pre-transcription Events / Interleukin-7 signaling / negative regulation of autophagy / transcription initiation-coupled chromatin remodeling / protein serine/threonine kinase binding / transcription corepressor binding / transcription coregulator binding / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / helicase activity / Formation of the beta-catenin:TCF transactivating complex / negative regulation of cell growth / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / kinetochore / positive regulation of miRNA transcription / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Regulation of expression of SLITs and ROBOs / RMTs methylate histone arginines / nuclear matrix / fibrillar center / cell morphogenesis / ubiquitin-protein transferase activity / p53 binding / transcription corepressor activity / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / nervous system development / positive regulation of cold-induced thermogenesis / Neddylation / microtubule cytoskeleton / regulation of gene expression / Replication of the SARS-CoV-2 genome / protein-containing complex assembly / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity
Similarity search - Function
SWI/SNF complex subunit BRG1 / BRK domain / BRK domain / BRK domain superfamily / domain in transcription and CHROMO domain helicases / Glutamine-Leucine-Glutamine, QLQ / QLQ / QLQ domain profile. / QLQ / Snf2-ATP coupling, chromatin remodelling complex ...SWI/SNF complex subunit BRG1 / BRK domain / BRK domain / BRK domain superfamily / domain in transcription and CHROMO domain helicases / Glutamine-Leucine-Glutamine, QLQ / QLQ / QLQ domain profile. / QLQ / Snf2-ATP coupling, chromatin remodelling complex / Snf2, ATP coupling domain / Snf2-ATP coupling, chromatin remodelling complex / domain in helicases and associated with SANT domains / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / Elongin-C / Elongin B / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / SKP1/BTB/POZ domain superfamily / Helicase conserved C-terminal domain / Bromodomain, conserved site / Bromodomain signature. / Bromodomain / bromo domain / Bromodomain / Bromodomain (BrD) profile. / Bromodomain-like superfamily / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Ubiquitin-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
: / von Hippel-Lindau disease tumor suppressor / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.11 Å
AuthorsWang, M. / Dou, Y. / Xu, C.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cancer Res. / Year: 2025
Title: PRT3789 is a First-in-Human SMARCA2-Selective Degrader that Induces Synthetic Lethality in SMARCA4-Mutated Cancers.
Authors: Hulse, M. / Wang, M. / Xu, C. / Carter, J. / Agarwal, A. / Lu, L. / Pitis, P. / Bhagwat, N. / Rager, J. / Kurian, J. / Basch, C. / Sivakumar, M. / Burtell, J. / Mondal, A. / Grego, A. / ...Authors: Hulse, M. / Wang, M. / Xu, C. / Carter, J. / Agarwal, A. / Lu, L. / Pitis, P. / Bhagwat, N. / Rager, J. / Kurian, J. / Basch, C. / Sivakumar, M. / Burtell, J. / Mondal, A. / Grego, A. / Moore, A. / Bachner, C. / Vykuntam, K. / Reichelderfer, A. / Park, J. / Cote, J. / Cowart, M. / Osinubi, O.P. / Bigot, L. / Da Silva, A. / Nobre, C. / Meteau, M. / Soares, M. / Tang, H.Y. / Bersch, K. / Dai, C. / Cao, G. / Shen, B. / Emm, T. / Ruepp, S. / Xavier, J. / Tankersley, C. / Heiser, D. / Lee, S.H. / Geeganage, S. / Ruggeri, B. / Lin, H. / Novotny, W. / Huang, J. / Vaddi, K. / Combs, A. / Scherle, P. / Ito, K.
History
DepositionOct 2, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 1, 2025Provider: repository / Type: Initial release
Revision 1.1Oct 8, 2025Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Elongin-B
B: Elongin-C
C: von Hippel-Lindau disease tumor suppressor
D: Transcription activator BRG1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,4998
Polymers57,4194
Non-polymers1,0814
Water5,873326
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)75.190, 58.880, 131.080
Angle α, β, γ (deg.)90.000, 90.330, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein , 4 types, 4 molecules ABCD

#1: Protein Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 11748.406 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q15370
#2: Protein Elongin-C / EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / ...EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / Transcription elongation factor B polypeptide 1


Mass: 10843.420 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q15369
#3: Protein von Hippel-Lindau disease tumor suppressor / Protein G7 / pVHL


Mass: 18615.215 Da / Num. of mol.: 1 / Fragment: UNP residues 54-213
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VHL
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P40337
#4: Protein Transcription activator BRG1 / ATP-dependent helicase SMARCA4 / BRG1-associated factor 190A / BAF190A / Mitotic growth and ...ATP-dependent helicase SMARCA4 / BRG1-associated factor 190A / BAF190A / Mitotic growth and transcription activator / Protein BRG-1 / Protein brahma homolog 1 / SNF2-beta / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4


Mass: 16211.580 Da / Num. of mol.: 1 / Fragment: UNP residues 1448-1569
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA4, BAF190A, BRG1, SNF2B, SNF2L4
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement

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Non-polymers , 5 types, 330 molecules

#5: Chemical ChemComp-A1BB4 / (4R)-4-hydroxy-1-[(2R)-2-(3-{[(2S)-1-{(3R)-3-[(2M,6aS,11S)-2-(2-hydroxyphenyl)-5,6,6a,7,9,10-hexahydro-8H-pyrazino[1',2':4,5]pyrazino[2,3-c]pyridazin-8-yl]pyrrolidin-1-yl}propan-2-yl]oxy}-1,2-oxazol-5-yl)-3-methylbutanoyl]-N-{(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl}-L-prolinamide


Mass: 891.092 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C47H58N10O6S
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 326 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationN

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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: 2.53 Å3/Da / Density % sol: 51.32 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.1 M Bis-Tris propane, pH 8.5, 0.2 M potassium thiocyanate, 20% w/v PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Sep 23, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.11→46.4 Å / Num. obs: 32922 / % possible obs: 99.2 % / Redundancy: 6.1 % / CC1/2: 0.999 / Rmerge(I) obs: 0.06 / Rpim(I) all: 0.026 / Rrim(I) all: 0.065 / Net I/σ(I): 16.8
Reflection shellResolution: 2.11→2.17 Å / Rmerge(I) obs: 0.409 / Mean I/σ(I) obs: 2.9 / Num. unique obs: 2502 / CC1/2: 0.905 / Rpim(I) all: 0.238 / Rrim(I) all: 0.477

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
PDB_EXTRACT3.28data extraction
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.11→46.4 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.942 / SU B: 10.705 / SU ML: 0.149 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.214 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2319 1513 4.6 %RANDOM
Rwork0.1853 ---
obs0.1875 31408 99.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 107.37 Å2 / Biso mean: 44.12 Å2 / Biso min: 26.86 Å2
Baniso -1Baniso -2Baniso -3
1-0.16 Å2-0 Å22.23 Å2
2--2.23 Å20 Å2
3----2.42 Å2
Refinement stepCycle: final / Resolution: 2.11→46.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3741 0 75 326 4142
Biso mean--46.25 48.65 -
Num. residues----462
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0133963
X-RAY DIFFRACTIONr_bond_other_d0.0020.0153838
X-RAY DIFFRACTIONr_angle_refined_deg1.5441.6835375
X-RAY DIFFRACTIONr_angle_other_deg1.2751.6038876
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0785471
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.54921.737213
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.77415715
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.5611532
X-RAY DIFFRACTIONr_chiral_restr0.0670.2513
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.024377
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02885
X-RAY DIFFRACTIONr_mcbond_it1.6942.9891878
X-RAY DIFFRACTIONr_mcbond_other1.6932.9861877
X-RAY DIFFRACTIONr_mcangle_it2.7514.4612351
LS refinement shellResolution: 2.11→2.165 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.301 119 -
Rwork0.257 2111 -
all-2230 -
obs--90.91 %
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)
10.23020.1930.79650.23440.88593.4259-0.0533-0.16910.0262-0.0723-0.01420.0246-0.2024-0.05540.06750.1014-0.10720.02590.5771-0.04940.104526.419810.351958.6179
20.058-0.0052-0.30211.3490.80452.40680.028-0.02850.0356-0.04530.0818-0.1285-0.0551-0.1532-0.10970.0342-0.04630.00850.3179-0.14840.101920.385512.643461.5132
32.4843-0.0206-1.85192.49470.20473.3057-0.0651-0.51340.17030.17350.16550.18620.09260.1217-0.10040.023-0.02130.02140.3498-0.08420.04422.152310.91570.145
41.1041-0.1354-1.72371.9039-0.05942.81580.0122-0.17980.0631-0.0180.0539-0.09240.06280.1304-0.06610.0563-0.0751-0.02460.335-0.08340.073827.21449.932663.4206
52.3087-1.8232-3.95222.11482.93276.8738-0.1406-0.1196-0.07180.1663-0.0297-0.16130.29780.16220.17030.1063-0.0434-0.04410.23290.05260.084127.0094-5.092860.187
65.65468.2563-8.911812.0701-13.100314.71710.2697-0.3389-0.12770.3081-0.4729-0.1985-0.01340.6440.20320.3075-0.00730.05830.1696-0.03440.217440.1664-14.313240.6021
70.2667-0.4621-0.48117.1746-0.43221.20540.06760.01780.0017-0.0336-0.05080.1159-0.0565-0.1439-0.01680.13-0.0505-0.02250.217-0.03670.134814.15195.551850.7589
85.21243.5742.24928.05870.20031.37980.0442-0.4099-0.23920.01910.1642-0.0516-0.0233-0.3106-0.20850.1282-0.08570.02250.1970.03360.109919.704-6.634852.9244
91.4359-0.3903-2.51375.13691.1724.4890.13770.1130.0387-0.4528-0.12270.1673-0.3145-0.3012-0.0150.09160.0052-0.05940.2777-0.0730.093616.24016.756244.7233
1012.18743.16974.13780.83381.07071.41950.0615-0.60520.0738-0.052-0.14870.02650.0443-0.21010.08720.44710.0825-0.07590.2410.01760.25316.72733.130143.4687
114.2021.0648-1.09812.26663.20876.40230.40620.27150.16340.2665-0.1926-0.07790.2733-0.6335-0.21360.2544-0.14530.0050.1670.00970.072316.2814-5.047145.8329
121.35141.2903-0.41671.9291-1.14621.23090.0262-0.14190.0641-0.0534-0.02440.05420.0241-0.0293-0.00180.091-0.0357-0.01350.1202-0.02730.117727.49176.082546.1255
133.13020.0484-0.43294.5448-1.82250.79020.0226-0.24430.1577-0.18-0.02350.01080.05260.06610.00090.1545-0.0792-0.0380.1272-0.0040.119835.319611.850842.8076
145.0738-2.86713.1542.1802-0.96223.7133-0.2128-0.2040.02320.03890.05790.01820.199-0.19030.15480.3284-0.040.0780.1029-0.01310.128528.3745-4.095740.2722
156.73821.25871.3452.98940.7673.2822-0.10840.7574-0.131-0.20770.23140.51790.0673-0.0618-0.1230.2776-0.0321-0.02290.19540.02840.125545.297823.020512.7511
160.6913-1.04150.20257.3277-5.07416.9462-0.16560.0285-0.08460.2505-0.1544-0.5663-0.49810.21170.320.2102-0.12080.0330.1242-0.01260.156951.451924.821929.8255
170.95430.96090.86980.97910.83730.9429-0.1090.1402-0.0983-0.080.1401-0.1047-0.29040.2375-0.03110.2308-0.1249-0.01830.1952-0.01440.0847.893213.611725.3192
181.03420.0273-1.511.8309-0.13853.4488-0.0079-0.16320.04370.04860.1541-0.2195-0.21740.5042-0.14620.1279-0.134-0.04160.2042-0.00520.083754.230718.965830.8611
190.08970.4658-0.38435.3583-2.06991.65410.0054-0.05220.0111-0.10870.06010.2404-0.05350.2077-0.06560.1583-0.1077-0.01370.1280.00320.124245.342518.772523.6659
201.2872-0.1845-0.40524.59030.55550.1887-0.05870.074-0.0002-0.10930.02630.1091-0.0242-0.00270.03240.1486-0.0894-0.06840.1194-0.01160.09542.456218.827628.2772
211.72320.711-0.27810.48760.37261.3308-0.1193-0.06420.0337-0.0074-0.00750.07910.07060.04260.12690.1438-0.0339-0.00860.07970.00890.104239.67945.686833.9335
223.336-0.2252-3.89343.25391.70616.2443-0.3020.6379-0.32270.30720.0855-0.0030.454-0.35030.21640.1726-0.08550.02260.2428-0.11740.152730.4146-9.435730.0445
234.3126-1.1091-0.20710.52690.80742.7049-0.02840.13360.5439-0.0948-0.0939-0.1601-0.1604-0.33010.12230.1875-0.0550.03770.1654-0.06340.260735.409512.061719.5918
242.0037-2.3567-0.82994.2811-2.3677.7653-0.1469-0.20250.18760.35790.0535-0.3117-0.33930.44610.09340.1586-0.0057-0.00710.2010.02620.213874.293626.6591-17.6607
253.84751.0241-4.59211.1897-1.03165.55170.19690.16780.18510.1434-0.04650.1029-0.2096-0.1932-0.15030.083-0.03830.01110.141-0.00370.138154.073226.3626-12.4316
267.3029-0.83422.57270.1443-0.73798.30810.1608-0.24750.11740.06410.0814-0.0319-0.12120.0943-0.24220.3459-0.0167-0.09070.1805-0.08420.080562.175722.24965.3926
272.1174-2.28750.46857.9323-0.68660.12310.0454-0.17340.06090.0593-0.0365-0.04310.02550.0088-0.00890.1658-0.0575-0.09620.21610.02630.074866.26913.29293.0748
281.59351.4158-2.01641.5068-1.70943.39460.1643-0.0818-0.11020.1152-0.1947-0.1330.06550.10970.03040.1743-0.0225-0.06850.11070.01480.115462.728118.4749-8.1788
290.60740.20250.45960.9791-1.65734.27750.08520.05910.06510.03050.0510.15460.0896-0.2225-0.13620.1412-0.0862-0.03270.1766-0.00280.100551.447518.2189-12.472
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 9
2X-RAY DIFFRACTION2A10 - 35
3X-RAY DIFFRACTION3A36 - 56
4X-RAY DIFFRACTION4A57 - 84
5X-RAY DIFFRACTION5A85 - 99
6X-RAY DIFFRACTION6A100 - 104
7X-RAY DIFFRACTION7B17 - 22
8X-RAY DIFFRACTION8B23 - 27
9X-RAY DIFFRACTION9B28 - 46
10X-RAY DIFFRACTION10B47 - 58
11X-RAY DIFFRACTION11B59 - 66
12X-RAY DIFFRACTION12B67 - 83
13X-RAY DIFFRACTION13B84 - 96
14X-RAY DIFFRACTION14B97 - 112
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